Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins. Required for spore germination.
Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
Tetramer of two alpha and two beta subunits.
Expressed during exponential growth and shut down at the entry into stationary phase.
Homodimer. Interacts with YycH and YycI.
Member of the two-component regulatory system WalK/WalR involved in the regulation of the ftsAZ operon, the yocH and ykvT, cwlO, lytE, ydjM, yjeA, yoeB genes and the tagAB and tagDEF operons. Phosphorylates WalR.
The imidazole derivatives NH125, NH126 and NH127 inhibited the incorporation of phosphate from ATP at 50 ug/ml. The zerumbone derivative NH0891 inhibited WalK.
Belongs to the 4-toluene sulfonate uptake permease (TSUP) (TC 2.A.102) family.
Cells lacking this gene have an unchanged spontaneous mutation frequency, even in triple mutT/yjhB/yvcI disruptions.
Probably mediates the hydrolysis of some nucleoside diphosphate derivatives.
Belongs to the polypeptide deformylase family.
Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
Belongs to the AB hydrolase superfamily.
Induced by entry into stationary phase, but not by carbon and energy starvation.
Positive regulator required for energy stress activation of the sigma-B transcription factor. Could be required for RsbP phosphatase activity.
Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
Catalyzes the polymerization of lipoteichoic acid (LTA) polyglycerol phosphate, a reaction that presumably uses phosphatidylglycerol (PG) as substrate.
Restores staphylococcal growth after ltaS depletion.
Belongs to the SOS response-associated peptidase family.
Glu-106 is involved in sensing abasic sites in single-stranded DNA (ssDNA). His-163 stabilizes the abasic sites by forming a hydrogen bond with the O4' hydroxyl group.
Sensor of abasic sites in single-stranded DNA (ssDNA) required to preserve genome integrity by promoting error-free repair of abasic sites. Recognizes and binds abasic sites in ssDNA at replication forks and chemically modifies the lesion by forming a covalent cross-link with DNA: forms a stable thiazolidine linkage between a ring-opened abasic site and the alpha-amino and sulfhydryl substituents of its N-terminal catalytic cysteine residue (By similarity). May act as a protease: mediates autocatalytic processing of its N-terminal methionine in order to expose the catalytic cysteine (By similarity).
Belongs to the extradiol ring-cleavage dioxygenase family.
Putative ring-cleavage dioxygenase that may contribute to the degradation of aromatic compounds.
Repressed by MhqR. Strongly induced by stress due to exposure to 2-methylhydroquinone (2-MHQ) and less strongly induced after diamide or catechol stress. Not induced by oxidative stress due to hydrogen peroxide or methylglyoxal.
Belongs to the acyl-CoA dehydrogenase family.
Induced by methionine. Repressed by sulfate via the cysteine metabolism repressor YrzC/CymR.
Belongs to the phosphosulfolactate synthase family.
Catalyzes the addition of sulfite to phosphoenolpyruvate (PEP) to yield (2R)-phospho-3-sulfolactate (PSL) (By similarity). Is probably involved in the biosynthesis of L-sulfolactate, which is a major constituent of sporulating cells and mature spores.
Cells lacking this gene have no visible phenotype is response to salt, ethanol or energy stress. However cells with multiple disruption (RsbRA, RsbRB and RsbRD) have an increased basal level of sigma-B, indicating this protein is a negative regulator of sigma-B.
Negative regulator of sigma-B activity. Non-phosphorylated RsbS binds to RsbT, preventing its association with RsbU. Requires any one of RsbRA, RsbRB, RsbRC or RsbRD to sequester RsbT. When RsbS and the RsbR paralog(s) are phosphorylated, they release RsbT, which can then bind and activate RsbU.
One of 4 functionally non-identical RsbR paralogs, it functions in the environmental signaling branch of the general stress response.
Probably present in the stressosome with RsbRA, RsbRB, RsbRC and RsbS.
Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. Is also able to use octanoate as substrate.
Cells lacking this gene grow normally in minimal medium in the absence of supplements and have a wild-type pattern of lipoylated proteins. However, a double mutant strain lacking both lplJ and lipM is unable to grow in minimal medium either in the presence or in the absence of lipoic acid, indicating that LplJ is the sole B.subtilis lipoic acid salvage enzyme.
In the transfer reaction, the free carboxyl group of lipoic acid is attached via an amide linkage to the epsilon-amino group of a specific lysine residue of lipoyl domains of lipoate-dependent enzymes.
Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family.
Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis.
Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 2 subfamily.
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Belongs to the methyl-accepting chemotaxis (MCP) protein family.
Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. All amino acids serve as attractants in B.subtilis, they appear to cause an increase in the turnover methyl groups, leading to methylation of an unidentified acceptor, while repellents have been shown to cause a decrease in methyl group turnover. The methyl groups are added by a methyltransferase and removed by a methylesterase. McpA is required for taxis towards glucose and alpha-methylglucoside.
Deamidated by CheD on Gln-593 and Gln-594, producing glutamate residues. The glutamate residues are then methylated. Other additional sites are deamidated and methylated as well.
Belongs to the ABC-2 integral membrane protein family.
Induced in response to linearmycins and other polyenes via the two-component regulatory system LnrJ/LnrK.
Required for resistance to linearmycins, a family of antibiotic-specialized metabolites produced by some streptomycetes (PubMed:26647299, PubMed:28461449). Part of the ABC transporter complex LnrLMN that probably facilitates linearmycin removal from the membrane. Responsible for the translocation of the substrate across the membrane (PubMed:28461449). Also mediates KinC-dependent biofilm morphology (PubMed:28461449).
The complex is composed of two ATP-binding proteins (LnrL) and two transmembrane proteins (LnrM and LnrN).
Disruption of the gene results in the enhancement of aprE expression.
Involved in the regulation of expression of DegU-controlled genes (PubMed:12950930). Inhibits the binding of DegU to the promoter regions of aprE, coding for an extracellular alkaline protease, and comK, a master regulator for development of genetic competence (PubMed:12950930). RapG does not stimulate dephosphorylation of DegU-P (PubMed:12950930).
Part of the rapG-phrG operon (PubMed:12950930). Expression shows a slight decrease in stationary phase (PubMed:12950930). Repressed by RghR (PubMed:16553878).
Belongs to the ATP-dependent AMP-binding enzyme family.
This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Glu and Orn as part of the biosynthesis of the lipopeptide antibiotic lipastatin. The Orn residue is further epimerized to the D-isomer form. The activation sites for these amino acids consist of individual domains.
The PTS EIIA type-2 domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the PTS EIIB type-2 domain.
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II CmtAB PTS system is involved in D-mannitol transport.
Negatively regulates SacY activity by catalyzing its phosphorylation on 'His-99'.
The EIIB domain is phosphorylated by phospho-EIIA on a cysteinyl or histidyl residue, depending on the transported sugar. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the EIIC domain.
The EIIC domain forms the PTS system translocation channel and contains the specific substrate-binding site.
The PTS EIIB type-2 domain may serve a regulatory function, through its phosphorylation activity.
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system may be involved in sucrose transport.
Also displays a weak uracil phosphoribosyltransferase activity which is not physiologically significant.
Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrR subfamily.
Homodimer and homohexamer; in equilibrium.
Mutagenesis studies identified four amino acid residues that seem to be involved directly in binding of the protein to pyr mRNA: Thr-18, His-22, Arg-141 and Arg-146. Arg-27 and Lys-152 were also likely to be involved in RNA-binding, but mutations may have altered their subunit-subunit interactions. Arg-19 was implicated in pyr regulation, but a specific role in RNA-binding could not be demonstrated.
Regulates transcriptional attenuation of the pyrimidine nucleotide (pyr) operon by binding in a uridine-dependent manner to specific sites on pyr mRNA. This disrupts an antiterminator hairpin in the RNA and favors formation of a downstream transcription terminator, leading to a reduced expression of downstream genes.
UMP and UTP increase the affinity of PyrR for RNA.
Inhibits the SpoIVB zymogen from undergoing autocatalytic activation by an unknown mechanism, and in this way plays a role in the sigma-K checkpoint of sporulation.
Phosphorylates B6 vitamers; functions in a salvage pathway. Uses pyridoxal, pyridoxine, and pyridoxamine as substrates. Can also use hydroxymethylpyrimidine (HMP) as substrate.
Was originally annotated in the complete genome as thiD.
Cells lacking this gene show little or no difference in growth under copper deprivation, whereas possessing enhanced growth under copper excess conditions. Possesses a high intracellular content of copper.
May act as a negative transcriptional regulator of ycnJ in the presence of copper. May use copper as a corepressor.
Significantly induced under copper-limiting conditions.
Was initially thought to be two separate ORFs named yitO and yitN.
Catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein ThiS.
Homodimer, probably forms a complex with cognate antitoxin YutD.
Probable toxic component of a putative type VII toxin-antitoxin (TA) system, probably an RNase. Probably neutralized by cognate antitoxin YutD.
Belongs to the pyrroline-5-carboxylate reductase family.
Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
The proG proH proI triple mutant is auxotrophic for proline.
Belongs to the dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family.
Catalyzes the proton-dependent, binding-protein-independent transport of glutamate and aspartate.
Glutamate uptake is inhibited by beta-hydroxyaspartate and cysteic acid.
Belongs to the binding-protein-dependent transport system permease family.
Involved in galactan degradation (PubMed:27501980). Part of the ABC transporter complex GanPQS involved in the uptake of galactooligosaccharides (PubMed:27501980, PubMed:29240795). Responsible for the translocation of the substrate across the membrane (Probable).
Repressed by the transcriptional regulator GanR and induced by galactobiose. Also repressed by glucose.
The complex is composed of two ATP-binding proteins (MsmX), two transmembrane proteins (GanP and GanQ) and a solute-binding protein (GanS).
Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
Belongs to the folylpolyglutamate synthase family.
Functions in two distinct reactions of the de novo folate biosynthetic pathway. Catalyzes the addition of a glutamate residue to dihydropteroate (7,8-dihydropteroate or H2Pte) to form dihydrofolate (7,8-dihydrofolate monoglutamate or H2Pte-Glu). Also catalyzes successive additions of L-glutamate to tetrahydrofolate, leading to folylpolyglutamate derivatives.
Belongs to the FtsK/SpoIIIE/SftA family.
Cells lacking this gene show a chromosome translocation defect and aberrant compartmentalization of both sigma-F and sigma-E, and fail to complete membrane fusion at the end of engulfment.
Consists of an N-terminal domain, followed by a linker domain, and a C-terminal domain, which forms the translocation motor involved in chromosome segregation. The C-terminal domain can be further subdivided into alpha, beta and gamma subdomains. Specific interactions between the gamma subdomain and specific SpoIIIE recognition sequences (SRS) regulate the compartment-specific activation of a mother-cell SpoIIIE complex. Interactions with nonpermissive SRS in the forespore lead to inactivation of the complex.
Homohexamer. Forms a ring that surrounds DNA. Assembles into complexes that could contain two hexamers.
Plays an essential role during sporulation. Required for the translocation of the chromosomal DNA from mother cell into the forespore during polar septation, for the final steps of compartmentalization in the presence of trapped DNA, and for the final steps of engulfment. The N-terminus mediates localization to the division septum and is required for both septal membrane fusion and engulfment membrane fusion. May form DNA-conducting channels across the two lipid bilayers of the septum after cell division. The C-terminus functions as a DNA motor that exports DNA in an ATP-dependent manner from mother cell into the forespore. DNA-binding proteins are stripped off the chromosome during translocation, which may play a key role in reprogramming developmental gene expression in the forespore. The two arms of the chromosome are simultaneously pumped into the forespore, which suggests that the septum contains at least two channels, one for each arm. Required for separation of chromosome termini. Also required for optimal chromosome partitioning in vegetative cells, by actively moving chromosomal DNA trapped within the division septum into the daughter cells.
Belongs to the acetyltransferase family.
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Disruption of this gene interrupts lipoate-dependent reactions, which strongly inhibits growth in minimal medium, impairing the generation of branched-chain fatty acids and leading to accumulation of copious amounts of straight-chain saturated fatty acids in B.subtilis membranes.
A double ring-shaped homohexamer of ClpQ is capped on each side by a ring-shaped ClpY homohexamer. The assembly of the ClpQ/ClpY complex is dependent on binding of ATP (By similarity).
A double ring-shaped homohexamer of HslV is capped on each side by a ring-shaped HslU homohexamer. The assembly of the HslU/HslV complex is dependent on binding of ATP.
ATPase activity is much induced upon complex formation with ClpQ.
ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity.
ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
Belongs to the ClpX chaperone family. HslU subfamily.
By phosphate starvation, via the PhoP/PhoR two-component regulatory system.
Belongs to the ABC transporter superfamily.
Part of the ABC transporter complex GlnHMPQ involved in glutamine transport. Probably responsible for energy coupling to the transport system (By similarity).
Positively regulated by TnrA under nitrogen-limited conditions.
The complex is composed of two ATP-binding proteins (GlnQ), two transmembrane proteins (GlnM and GlnP) and a solute-binding protein (GlnH).
A monocistronic operon. Induced by L-alanine in minimal media. Constitutively expressed in rich medium, declines during sporulation. Induced early during sporulation on minimal medium by L-alanine. Affects its own expression (PubMed:8226620). Transcription activated by AdeR (PubMed:22797752).
Catalyzes the reversible oxidative deamination of L-alanine to pyruvate. Oxidative deamination proceeds through a sequential, ordered ternary-binary mechanism, where NAD(+) binds first followed by L-alanine; the products are released in the order ammonia, pyruvate and NADH (PubMed:6794611, PubMed:6794612) (Probable). Disruption blocks sporulation probably in stage V; 20-30% sporulation can be restored if the media is supplemented with pyruvate, suggesting lack of pyruvate blocks sporulation. Thus it is a key factor in the assimilation of L-alanine as an energy source via the tricarboxylic acid cycle during sporulation (PubMed:8226620).
Homohexamer. Trimer of dimer (By similarity).
Strain cannot grow on L-alanine as a sole carbon source. Disruption of ald causes a sporulation defect, most likely in stage V.
Belongs to the 'phage' integrase family.
Putative integrase that is involved in the insertion of the integrative and conjugative element ICEBs1. Required for the excision of ICEBs1 from the donor cell genome and subsequent integration in the recipient cell genome. Appears not to be transferred through the mating pore. Integration of ICEBs1 involves an attachment site in the chromosome, attB, and a site in the circular form of ICEBs1, attICEBs1.
Belongs to the bacterial solute-binding protein 5 family.
Interacts with FloT in detergent-resistant membranes (DRM) (PubMed:23651456). Colocalizes rarely with FloT membrane assemblies (PubMed:27362352).
This protein is a component of the oligopeptide permease, a binding protein-dependent transport system, It binds peptides up to five amino acids long with high affinity. Also required for sporulation and competence.
Belongs to the short-chain dehydrogenases/reductases (SDR) family.
Belongs to the methylmalonyl-CoA epimerase family.
Belongs to the major facilitator superfamily.
Autophosphorylated in vitro, which inhibits ATPase activity. Dephosphorylated by YwqE in vitro.
May be involved in the regulation of capsular polysaccharide biosynthesis. Autophosphorylates in vitro. Phosphorylates and activates in vitro two UDP-glucose dehydrogenases, YwqF and TuaD, as well as the DNA-binding proteins Ssb and SsbB.
Belongs to the antibiotic biosynthesis monooxygenase family.
Catalyzes the oxidative degradation of the heme macrocyclic porphyrin ring in the presence of a suitable electron donor such as ascorbate or NADPH--cytochrome P450 reductase, with subsequent release of free iron.
Neither hmoB single mutant nor the hmoA hmoB double mutant display robust and reproducible phenotypes relative to the wild-type.
Belongs to the universal ribosomal protein uL30 family.
Expressed in the mother cell during sporulation.
Expression is regulated by the sporulation transcription factor sigma E.
Inactivation of the gene does not affect sporulation, but a ylmC/ymxH double mutant shows a 100-fold reduction in the efficiency of sporulation.
Belongs to the polysaccharide synthase family.
Belongs to the 2-oxoacid dehydrogenase family.
E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
Forms a 24-polypeptide structural core with octahedral symmetry. Part of the 2-oxoglutarate dehydrogenase (OGDH) complex composed of E1 (2-oxoglutarate dehydrogenase), E2 (dihydrolipoamide succinyltransferase) and E3 (dihydrolipoamide dehydrogenase); the complex contains multiple copies of the three enzymatic components (E1, E2 and E3).
Involved in the production of the bacteriocin subtilosin.
Transcription is highly induced by oxygen limitation and is under dual and independent control of Spo0A-AbrB and ResDE.
Belongs to the isochorismate synthase family.
Belongs to the CDP-glycerol glycerophosphotransferase family.
Positively regulated by WalR. Mainly expressed during exponential growth and rapidly shut off as cells enter the stationary phase.
Responsible for the polymerization of the main chain of the major teichoic acid by sequential transfer of glycerol phosphate units from CDP-glycerol to the disaccharide linkage unit. Synthesizes polymers of approximately 35 glycerol phosphate units in length.
Transcribed under partial control of SigM ECF sigma factor (PubMed:17434969).
Catalyzes the dehydration of galactarate to form 5-dehydro-4-deoxy-D-glucarate (5-KDG).
Belongs to the glycosyl hydrolase 32 family.
Catalyzes the degradation of levan mainly into levanbiose (difructose). Is not active on sucrose.
Belongs to the D-lyxose ketol-isomerase family.
Sugar isomerase that catalyzes the reversible isomerization of D-lyxose to D-xylulose.
Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate (PubMed:28830929). In addition, counteracts the inhibitory action of PxpB (KipI) on sporulation, by binding to PxpB and preventing its function as an inhibitor of kinase A (PubMed:9334321).
Disruption of the gene decreases sporulation (PubMed:9334321). Deletion mutant grows less well than wild type on minimal medium with ammonium as nitrogen source and cannot grow on 5-oxoproline. Mutant lacks 5-oxoprolinase activity and accumulates 5-oxo-L-proline (PubMed:28830929).
Forms a complex composed of PxpA, PxpB and PxpC (PubMed:28830929). Interacts with PxpB (PubMed:9334321, PubMed:21050859, PubMed:28830929).
Induced by glucose when readily available sources of nitrogen, such as ammonia or glutamine, are scarce. Transcriptionally activated by TnrA and repressed by KipR.
Was originally (PubMed:8574415, PubMed:8969502) thought to be a longer ORF that encodes what is now known to be pxpB (kipI) and pxpC (kipA).
A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-CTCGAG-3'; the cleavage site is unknown.
BsuMI restriction activity requires YdiR, YdiS and YdjA.
Constitutively expressed during exponential growth. Encoded in an operon with ydiR and ydjA.
Not essential; its disruption results in increased transformation by plasmid DNA carrying multiple BsuMI target sequences (PubMed:11751814). Triple deletion ydiO-ydiP-ydiS leads to loss of susceptibility to MspJI, which only digests C-methylated DNA (PubMed:32324221).
An anti-sigma factor for sporulation specific sigma-F factor, by antagonizing sigma-F it allows the switch to sigma-G factor and progression to the late sporulation development stages (PubMed:21037003). Might stabilize or process Holliday junction intermediates, although this may be due to polar effects on the downstream mfd gene (PubMed:15317759).
Cells missing this gene prolong the activity of sigma-F factor and do not fully induce the activity of sigma-G factor; sporulation efficiency is reduced 50-fold with most spores arresting in the engulfment stage (III) (PubMed:21037003). About 10-fold increased sensitivity to DNA damaging agents, 60% reduced chromosomal DNA transformation; plasmid transformation is unaffected. Partially suppresses DNA damaging agent sensitivity of recU deletions (PubMed:11810266). Partially suppresses DNA damaging agent sensitivity of recU deletions (PubMed:11810266). Partially suppresses DNA repair and chromosome segregation defects in ruvA and recG mutants cells, but not in recD or recU mutant cells (PubMed:15317759).
Diffusely expressed in the forespore throughout spore development.
Induced at 2 hours after sporulation onset as part of the sigma-F regulon, followed by further induction after 3 hours as part of the sigma-G regulon; its concentration rises throughout sporulation (at protein level) (PubMed:21037003).
Recombination phenotypes may be due to polar effects on the downstream gene mfd rather than due to loss of the anti-sigma factor (PubMed:21037003).
Involved in the reduction of extracellular and cell-associated protease levels, as well as in the reduced levels of alpha-amylase, levansucrase, alkaline phosphatase and sporulation inhibition, when present in high copy number.
Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. BioF subfamily.
Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
Negatively regulated by TnrA under nitrogen-limited conditions.
Activity is strongly inhibited by Cu(2+) and Fe(3+).
Belongs to the GTP cyclohydrolase I family. QueF type 1 subfamily.
Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1), a late step in the queuosine pathway.
Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
Crystallographic structure revealed that QueF enzyme forms an asymmetric tunnel-fold homodecamer (PubMed:22787148) and not a homododecamer as originally proposed (PubMed:15767583).
Forms an asymmetric tunnel-fold homodecamer of two head-to-head facing pentamers, harboring 10 active sites at the intersubunit interfaces.
Belongs to the aldo/keto reductase family.
Belongs to the 'phage' integrase family. XerD subfamily.
Forms a cyclic heterotetrameric complex composed of two molecules of XerC and two molecules of XerD.
Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC-XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids.
Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide.
Elevated levels of expression during entry into the stationary phase of the growth cycle.
Insertion mutant shows increased sensitivity to H(2)0(2), reduced catalase expression and an absence of induced protection of the cell.
Accelerated cannibalism by skf- cells is seen on solid media but not in liquid media.
By Spo0A (PubMed:12817086) and PhoP (PubMed:16816204), during nutrient starvation, especially phosphate starvation. Repressed by AbrB during normal growth when nutrients are plentiful, in association with the transcriptional repressor Abh.
Produces a 26-residue extracellular sporulation filling factor (SKF) that induces the lysis of other B.subtilis cells that have not entered the sporulation pathway, providing a source of nutrients to support sporulation, and at the same time delaying commitment to the energetically expensive and irreversible onset of sporulation (PubMed:12817086, PubMed:20805502). Can also inhibit growth of other bacteria at high concentrations (PubMed:11851812). Addition of SKF to solid cultures induces killing, but it is much less effective than SDP (AC O34344) (PubMed:20805502). Has a role in protecting the secreted lipase LipA against proteolysis, either by modulating its folding or by acting as a protease inhibitor (PubMed:15812018).
This is a cyclic peptide (PubMed:20805502, PubMed:23282011). The first step in SKF maturation is probably thioether bond formation (PubMed:23282011).
When the skfA-skfB-skfC-skfE-skfF-skfG-skfH operon is deleted, increased rate of spore formation; a double operon deletion (sdpA-sdpC plus skfA-skfH) makes spores even faster (PubMed:12817086). In a single gene deletion no SKP is produced (PubMed:20805502).
Belongs to the GerABKC lipoprotein family.
Belongs to the glutamate 5-kinase family.
Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
Belongs to the homoserine dehydrogenase family.
Lacks conserved residue(s) required for the propagation of feature annotation.
Involved in the biosynthesis of the catecholic siderophore bacillibactin. Catalyzes the activation of the carboxylate group of 2,3-dihydroxy-benzoate (DHB), via ATP-dependent PPi exchange reactions, to the acyladenylate.
Belongs to the GRP transporter (TC 2.A.7.5) family.
Reduces benzil stereospecifically to (S)-benzoin.
Activates ald expression in response to alanine availability and is important for normal sporulation in B.subtilis.
Disruption of adeR causes a sporulation defect.
A null mutation does not lead to any detectable defect in guanosine uptake. However, in the nupG-nupN double mutant, guanosine uptake is reduced to an almost undetectable level.
Part of an ABC transporter complex involved in the uptake of guanosine (PubMed:21926227). Is probably the substrate-binding protein of the system (PubMed:21926227). May be a nucleoside transporter of broad specificity but with various affinities for different substrates (PubMed:21926227).
The complex is composed of two ATP-binding proteins (NupO), two transmembrane proteins (NupP and NupQ) and a solute-binding protein (NupN).
Autoregulated. Induced by antibiotics (vancomycin, bacitracin, nisin and ramoplanin), cationic antimicrobial peptides (human LL-37 and porcine PG-1), Triton X-100 and severe secretion stress.
Member of the two-component regulatory system LiaS/LiaR probably involved in response to a subset of cell wall-active antibiotics that interfere with the lipid II cycle in the cytoplasmic membrane (bacitracin, nisin, ramoplanin and vancomycin). Seems also involved in response to cationic antimicrobial peptides and secretion stress. LiaR regulates the transcription of the liaIHGFSR operon.
Belongs to the binding-protein-dependent transport system permease family. MalFG subfamily.
Part of the ABC transporter complex AraNPQ involved in the uptake of arabinooligosaccharides. Transports alpha-1,5-arabinooligosaccharides, at least up to four L-arabinosyl units (PubMed:20693325). Responsible for the translocation of the substrate across the membrane (Probable).
The complex is composed of two ATP-binding proteins (MsmX), two transmembrane proteins (AraP and AraQ) and a solute-binding protein (AraN).
Transcription is repressed by glucose and by the binding of AraR to the operon promoter. L-arabinose acts as an inducer by inhibiting the binding of AraR to the DNA, thus allowing expression of the gene.
Effects nucleoid occlusion by binding relatively nonspecifically to DNA and preventing the assembly of the division machinery in the vicinity of the nucleoid, especially under conditions that disturb the cell cycle. It helps to coordinate cell division and chromosome segregation by preventing the formation of the Z ring through the nucleoid, which would cause chromosome breakage.
Belongs to the sulfate adenylyltransferase family.
Up-regulated by sulfur starvation and repressed by cysteine. Also induced by O-acetyl-L-serine (OAS), a direct precursor of cysteine, maybe via inactivation of a putative transcriptional repressor of the cysH operon whose activity is controlled by the intracellular levels of OAS.
Role in growth and sporulation on acetoin or butanediol. Involved in the breakdown of these compounds used as a carbon source.
Belongs to the sigma-70 factor family. ECF subfamily.
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Positively regulates the expression of proteins involved in stress responses against bacitracin, paraquat and tellurite.
Belongs to the glucosamine/galactosamine-6-phosphate isomerase family. NagB subfamily.
Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
Expression is repressed by the HTH-type transcriptional regulator NagR.
Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. Attractants increase the level of methylation while repellents decrease the level of methylation (By similarity).
Belongs to the 3-oxoacid CoA-transferase subunit A family.
Heterodimer of a subunit A and a subunit B.
Belongs to the carbohydrate esterase 7 family.
Esterase that removed acetyl groups from a number of O-acetylated small substrates, such as acetylated xylose, short xylooligosaccharides and cephalosporin C. Has no activity towards polymeric acetylated xylan. Cannot cleave amide linkages.
Used in the pharmaceutical industry for the chemoenzymatic deacetylation of cephalosporins and the synthesis of novel antibiotics.
By inositol. Subjected to catabolite repression.
Involved in the oxidation of myo-inositol (MI) and D-chiro-inositol (DCI) to 2-keto-myo-inositol (2KMI or 2-inosose) and 1-keto-D-chiro-inositol (1KDCI), respectively. Can also use D-glucose and D-xylose, and shows a trace of activity with D-ribose and D-fructose.
Plays a role in the flagellum-specific transport system.
Abolishes riboflavin uptake, cell growth less inhibited by roseoflavin, a toxic riboflavin analog.
Belongs to the energy-coupling factor EcfT family.
Forms a stable energy-coupling factor (ECF) transporter complex composed of 2 membrane-embedded substrate-binding proteins (S component), 2 ATP-binding proteins (A component) and 2 transmembrane proteins (T component).
Forms a stable energy-coupling factor (ECF) transporter complex composed of 2 membrane-embedded substrate-binding proteins (S component), 2 ATP-binding proteins (A component) and 2 transmembrane proteins (T component). May be able to interact with more than 1 S component at a time (By similarity).
Transmembrane (T) component of an energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates (By similarity). Involved in riboflavin transport.
Transmembrane (T) component of an energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
Belongs to the dihydrofolate reductase family.
Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity).
Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
Belongs to the NAD(P)-dependent epimerase/dehydratase family.
To bacterial alkanal monooxygenase alpha and beta chains.
Belongs to the polysaccharide lyase 3 family.
Catalyzes the depolymerization of both polygalacturonate and pectins of methyl esterification degree from 22 to 89%, with an endo mode of action. In contrast to the majority of pectate lyases, displays high activity on highly methylated pectins.
Catalyzes the depolymerization of both polygalacturonate and pectins of methyl esterification degree from 22 to 89%, with an endo mode of action. In contrast to the majority of pectate lyases, displays high activity on highly methylated pectins. Is also able to cleave trigalacturonate to galacturonic acid and unsaturated digalacturonate.
Maximally expressed in early stationary phase in medium containing glucose and glutamine.
Belongs to the universal ribosomal protein uS17 family.
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
Catalyzes the ATP-dependent dehydration of threonylcarbamoyladenosine at position 37 (t(6)A37) to form cyclic t(6)A37 (ct(6)A37) in tRNAs that read codons beginning with adenine.
Belongs to the bacterial ribosomal protein bL21 family.
Part of the 50S ribosomal subunit (PubMed:30126986). Contacts protein L20 (By similarity).
Part of the 50S ribosomal subunit. Contacts protein L20.
This protein binds to 23S rRNA in the presence of protein L20.
Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family.
Belongs to the glutamine synthetase family.
Completely inhibited by glutamine and partially inhibited by glycine, alanine and AMP (PubMed:4149044, PubMed:24158439). Also inhibited by L-methionine-SR-sulphoximine (Met-Sox) (PubMed:8093698, PubMed:24158439).
Glutamine synthetase (GS) is an unusual multitasking protein that functions as an enzyme, a transcription coregulator, and a chaperone in ammonium assimilation and in the regulation of genes involved in nitrogen metabolism (PubMed:25691471). It catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia (PubMed:24158439). Feedback-inhibited GlnA interacts with and regulates the activity of the transcriptional regulator TnrA (PubMed:11719184, PubMed:12139611). During nitrogen limitation, TnrA is in its DNA-binding active state and turns on the transcription of genes required for nitrogen assimilation (PubMed:11719184, PubMed:12139611, PubMed:25691471). Under conditions of nitrogen excess, feedback-inhibited GlnA forms a stable complex with TnrA, which inhibits its DNA-binding activity (PubMed:11719184, PubMed:12139611, PubMed:25691471). In contrast, feedback-inhibited GlnA acts as a chaperone to stabilize the DNA-binding activity of GlnR, which represses the transcription of nitrogen assimilation genes (PubMed:25691471).
In cells lacking this gene, expression of glnR, tnrA, nasB, nrgAB, gabP and ure genes is derepressed.
Oligomer of 12 subunits arranged in the form of two hexagons.
Oligomer of 12 subunits arranged in the form of two hexagons. In its feedback-inhibited form, interacts with TnrA in order to block its DNA-binding activity. This inhibitory effect is the highest when both glutamine and AMP are present.
Repressed by GlnR under conditions of nitrogen excess (PubMed:2573733). Repressed by TnrA under conditions of nitrogen limitation.
Member of the two-component regulatory system WalK/WalR involved in the regulation of the ftsAZ operon, the yocH, ykvT, cwlO, lytE, ydjM, yjeA, yoeB genes and the tagAB and tagDEF operons. Binds to the ftsAZ P1 promoter sequence in vitro. WalR has been shown to directly bind to the regulatory regions of yocH, ykvT, tagAB/tagDEF. Activates cwlO, lytE and ydjM and represses yoeB and yjeA.
Belongs to the major facilitator superfamily. Proton-dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family.
Part of an ABC transporter complex involved in the uptake of guanosine (PubMed:21926227). Responsible for the translocation of the substrate across the membrane (Probable). May be a nucleoside transporter of broad specificity but with various affinities for different substrates (PubMed:21926227).
Activated by phosphorylation and inhibited by fructose 1,6-bisphosphate (FBP).
Homotetramer and homodimer (in equilibrium).
Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), including enzyme I, and histidine-containing protein (HPr) are required for the phosphorylation, which leads to the activation of the enzyme.
Belongs to the ABC transporter superfamily. SkfA peptide export (TC 3.A.1.128.1) family.
By Spo0A (PubMed:12817086) and PhoP, during nutrient starvation, especially phosphate starvation. Repressed by AbrB during normal growth when nutrients are plentiful, in association with the transcriptional repressor Abh.
Probably part of the ABC transporter SkfEF involved in the export of the bacteriocin SKF. Probably responsible for energy coupling to the transport system.
When the skfA-skfB-skfC-skfE-skfF-skfG-skfH operon is deleted, increased rate of spore formation; a double operon deletion (sdpA-sdpC plus skfA-skfH) makes spores even faster (PubMed:12817086).
Could be member of the two-component regulatory system YclK/YclJ.
A probable DEAD-box RNA helicase that plays a role in ribosomal 50S subunit assembly. May be a non-specific RNA helicase.
Belongs to the DEAD box helicase family.
In rich medium highest expression in exponential growth, expression decreases in stationary phase (at protein level).
No visible effect at 37 degrees Celsius, decreased growth at 16 degrees Celsius. A quadruple disruption of all RNA helicases (cshA, cshB, deaD, yfmL) is not lethal at 37 degrees Celsius, although both 50S and 70S ribosomes are decreased, while growth stops at 16 degrees.
Expressed in the forespore during sporulation.
Expression is dependent on sigma G, and to a much lesser extent on sigma F.
Mutant sporulates normally and has the same resistance to heat and UV radiation than wild-type spores. It exhibits no defect in the initiation of spore germination, but the spore outgrowth is slower than that of wild-type spores (PubMed:9611260). Mutant shows a reduced rate of spore germination in L-alanine (PubMed:28333204).
Probably contributes, directly or indirectly, to early events in germination (PubMed:28333204). May play a role in spore outgrowth (PubMed:9611260).
Belongs to the ABC-5 integral membrane protein family.
Expressed early in the stationary phase.
Part of the ABC transporter complex YtrBCDEF that plays a role in acetoin utilization during stationary phase and sporulation.
The complex is composed of 2 ATP-binding proteins (YtrB and YtrE), 2 transmembrane proteins (YtrC and YtrD) and a solute-binding protein (YtrF).
Belongs to the glycosyl hydrolase 4 family.
Catalyzes the hydrolysis of melibiose and alpha-galactosides of the raffinose family of oligosaccharides (RFOs) such as raffinose and stachyose. Cannot act on polymeric substrates such as locust bean gum.
Repressed by the transcriptional regulator MelR. Induced by melibiose and raffinose.
Belongs to the universal ribosomal protein uS19 family.
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
Repressed by zinc via the metallo-regulatory protein zur.
Belongs to the CDP-alcohol phosphatidyltransferase class-I family.
Cells appear normal, no effect on flotillin cluster numbers or size.
Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Association with RNAP core increases during sporulation but not tested stresses (at protein level).
Interacts transiently with the RNAP core.
Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released. This sigma factor is involved in the transition to post-exponential phase in the beginning of sporulation. It is also required for transcription of several stationary phase genes. Association with the RNAP core increases rapidly in early exponential phase, and reamins constant expression level after (PubMed:21710567).
Binds 2 magnesium ions per subunit. The first is coordinated via water, the second is coordinated to ATP but its significance is unclear.
Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
Belongs to the glycosyltransferase 2 family.
Transfers a hexose moiety onto 'Cys-41' of bacteriocin sublancin-168 (SunA). Accepts UDP-glucose (UDP-Glc), UDP-N-acetylglucosamine (UDP-GlcNAc), UDP-galactose (UDP-Gal), UDP-xylose (UDP-Xyl) and GDP-mannose as substrate.
Involved in the production of the bacteriocin subtilosin. Required for immunity to subtilosin.
Bifunctionality as a citrate and 2-methylcitrate synthase is likely important in the mother cell's physiological milieu.
Expressed in the mother cell at intermediate stages of sporulation under the control of the sigma-E factor.
Involved in both the tricarboxylic acid (TCA) and methylcitric acid cycles (PubMed:28956599). Has both 2-methylcitrate synthase and citrate synthase activities. Catalyzes the condensation of propionyl-CoA and oxaloacetate to yield 2-methylcitrate (2-MC) and CoA, and the condensation of acetyl-CoA and oxaloacetate to yield citrate and CoA (PubMed:8759838, PubMed:28956599). Has 2.3-fold higher activity as a 2-methylcitrate synthase (PubMed:28956599). Catalyzes the formation of either (2S,3R)- or (2R,3S)-2-methylcitrate (PubMed:28956599).
Putative single-stranded-DNA-specific exonuclease.
LevD and LevE act as negative regulators of the levanase operon. They may be involved in a PTS-mediated phosphorylation of a regulator.
The PTS EIIB type-4 domain is phosphorylated by phospho-EIIA on a histidyl residue. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the PTS EIIC type-4 domain.
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II LevDE PTS system is involved in fructose transport.
In the C-terminal section; belongs to the methylenetetrahydrofolate reductase family.
Catalyzes the conversion of chorismate to isochorismate.
Belongs to the major facilitator superfamily. TCR/Tet family.
Positive regulator of the glv operon expression, which consists of GlvA, GlvR and GlvC.
Belongs to the gluconeogenesis factor family.
Deletion leads to growth defects when cells are grown on minimal medium containing ribose, gluconate, citrate, fumarate or succinate, but does not affect growth and morphology on minimal medium containing glycolytic substrates such as glucose, sucrose or glycerol. Mutants exhibit media-dependent filamentous or L-shape-like aberrant morphologies.
Required for morphogenesis under gluconeogenic growth conditions.
Required for morphogenesis under gluconeogenic growth conditions. Required, in gluconeogenic growth conditions, for the correct localization of PBP1 and hence for displaying a normal rod shape.
When bacteria are grown on a gluconeogenic carbon source, overproduction can restore a normal rod-shaped morphology in a mreB mutant by rescuing the PBP1 localization.
Binds 1 thiamine pyrophosphate per subunit.
Involved in the cleavage of the C1-C2 bond of 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione (THcHDO) to yield 5-deoxy-glucuronate (5DG).
Belongs to the HAD-like hydrolase superfamily. MtnX family.
Dephosphorylates 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P) yielding 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Belongs to the sulfur carrier protein ThiS family.
C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-adenylated (-COAMP) by ThiF, then thiocarboxylated (-COSH) by ThiI.
Is the sulfur donor in the synthesis of the thiazole phosphate moiety of thiamine phosphate.
Acts as a transcriptional activator of the acoABCL operon encoding the acetoin dehydrogenase complex.
Negatively controlled by CcpA, a global regulator of carbon catabolite repression.
Belongs to the succinate/malate CoA ligase beta subunit family.
Heterotetramer of two alpha and two beta subunits (By similarity). Interacts with BrxC (PubMed:33722570).
Heterotetramer of two alpha and two beta subunits.
Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Belongs to the major facilitator superfamily. Nitrate/nitrite porter (TC 2.A.1.8) family.
May be involved in the production of the exopolysaccharide (EPS) component of the extracellular matrix during biofilm formation. EPS is responsible for the adhesion of chains of cells into bundles. Required for biofilm maintenance.
Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
Homotetramer. Forms heterodimers with either ThiH or ThiS.
Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family. MmpL subfamily.
Regulated by the two-component regulatory system YdfH/YdfI.
Binds 2 Zn(2+) or Co(2+) ions per subunit.
Belongs to the encapsulin family. Family 3 subfamily.
Activated by the cyclic di-AMP (c-di-AMP) receptor DarB in the absence of c-di-AMP.
Decreased growth rate; growth is almost completely restored in a triple relA-yjbM-ywaC mutant (PubMed:18067544).
Homodimer (PubMed:33619274). At very low potassium concentrations, when intracellular levels of c-di-AMP are low, interacts with apo-DarB (PubMed:33619274). c-di-AMP inhibits the binding of DarB to RelA (PubMed:33619274).
In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance.
In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. This enzyme catalyzes the formation of pppGpp which is then hydrolyzed to form ppGpp, it is probably the hydrolysis activity that is required for optimal growth (Probable).
Activates transcription of the blt gene in response to structurally dissimilar drugs.
Transcriptional repressor of the azlBCD operon involved in branched-chain amino acid transport.
Negative regulator of class I heat shock genes (grpE-dnaK-dnaJ and groELS operons). Prevents heat-shock induction of these operons.
Belongs to the SNF2/RAD54 helicase family.
Involved in the production of the bacteriocin subtilosin. Required for maximal production and for optimal immunity to subtilosin.
Correct processing of the 3' end of 23S rRNA no longer occurs in the absence of mrnC.
Homohexameric ring arranged as a trimer of dimers (PubMed:14767080). It has been suggested that the active form is the dimer which binds tRNA and that the hexameric form protects the substrate recognition loop (approximately residues 65-82) from proteolysis (PubMed:14767080).
Homohexameric ring arranged as a trimer of dimers.
Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. Plays a role in the secondary pathway of 23S rRNA 3' end maturation (PubMed:19880604).
Sulfate ions in the crystal structure may represent the inorganic phosphate substrate.
Belongs to the bacterial solute-binding protein SsuA/TauA family.
Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. It catalyzes the transfer of the malonyl-CoA group to the acyl-carrier-protein AcpK (Mal-AcpK).
Deletion of the yeeF-yezG operon has no visible growth phenotype, however it is out-competed by wild-type cells.
Expressed on rich and minimal solid media likely in early stationary phase; dependent on DegSU. Not expressed in liquid LB, but only under conditions that promote biofilm formation.
In the N-terminal section; belongs to the LXG family.
Interacts with cognate immunity protein YezG but not with non-cognate immunity protein YobK. The interaction probably inhibits the toxic activity of YeeF.
Toxic component of one of 6 LXG toxin-immunity modules in this strain. They promote kin selection, mediate competition in biofilms, and drive spatial segregation of different strains, indicating that LXG toxins may help avoid warfare between strains in biofilms. Mediates intercellular competition during biofilm formation; disruption of the operon disadvantages the bacteria, but overexpression of the cognate immunity protein restores growth in competition with wild-type. Overexpression alone in situ causes growth arrest but not cell lysis, a large decrease in chromosomal DNA content and the production of anucleate cells. No effect is seen on rRNA. Co-overexpression with cognate immunity protein YezG does not cause growth arrest. The toxic effect is dependent on the epsA and tapA operons which are required for biofilm formation (PubMed:34280190). Binds DNA in the presence and absence of YezG (By similarity).
Was originally suggested to be an RNase.
Cells lacking this gene are blocked in YukE secretion (PubMed:23861817, PubMed:24798022). They display an increased bacteriophage SPP1 resistance phenotype (PubMed:15576783).
Required for YukE secretion. Probable component or regulator of the ESX/ESAT-6-like secretion system (BsEss).
Interacts (via domains I (1-82) and III (111-326)) with CcrZ (PubMed:35576203). Some 20 DnaA protein molecules bind their sites in oriC.
Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids. DnaA can inhibit its own gene expression as well as that of other genes.
Belongs to the universal ribosomal protein uL4 family.
Forms part of the polypeptide exit tunnel.
One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.
Was originally thought to be comB, a competence gene.
Shows carboxylesterase activity in vitro.
Activity of CodY is modulated by interaction with two types of effectors: the branched-chain amino acids (BCAAs) leucine, isoleucine and valine, which are signals of the nutritional status of the cell, and GTP, which may signal the energetic status of the cell (PubMed:11331605, PubMed:15228537, PubMed:16488888, PubMed:17993518, PubMed:18083814, PubMed:19749041, PubMed:21764931, PubMed:25645558). During growth in a nutrient-rich medium, the concentrations of these effectors are high, and CodY, once activated by binding to these effectors, shows an increased affinity for its target promoters (PubMed:11331605, PubMed:15228537, PubMed:17993518, PubMed:18083814). GTP and the BCAAs act additively to increase the affinity of CodY for DNA (PubMed:17993518, PubMed:18083814). When nutrients become limiting, the concentrations of BCAAs and GTP drop, leading to dissociation of CodY from the DNA and derepression of genes that are required for adaptation to nutrient-poor conditions (PubMed:11331605, PubMed:15228537, PubMed:17993518). Interacts specifically with GTP and dGTP; no other naturally occurring nucleotides that were tested, including ppGpp and pppGpp, result in DNA protection (PubMed:17993518). GTP hydrolysis is not required for DNA binding (PubMed:17993518).
DNA-binding global transcriptional regulator which is involved in the adaptive response to starvation and acts by directly or indirectly controlling the expression of numerous genes in response to nutrient availability. During rapid exponential growth, CodY is highly active and represses genes whose products allow adaptation to nutrient depletion.
Homodimer (PubMed:15937175, PubMed:16488888, PubMed:19500589, PubMed:28011634). Homotetramer (PubMed:28011634). Homodimer under physiological conditions, but homotetramers are observed in the crystals (PubMed:28011634).
In B.subtilis, CodY targets include several hundred genes involved in many different processes, including sporulation, competence, transport systems and catabolic processes (PubMed:12618455, PubMed:23569278). CodY bound to GTP represses many stationary-phase and some early-sporulation genes during growth in excess nutrients (PubMed:11331605). Among others, it binds to the ilvB promoter region and mediates regulation of the ilvB operon by GTP and branched-chain amino acids (BCAAs) (PubMed:15228537, PubMed:17993518, PubMed:18083814, PubMed:19749041). It represses expression of the dipeptide transport operon (dpp) during the exponential growth phase in rich medium (PubMed:7783641, PubMed:11331605, PubMed:18083814). Is also involved in the repression of competence by casamino acids via direct binding and repression of the srfA and comK promoter regions (PubMed:8830686). CodY acts predominantly as a repressor of transcription, but it can also activate transcription of a few genes, including the acetate kinase gene ackA, whose expression is primarily dependent on BCAA levels and only secondarily on GTP levels (PubMed:16995897). Binds to a 15-bp canonical consensus DNA motif, the CodY-binding site (PubMed:18083814, PubMed:21764931, PubMed:23569278). CodY operators may contain multiple CodY-binding sites with 6-bp overlaps (PubMed:21764931). Most CodY-binding sites are in intergenic regions, but sites located within coding regions were also identified (PubMed:23569278).
Modular protein made up of an N-terminal effector binding GAF-type domain and a C-terminal wHTH DNA binding domain, separated by a helical linker (PubMed:16488888, PubMed:28011634). The GAF domain is involved in the formation of homodimers (PubMed:28011634). Amino acid binding to the GAF domain is associated with drastic but localized changes in structure (PubMed:19500589). Structural changes upon isoleucine binding may lead to increased affinity of Ile-bound CodY for its target DNA (PubMed:28011634).
Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. Is able to use the non-natural R enantiomer of 3,4-dihydroxy-2-butanone 4-phosphate as a substrate, but with less efficiency than the natural S enantiomer. Cannot use unphosphorylated 3,4-dihydroxy-2-butanone, 3,4-dihydroxy-2-butanone 3-phosphate or diacetyl as substrates.
Forms an icosahedral capsid composed of 60 subunits, arranged as a dodecamer of pentamers.
Forms an icosahedral capsid composed of 60 subunits, arranged as a dodecamer of pentamers. Can interact with riboflavin synthase, forming a lumazine synthase/riboflavin synthase complex, also designated as 'heavy riboflavin synthase complex', which consists of a trimer of riboflavin synthase enclosed within the icosahedral structure composed of 60 subunits of 6,7-dimethyl-8-ribityllumazine synthase.
Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines.
Activated by peptide binding to the PDZ domain.
Involved in the signal transduction pathway leading to the proteolytic activation of the mother cell transcription factor pro-sigma-K during sporulation. The signaling serine protease CtpB triggers pro-sigma-K processing by cleaving the pre-processed regulatory protein SpoIVFA and is necessary for the proper timing of sigma-K activation.
Is cleaved by SpoIVB in vitro and in vivo but this cleavage does not appear to be necessary for CtpB activation. CtpB can also cleave itself in vivo.
Is expressed in the forespore under the control of sigma-G, and in the mother cell under the control of sigma-E.
Pro-sigma-K processing is delayed by approximately 30 minutes, and sporulation efficiency is reduced approximately two-fold.
The PDZ domain functions as a gatekeeper to the protease tunnel and defines resting and active conformations of the protease.
Belongs to the mannonate dehydratase family.
Catalyzes the dehydration of D-mannonate.
Induced by galacturonate, repressed by glucose.
Member of the exu locus which is required for galacturonate utilization.
Allows bacterial pathogens to use the host heme as an iron source. Catalyzes the oxidative degradation of the heme macrocyclic porphyrin ring in the presence of a suitable electron donor such as ascorbate or NADPH--cytochrome P450 reductase, with subsequent release of free iron.
Neither hmoA single mutant nor the hmoA hmoB double mutant display robust and reproducible phenotypes relative to the wild-type.
Repressed by fur in the presence of iron.
Belongs to the transcriptional antiterminator BglG family.
Mediates positive regulation of the sacPA operon by functioning as an antiterminator factor of transcription.
Phosphorylated and inactivated by SacP (EII-Scr).
Belongs to the MenA family. Type 1 subfamily.
Conversion of 1,4-dihydroxy-2-naphthoate (DHNA) to demethylmenaquinone (DMK).
Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family.
Deletion of the gene does not affect growth on glucose, but the mutant cannot grow in the presence of arabinose. Deletion has a negative effect on the ability of the mutant to grow on alpha-1,5-arabinobiose. AraE/araN double mutant is unable to grow in the presence of alpha-1,5-arabinobiose.
Transcription is repressed by the binding of AraR to the promoter. L-arabinose acts as an inducer by inhibiting the binding of AraR to the DNA, thus allowing expression of the gene.
Uptake of L-arabinose across the cytoplasmic membrane with the concomitant transport of protons into the cell (symport system) (PubMed:9401028). In the presence of inducing amounts of L-arabinose, can import both D-galactose and D-xylose (PubMed:9620981). Can also transport the disaccharide alpha-1,5-arabinobiose (PubMed:20693325).
Involved in excretion of nitrite produced by the dissimilatory reduction of nitrate.
Belongs to the mandelate racemase/muconate lactonizing enzyme family.
Catalyzes the epimerization of L-Ala-D-Glu to L-Ala-L-Glu and has probably a role in the metabolism of the murein peptide, of which L-Ala-D-Glu is a component. Is also able to catalyze the reverse reaction and the epimerization of the other Ala-X dipeptides L-Ala-L-Asp, L-Ala-L-Leu, L-Ala-L-Met, and L-Ala-L-Ser. Is not able to epimerize other L-Ala-X dipeptides. Is also active with L-Ser-L-Glu and, oddly, L-Pro-L-Glu, but not with L-Glu-L-Glu, L-Lys-L-Glu, L-Lys-L-Ala, or D-Ala-D-Ala.
Repressed by AbrB, a transcription factor that negatively controls biofilm formation.
May be involved in the assembly, structure, or function of the flagellum. May polymerize to form a filamentous structure that is part of the flagellum.
Expression is induced in response to phosphate starvation in a PhoR-dependent manner.
Belongs to the RuBisCO large chain family. Type IV subfamily.
Catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P).
Positive regulator of sigma-B activity. Dephosphorylates RsbV in response to energy stress.
The PAS domain may participate in sensing the overall energy level of the cell and communicate this information to the phosphatase domain.
Transcriptional repressor for the ars operon.
Involved in positive regulation of the levanase operon which comprises the levDEFG genes for a fructose PTS system, and sacA for levanase.
Possibly phosphorylated and inactivated by the PTS system.
The PTS EIIA type-4 domain may serve a regulatory function, through its phosphorylation activity.
Belongs to the NOS family. Bacterial NOS oxygenase subfamily.
Catalyzes the production of nitric oxide.
Tetrahydrobiopterin (H4B). Can also use tetrahydrofolate (THF) in place of tetrahydrobiopterin (H4B) but binds THF with much lower affinity than H4B.
This protein is similar to the oxygenase domain of eukaryotic nitric oxide synthases but lacks the reductase domain which, in eukaryotes, is responsible for transfer of electrons to the ferric heme during nitric oxide synthesis.
4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by acpS.
Belongs to the acyl carrier protein (ACP) family.
Carrier of the growing fatty acid chain in fatty acid biosynthesis.
Belongs to the inorganic carbon transporter (TC 9.A.2) DabA family.
Part of an energy-coupled inorganic carbon pump.
ATPase required for the correct placement of the division site. Cell division inhibitors MinC and MinD act in concert to form an inhibitor capable of blocking formation of the polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings (By similarity).
ATPase required for the correct placement of the division site. Cell division inhibitors MinC and MinD act in concert to form an inhibitor capable of blocking formation of the polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings.
Belongs to the ParA family. MinD subfamily.
Interacts with MinC and FtsZ (By similarity). Interacts with MinJ.
Belongs to the glycosyltransferase 28 family. MurG subfamily.
Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
The active site is a redox-active disulfide bond.
Belongs to the ABC transporter superfamily. Ycf16 family.
Belongs to the nucleobase:cation symporter-2 (NCS2) (TC 2.A.40) family.
Forms a complex with cognate antitoxin YopB.
In the C-terminal section; belongs to the MbcT/ParT/Res family.
May be the toxic component of a type II toxin-antitoxin (TA) system. Neutralized by its cognate antitoxin YopB.
Belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family.
Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).
Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
May be a structural component of the flagellum that anchors the rod to the membrane.
Required for production of the bacteriocin SkfA.
Induced, via LiaR, by antibiotics (vancomycin, bacitracin, nisin and ramoplanin), cationic antimicrobial peptides (human LL-37 and porcine PG-1), Triton X-100 and severe secretion stress.
Member of the two-component regulatory system LiaS/LiaR probably involved in response to a subset of cell wall-active antibiotics that interfere with the lipid II cycle in the cytoplasmic membrane (bacitracin, nisin, ramoplanin and vancomycin). Seems also involved in response to cationic antimicrobial peptides and secretion stress. Activates probably LiaR by phosphorylation.
Belongs to the major facilitator superfamily. EmrB family.
Resistance to the epoxide antibiotic methylenomycin.
Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.
Mutations in spoVJ block sporulation at a late stage. Probably only functions late in development.
Activates, in anaerobic conditions, the transcription of the fermentative operons lctEP and alsDS, of the hmp gene encoding a flavohemoglobin-like protein, the nitrite reductase operon nasDE and the heme biosynthesis genes hemN and hemZ.
Cytochrome c oxidase activity is partially restored by mutations in bdbC or bdbD that are defective in the synthesis of disulfide bond containing proteins. The same mutations abrogate the need for CcdA in sporulation.
Required for cytochrome c synthesis and stage V of sporulation. Might transfer reducing equivalents across the cytoplasmic membrane, promoting efficient disulfide bond isomerization of proteins localized on the outer surface of the membrane or in the spore coat.
ATPase activity (residues 84-303) prefers Mg(2+) over Mn(2+).
Belongs to the GdpP/PdeA phosphodiesterase family.
Binds 1 heme (probably heme b) per subunit, probably hexa-coordinated, which inhibits PDE and ATPase. The Fe(2+) binds CN(-), CO and NO.
Expressed at low levels at the onset of sporulation, it rises during sporulation (at protein level).
For phosphodiesterase activity (residues 84-695), probably binds 2 Mn(2+) per subunit, can also use Co(2+), Mg(2+) or Ni(2+).
For phosphodiesterase activity, probably binds 2 Mn(2+) per subunit.
Has a GGDEF domain (residues 173-310) preceded by a PAS-like domain (residues 84-149) which together have ATPase activity, followed by a region with a DHH (339-496) and a DHHA1 (591-646) domain (PubMed:19901023). The combined GGDEF, DHH and DHHA1 domains have c-di-AMP phosphodiesterase activity (residues 150-659) that is 10-fold enhanced by inclusion of the PAS-like domain (84-149); PDE activity may only require the DHH/DHHA1 domains (PubMed:19901023). The PAS-like domain is important for heme b-binding (PubMed:21257773).
Has phosphodiesterase (PDE) activity against cyclic-di-AMP (c-di-AMP) and to a much lesser extent against cyclic-di-GMP (c-di-GMP) in the DHH/DHHA1 domains (PubMed:19901023, PubMed:21257773). Also has ATPase activity, probably via the GGDEF domain (PubMed:19901023, PubMed:21257773). Overexpression leads to increased sensitivity to methyl methanesulfonate (MMS) and H(2)O(2) (PubMed:25616256). Overexpression leads to extreme sensitivity to the beta-lactam antibiotic cefuroxime (CEF), probably dependent on PDE activity (PubMed:22211522). May monitor cellular heme or NO levels (PubMed:21257773). In B.subtilis c-di-AMP is a second messenger that mediates growth, DNA repair and cell wall homeostasis; it is toxic when present in excess (PubMed:26240071).
Has phosphodiesterase (PDE) activity against cyclic-di-AMP (c-di-AMP).
Increased resistance to acid stress, increased sporulation efficiency following DNA damage (by nalidixic acid) (PubMed:19901023). Increases c-di-AMP levels in mid-exponential phase from about 3.8 uM to about 4.3 uM in strain BG214 (PubMed:25616256). Increased levels of c-di-AMP 4-fold during sporulation (PubMed:21566650). Insertion mutations in this gene partially restore antibiotic resistance to the beta-lactam antibiotic cefuroxime (CEF) in a sigM deletion mutant (PubMed:22211522). Decreased sensitivity to MMS and H(2)O(2) (PubMed:25616256). In strain 168 grown in minimal medium and glutamate, 2.2-fold increase in c-di-AMP levels while a double pgpH-gdpP mutant has 4.2-fold increased levels of in c-di-AMP; double mutants die on solid medium after 2 days (PubMed:26240071).
Phosphodiesterase (PDE) inhibited by Zn(2+), Ca(2+) inhibits in the presence of Mg(2+) but not Mn(2+); c-di-AMP PDE activity is competitively inhibited by ppGpp (PubMed:19901023). Heme binding (by Fe(2+) or Fe(3+) heme) inhibits PDE, activity is partially restored by KCN or NO only for Fe(2+) heme (PubMed:21257773). Binding of NO to Fe(2+) heme switches from hexa- to pentacoordination (PubMed:21257773). Heme binding inhibits the ATPase activity (PubMed:21257773).
Probably transcribed under control of the sigma A factor (sigA), protein levels are negatively regulated by an antisense RNA (PubMed:22956758).
Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily.
Central regulator of manganese homeostasis that regulates the expression of both manganese uptake and efflux systems (PubMed:27748968, PubMed:10760146, PubMed:12950915). In the presence of high levels of manganese, it mediates repression of the manganese uptake systems MntH and MntABCD and activation of the efflux systems MneP and MneS. Binds with high affinity to the regulatory regions of its target genes (PubMed:27748968, PubMed:12950915). The manganese concentration required for activation of efflux is higher than that for repression of uptake (PubMed:27748968).
Central regulator of manganese homeostasis.
Contains an N-terminal DNA-binding domain and a C-terminal dimerization domain (PubMed:12847518, PubMed:16533030, PubMed:23298157). Contains two metal binding sites per subunit, site A (corresponding to metal ion 2) and site C (corresponding to metal ion 1), which both contribute to the metal selectivity of MntR. A large metal cation is needed at the A site to correctly orient and position the C site ligands. Smaller, non-cognate metal cations bind at the A site, but disrupt the C site, blocking the full activation of MntR. Binding at the C site also favors Mn(2+) and Cd(2+) over other metals (PubMed:16533030, PubMed:23298157).
DNA binding is strongly activated by Mn(2+) and Cd(2+), but it is poorly activated by non-cognate metal cations, including Co(2+), Fe(2+), Ni(2+), Ca(2+) and Zn(2+). In the strict absence of divalent transition metal ions, MntR has a low affinity for DNA.
DNA binding is strongly activated by Mn(2+).
Null mutant is very sensitive to manganese (PubMed:27748968, PubMed:10760146). Mutant also displays increased sensitivity to cadmium (PubMed:10760146).
Was originally thought to act as an activator for the mntABCD operon.
Has low dephosphorylation activity on GMP and glucose-6-phosphate.
Belongs to the zinc-containing alcohol dehydrogenase family.
Cells lacking this gene retain acetoin reductase/2,3-butanediol dehydrogenase activity.
Binds 4 Mg(2+) or Mn(2+) ions per subunit.
Involved in the anaerobic nitrogen utilization via the assimilation of allantoin (PubMed:11344136). Catalyzes specifically the hydrolysis of allantoate to yield CO2, NH3 and S-ureidoglycine, which is unstable and readily undergoes a second deamination by S-ureidoglycine aminohydrolase AllE to yield S-ureidoglycolate and NH3 (By similarity).
Transcriptionally regulated by PucR. Expression is very low in excess nitrogen (glutamate plus ammonia) and is induced during limiting-nitrogen conditions (glutamate). Expression is further induced when allantoin is added during limiting-nitrogen conditions.
Member of a high affinity multicomponent binding-protein-dependent transport system for glycine betaine, carnitine, and choline.
The complex is composed of two ATP-binding proteins (OpuCA), two transmembrane proteins (OpuCB and OpuCD) and a solute-binding protein (OpuCC).
Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB.
B.subtilis has three MreB paralogs: MreB, Mbl and MreBH. All paralogs have the ability to support rod-shaped cell growth normal conditions. The multiplicity of paralogs becomes important under stress conditions. They are probably used to allow cells to maintain proper growth and morphogenesis under changing conditions.
Disruption of the gene leads to cells that are curved, bent at irregular angles and affected in length and width.
Forms membrane-associated dynamic filaments that are essential for cell shape determination (PubMed:16950129, PubMed:19659933). Acts by regulating cell wall synthesis and cell elongation, and thus cell shape (PubMed:16950129, PubMed:19659933). A feedback loop between cell geometry and MreBH localization may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature (By similarity). Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on MreBH polymerization (PubMed:21636745, PubMed:21636744). Organizes peptidoglycan synthesis in the lateral cell wall (PubMed:19659933). Required for the localization of the cell wall hydrolase LytE into the cylindrical part of the cell wall (PubMed:16950129).
Forms membrane-associated dynamic filaments that are essential for cell shape determination. Acts by regulating cell wall synthesis and cell elongation, and thus cell shape. A feedback loop between cell geometry and MreB localization may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature.
Forms polymers (PubMed:16950129). Forms a complex with Mbl and MreB (PubMed:19659933). Interacts with the C-terminal catalytic domain of LytE (PubMed:16950129).
Belongs to the NADH dehydrogenase family.
Belongs to the bacterial solute-binding protein 3 family.
Probably part of a binding-protein-dependent transport system.
Belongs to the mandelate racemase/muconate lactonizing enzyme family. GlucD subfamily.
Catalyzes the dehydration of glucarate to 5-keto-4-deoxy-D-glucarate (5-kdGluc).
Belongs to the universal ribosomal protein uL6 family.
This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.
Cells lacking this gene have a twofold decreased response to salt and ethanol stress, and a somewhat reduced response to energy stress, indicating that PhoT is a positive regulator of sigma-B activity. It acts independently of both RsbRA and RsbRB (YkoB).
Exhibits the same spectroscopical features and blue-light induced photochemistry as plants phototropins, with the reversible formation of a blue-shifted photoproduct, assigned to an FMN-cysteine thiol adduct. Although it is a positive regulator in the activation of the environmental signaling branch of the general stress transcription factor sigma-B, its precise role is undetermined.
FMN binds covalently to cysteine after exposure to blue light and this bond is spontaneously broken in the dark.
Belongs to the bacterial solute-binding protein 1 family.
Deletion of the gene abolishes induction in the presence of melibiose and raffinose.
Part of the ABC transporter complex MelEDC-MsmX involved in melibiose, raffinose and stachyose import. Binds melibiose, raffinose and stachyose.
The complex is composed of two ATP-binding proteins (MsmX), two transmembrane proteins (MelC and MelD) and a solute-binding protein (MelE).
Belongs to the transglycosylase Slt family.
Exhibits both muramidase and lytic transglycosidase activities (PubMed:20609359). Cleaves the beta-1,4-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine (MurNAc-GlcNAc) in peptidoglycan, producing both N-acetylmuramic acid and 1,6-anhydro-N-acetylmuramic acid (PubMed:20609359). Is conditionally required for swarming motility and may play a role in flagella function specifically on harder surface environments, but is not required for flagellar assembly (PubMed:33649146).
Expressed by the motility sigma factor SigD.
Mutants exhibit wild-type swimming motility in liquid, but they exhibit a severe defect in flagellum-dependent swarming motility (PubMed:33649146). Mutants are not defective in flagellar assembly (PubMed:33649146). They have a slight but statistically significant reduction in the number of flagellar hooks and basal bodies (PubMed:33649146).
The N-terminal domain is important for secretion and protein stability.
Alteration (reduction or loss for the most part) of expression of about 60 genes that are high-pH-inducible, including sigW and its anti-sigma factor rsiW (PubMed:11454200).
By different stresses causing damage to the cell envelope, such as alkaline shock (PubMed:11454200), salt shock (PubMed:11544224), phage infection and certain antibiotics that affect cell wall biosynthesis (PubMed:12207695, PubMed:15870467). Does not respond to oxidative stress caused by diamide (PubMed:21685450). Association with RNAP core increases during most stresses but not during sporulation (at protein level) (PubMed:21710567).
Extracytoplasmic function (ECF) sigma factors are held in an inactive form by a cognate anti-sigma factor (RsiW for this protein) until released by regulated membrane proteolysis (RIP). RIP occurs when an extracytoplasmic signal (envelope stress) triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The anti-sigma factor RsiW is a membrane protein, binding sigma-W in the cytoplasm. RsiW is first cut extracytoplasmically (site-1 protease, S1P, by PrsW) (PubMed:16816000), then within the membrane itself (site-2 protease, S2P, by RasP) (PubMed:15130127), while cytoplasmic proteases (predominantly ClpX-ClpP) finish degrading the regulatory protein, liberating sigma-W (PubMed:16899079).
Interacts transiently with the RNA polymerase catalytic core formed by RpoA, RpoB, RpoC and RpoZ (2 alpha, 1 beta, 1 beta' and 1 omega subunit) to form the RNA polymerase holoenzyme that can initiate transcription. Forms a heterodimer with cognate anti-sigma factor RsiW, which prevents it from binding to the -10 and -35 promoter elements (PubMed:28319136).
Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released. Sigma-W controls genes involved in response to cell envelope stress such as antimicrobial peptides (PubMed:12207695, PubMed:15870467), alkaline pH (PubMed:11454200), transport processes and detoxification.
The sigma-70 factor domain-2 mediates sequence-specific interaction with the -10 element in promoter DNA (PubMed:28319136), and plays an important role in melting the double-stranded DNA and the formation of the transcription bubble. Also mediates interaction with the RNA polymerase subunits RpoB and RpoC (By similarity).
The sigma-70 factor domain-4 contains a helix-turn-helix (H-T-H) motif that mediates interaction with the -35 element in promoter DNA (PubMed:28319136). The domain also mediates interaction with the RNA polymerase subunit RpoA (By similarity).
Suggested to be part of an ABC transporter complex YydIJ involved in export of the modified peptide YydF (Probable). Responsible for energy coupling to the transport system (By similarity).
The complex is composed of two ATP-binding proteins (YydI), two transmembrane proteins (YydJ).
Transcriptionally repressed by rok (PubMed:15743949), this was not found to be the case in another study (PubMed:17921301).
Up-regulates expression of the LiaRS two-component regulatory system; this effect is more pronounced on modified competence medium than on rich or sporulation medium.
Belongs to the binding-protein-dependent transport system permease family. OppBC subfamily.
Nutrient deficiency conditions, which also induce sporulation.
Probably part of the ABC transporter DppBCDE involved in dipeptide transport (Probable). Responsible for the translocation of the substrate across the membrane (Probable).
Involved in the degradation of long-chain fatty acids.
Repressed by FadR in the absence of LCFAs (fatty acids of 14-20 carbon atoms). When LCFAs are present in the medium, they are converted to long-chain acyl-CoAs, which antagonize FadR as to its binding to FadR boxes on target DNA and thus derepress transcription.
Could be composed of four subunits: PucA, PucC, PucD and PucE.
Expression is very low in excess nitrogen (glutamate plus ammonia) and is induced during limiting-nitrogen conditions (glutamate). Expression decreases when allantoin is added during limiting-nitrogen conditions.
Oxidizes hypoxanthine and xanthine to uric acid.
Belongs to the binding-protein-dependent transport system permease family. CysTW subfamily.
Involved in a high affinity multicomponent binding-protein-dependent transport system for choline; probably responsible for the translocation of the substrate across the membrane.
Belongs to the triosephosphate isomerase family.
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Expression is up-regulated by cumene hydroperoxide (CHP).
N-terminal Cys of the CXC active site motif can react with bacillithiol (BSH) to form mixed disulfides. S-bacillithiolation protects Cys residues against overoxidation by acting as a redox switch in response to oxidative stress.
S-bacillithiolation is the formation of mixed disulfide bonds between protein thiols and the general thiol reductant bacillithiol (BSH) under oxidative stress. BSH is an equivalent of glutathione (GSH) in Firmicutes. This protein is a dithiol bacilliredoxin, which debacillithiolates (removes BSH) the S-bacillithiolated OhrR (OhrR-SSB) in vitro and in vivo NaOCl-generated S-bacillithiolated MetE (MetE-SSB). Involved in maintaining redox homeostasis in response to disulfide stress conditions.
Sensitive to cumene hydroperoxide (CHP) as indicated by growth inhibition assay. No effect on growth after NaOCl treatment.
Belongs to the ChdC family. Type 1 subfamily.
Fe-coproporphyrin III acts as both substrate and redox cofactor.
Involved in coproporphyrin-dependent heme b biosynthesis (PubMed:25646457). Catalyzes the decarboxylation of Fe-coproporphyrin III (coproheme) to heme b (protoheme IX), the last step of the pathway (By similarity). The reaction occurs in a stepwise manner with a three-propionate harderoheme intermediate (By similarity).
Belongs to the acireductone dioxygenase (ARD) family.
Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway.
Catalyzes 2 different reactions between oxygene and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway.
Belongs to the sulfur carrier protein TusA family.
Required for xanthine dehydrogenase activity. Could be involved in formation of the molybdenum cofactor required by xanthine dehydrogenase.
Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. Phosphorylated CheY interacts with the flagella switch components FliM and FliY, which causes counterclockwise rotation of the flagella, resulting in smooth swimming.
Phosphorylated CheY binds to FliM and FliY.
Phosphorylated by CheA. Dephosphorylated (inactivated) by FliY and CheC.
The signaling mechanism of chemotaxis in B.subtilis appears to be inverted in comparison to E.coli.
Negatively regulates mhqA, mhqED, mhqNOP, and azoR2 which may contribute to the degradation of aromatic compounds.
Repressed by 2-methylhydroquinone (2-MHQ), diamide and catechol stress. Not subject to autorepression.
Belongs to the amino acid-polyamine-organocation (APC) superfamily.
May be involved in maturation of the outermost layer of the spore.
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF (By similarity).
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF.
Belongs to the ABC transporter superfamily. L-cystine importer (TC 3.A.1.3.13) family.
More strongly expressed in the presence of methionine than in the presence of sulfate.
Part of the ABC transporter complex TcyJKLMN involved in L-cystine import. Responsible for energy coupling to the transport system (Probable). Is also involved in cystathionine, djenkolate, and S-methylcysteine transport.
The complex is composed of two ATP-binding proteins (TcyN), two transmembrane proteins (TcyL and TcyM) and two solute-binding proteins (TcyJ and TcyK).
Belongs to the PEP-utilizing enzyme family.
Lacks almost all of the known catalytic and substrate-binding residues for this enzyme; hence it is annotated as putative.
Might catalyze the phosphorylation of pyruvate to phosphoenolpyruvate.
CSF, PhrF and PhrK stimulate ComA-dependent gene expression to different levels and are all required for full expression of genes activated by ComA.
Contains a predicted signal peptide cleavage site in the N-terminal region, however the propeptide is probably only subject to processing events at the ends of the mature peptide.
Deletion of the gene results in decreased expression of genes activated by ComA, and significantly changes the expression of 40 operons.
Signaling molecule involved in the regulation of genetic competence development (PubMed:16816200). Secreted during production, but the mature peptide acts intracellularly, indicating that it needs to be imported into the cell to function (By similarity). Stimulates expression of the genes controlled by ComA, a transcriptional factor that regulates the development of genetic competence (PubMed:16816200). Acts by inhibiting RapK, which regulates the activity of ComA (PubMed:16816200).
Belongs to the methylthiotransferase family. MiaB subfamily.
Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
Belongs to the membrane fusion protein (MFP) (TC 8.A.1) family.
Belongs to the prokaryotic/mitochondrial release factor family.
Methylated by PrmC. Methylation increases the termination efficiency of RF1 (By similarity).
Methylated by PrmC. Methylation increases the termination efficiency of RF1.
Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
Transcriptional repressor of the gmuBACDREFG operon which is involved in the uptake and degradation of glucomannan.
Up-regulated by konjac glucomannan and by cellobiose and mannobiose, the possible degradation products of glucomannan. Repressed by glucose via the carbon catabolite repression system.
Belongs to the ATP-dependent DNA ligase family.
Expressed in vegetative cells. Also present in dormant spores in the forespore inner membrane.
Involved in the synthesis of peptidoglycan associated with cell wall elongation, especially following spore germination (PubMed:9139922). Has a partially redundant function with PBP 1 (ponA) or PBP 4 (pbpD) during spore outgrowth (PubMed:9851991). Plays a redundant role with PbpH in determining the rod shape of the cell during vegetative growth and spore outgrowth (PubMed:12896990).
No visible phenotype during vegetative growth rate in rich media, no difference in sporulation or initial spore germination. Spores have a significant delay in outgrowth, between 60-90 minutes cells swell rather than elongate, upon eventual elongation they have a larger diameter and are often bent (PubMed:9139922, PubMed:9851991). Single deletions have reduced peptidoglycan (PG) synthesis and turnover rates. Double ponA-pbpA deletions spores have greatly decreased viability, PG synthesis and elongate poorly; increased levels of Mg(2+) increase spore viability. Double pbpA-pbpD deletions spores have greatly decreased spore outgrowth and peptidoglycan synthesis (PubMed:9851991). Single pbpA mutants are less resistant to ceftriaxone and mecillinam. Double pbpA-pbpH mutants cannot be made, suggesting the 2 proteins have redundant, essential roles in vegetative growth (PubMed:12896990).
Transcribed during vegetative phase, drops off during sporulation, rises again 30-40 minutes after germination. A small amount is present in dormant spores.
Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily.
Catalyzes the addition of glucose to the C-2 hydroxy group of the glycerol units in teichoic acid.
Not essential. No glucose groups on the glycerol residues of teichoic acid in cell walls.
Belongs to the bacterial ribosomal protein bS16 family.
Belongs to the ABC transporter superfamily. Cysteine exporter (TC 3.A.1.129.1) family.
In CydD the ATP-binding domain (NBD) and the transmembrane domain (TMD) are fused.
Part of the ABC transporter complex CydDC that exports the reduced low-molecular-weight thiols cysteine and glutathione from the cell. Export of these thiol-containing redox-active molecules may be crucial for redox homeostasis, permitting correct assembly of various respiratory complexes and formation of correct disulfide bonds in secreted proteins. CydD contains transmembrane domains (TMD), which form a pore in the membrane, and an ATP-binding domain (NBD), which is responsible for energy generation.
Part of the binding-protein-dependent transport system for molybdenum; probably responsible for the translocation of the substrate across the membrane.
could be part of the binding-protein-dependent transport system for molybdenum; probably responsible for the translocation of the substrate across the membrane.
Contains large globular domains required for ATP hydrolysis at each terminus and a third globular domain forming a flexible SMC hinge near the middle of the molecule. These domains are separated by coiled-coil structures.
Contains large globular domains required for ATP hydrolysis at each terminus and a third globular domain forming a flexible hinge near the middle of the molecule. These domains are separated by coiled-coil structures.
Mutants produce anucleate cells and show defects in nucleoid structure and in chromosome partitioning.
Required for chromosome condensation and partitioning.
As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner (By similarity). Catalyzes the attachment of valine to tRNA(Val).
Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily.
By valine starvation. Is transcribed by itself and in an operon with folC. A GUC triplet (Val, the specifier codon) 190 nucleotides upstream of the initiator codon confers induction upon valaine starvation; replacing it with ACC (Thr) confers induction upon threonine starvation, replacing it with UAA (stop), renders the gene uninducible. Negatively regulates its own transcription; this depends on the presence of the GUC specifier codon.
Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
Cells lacking this gene grow normally, suggesting there is a second functional gene with valine-tRNA synthetase activity in B.subtilis.
The C-terminal coiled-coil domain is crucial for aminoacylation activity.
ValRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated threonine is translocated from the active site to the editing site.
Necessary for flagellar biosynthesis. May be involved in translocation of the flagellum.
Monomer. Binds 30S ribosomal subunits, but not 50S ribosomal subunits or 70S ribosomes.
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA.
Activity is stimulated by low concentrations of salts and by moderate concentrations of glycine betaine. Highly tolerant to high ionic conditions. In vitro, activity is highly stimulated in the presence of proline.
Belongs to the aldehyde dehydrogenase family.
By choline and by high osmolarity in the presence of choline (PubMed:8752328, PubMed:22408163). Repressed by GbsR (PubMed:22408163).
Deletion of the gbsAB genes abolishes the choline-glycine betaine synthesis pathway and the ability of B.subtilis to deal effectively with high-osmolarity stress in choline- or glycine betaine aldehyde-containing medium (PubMed:8752328). No effect on vanillin degradation (PubMed:26658822).
Involved in the biosynthesis of the osmoprotectant glycine betaine from choline (PubMed:8752328, PubMed:9297465). Catalyzes the oxidation of betaine aldehyde to betaine (PubMed:9297465). Shows specificity for betaine aldehyde as substrate. Can use both NAD(+) and NADP(+), but NAD(+) is strongly preferred (PubMed:9297465).
Belongs to the DCC thiol-disulfide oxidoreductase family.
Provides the crucial link between the upstream module (communication of environmental stress) and the downstream module (integration of the environmental signals with signals of energy stress) that compose the signal transduction pathway controlling the sigma-B factor. Phosphorylates and inactivates its specific antagonist protein RsbS thanks to its serine kinase activity. Upon phosphorylation of RsbS, RsbT is released to stimulate RsbU, a PP2C phosphatase, thereby initiating the signaling cascade that ultimately activates sigma-B. The activity of the RsbU phosphatase may be stimulated by a long-lived interaction with RsbT and the serine kinase function of RsbT is not required to directly modify RsbU. Also phosphorylates RsbR thanks to its threonine kinase activity, preventing it to phosphorylate RsbT.
This protein is a component of an oligopeptide permease, a binding protein-dependent transport system. This APP system can completely substitute for the OPP system in both sporulation and genetic competence, though, unlike OPP, is incapable of transporting tripeptides. Probably responsible for energy coupling to the transport system.
Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate. Can functionally substitute for the FBPase class 3 (Fbp) of B.subtilis.
Disruption of ywjI alone (or fbp alone) does not affect growth on various carbon sources. But the ywjI fbp double mutant is unable to grow with carbon sources demanding FBPase activity, i.e. glycerol, malate, and a mixture of succinate and glutamate.
Expressed at the same level under glycolytic or gluconeogenic conditions.
Belongs to the class-A beta-lactamase family.
This protein is a beta-lactamase with a substrate specificity for penicillins.
Belongs to the polysaccharide deacetylase family.
Belongs to the universal ribosomal protein uS10 family.
Involved in the binding of tRNA to the ribosomes.
Belongs to the ABC transporter superfamily. Phosphate importer (TC 3.A.1.7) family.
Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
The complex is composed of two ATP-binding proteins (PstB), two transmembrane proteins (PstC and PstA) and a solute-binding protein (PstS).
Belongs to the sodium:galactoside symporter (TC 2.A.2) family.
Expressed at low levels during exponential growth, it increases dramatically at the onset of sporulation (at protein level). A member of the spoIISA-spoIISB operon.
Probably forms an oligomer; X-ray data suggests the inactive complex forms a heterotetramer of SpoIISA(2)-SpoIISB(2), which inactivates the toxic activity of SpoIISA.
Toxic component of a type II toxin-antitoxin (TA) system. Its toxic activity is neutralized by cognate antitoxin SpoIISB. Expression in the absence of SpoIISB permits sporulation to stage II, when plasmolysis zones and holes in the peptidoglycan layer are observed, resulting in cell death. Lethal when synthesized during vegetative growth in the absence of SpoIISB. In E.coli both the membrane bound and soluble domain are required in cis for toxin activity.
Part of the ABC transporter complex MetNPQ involved in methionine import. Responsible for the translocation of the substrate across the membrane (Probable). It has also been shown to be involved in methionine sulfoxide transport.
Repressed by methionine via the S-box system.
The complex is composed of two ATP-binding proteins (MetN), two transmembrane proteins (MetP) and a solute-binding protein (MetQ).
Induced, via the two-component regulatory system LiaS/LiaR, by antibiotics (vancomycin, bacitracin, nisin and ramoplanin), cationic antimicrobial peptides (human LL-37 and porcine PG-1), Triton X-100 and severe secretion stress.
Up-regulates expression of liaI which in turn induces the liaRS two-component regulatory system.
By phosphate starvation, via the alternative sigma factor sigma-B.
Part of a complex composed of YknX, YknY and YknZ. The complex interacts with YknW.
Part of an unusual four-component transporter, which is required for protection against the killing factor SdpC (sporulation-delaying protein).
Belongs to the nucleobase:cation symporter-2 (NCS2) (TC 2.A.40) family. Azg-like subfamily.
Expression is regulated by the purR regulon. Down-regulated by adenine and up-regulated by guanosine.
Involved in the uptake of the purine bases hypoxanthine and guanine. May work at purine concentrations higher than 100 uM.
Belongs to the universal ribosomal protein uL16 family.
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.
Belongs to the major facilitator superfamily. Phthalate permease family.
Transport of aldohexuronates such as D-glucuronate and D-galacturonate.
Belongs to the NADH:flavin oxidoreductase/NADH oxidase family. NamA subfamily.
By toxic xenobiotic compounds (2,4,6-trinitrotoluene and nitroglycerin), and in response to oxidative stress (hydrogen peroxide and paraquat).
Catalyzes the reduction of the double bond of an array of alpha,beta-unsaturated aldehydes and ketones. It also reduces the nitro group of nitroester and nitroaromatic compounds. It could have a role in detoxification processes.
Forms a charge transfer complex with a variety of phenolic compounds.
Homotetramer. Composed of a dimer of active dimers.
Inhibited by p-hydroxybenzaldehyde (pHBA) and p-nitrophenol (pNP).
Cells lacking this gene are blocked in YukE secretion (PubMed:23861817, PubMed:24798022). They display an increased bacteriophage SPP1 resistance phenotype (PubMed:15576783). Loss of delivery of LXG toxins to target cells (PubMed:34280190).
Required for YukE secretion. Probable component or regulator of the ESX/ESAT-6-like secretion system (BsEss) (PubMed:23861817, PubMed:24798022). Required to deliver LXG toxins to target cells (PubMed:34280190).
The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Belongs to the thiamine-phosphate synthase family.
Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). Is also able to use the 2-methoxy analog MeO-HMP-PP, as substrate in vitro, but not the 2-trifluoromethyl analog CF(3)-HMP-PP.
Is weakly repressed by THZ and not at all by thiamine.
Thiamine phosphate synthase appears to proceed with a dissociative mechanism (SN1 like) in which the pyrimidine pyrophosphate dissociates to give a reactive pyrimidine intermediate which is then trapped by the thiazole moiety.
Belongs to the glycerate kinase type-1 family.
Involved in a multicomponent binding-protein-dependent transport system for glycine betaine.
The complex is composed of two ATP-binding proteins (OpuAA), two transmembrane proteins (OpuAB) and a solute-binding protein (OpuAC) (PubMed:7622480). Interacts with FloT (PubMed:23651456).
Belongs to the cysteine synthase/cystathionine beta-synthase family.
Catalyzes the conversion of O-acetylserine to cysteine. Also acts as a sensor of cysteine availability in the signal transduction pathway modulating CymR activity. When cysteine is present, the pool of O-acetylserine (OAS) is low, which leads to the formation of a CymR-CysK complex and transcriptional repression of the CymR regulon occurs. In the absence of cysteine, the OAS pool is high and the CymR-CysK complex is mostly dissociated, leading to a faster dissociation of CymR from its DNA targets and the lifting of CymR-dependent repression.
Grows very slowly with sulfate, butanesulfonate or cystine as sole sulfur source.
Highly expressed in the presence of methionine, but poorly expressed in the presence of cystine. Also induced by superoxide. Repressed both by sulfate and cysteine.
Homodimer. Forms CymR(2):CysK(2) or CymR(4):CysK(4) complexes in the absence of O-acetylserine.
Belongs to the iron-containing alcohol dehydrogenase family.
Deletion of the gbsAB genes abolishes the choline-glycine betaine synthesis pathway and the ability of B.subtilis to deal effectively with high-osmolarity stress in choline- or glycine betaine aldehyde-containing medium.
Involved in the biosynthesis of the osmoprotectant glycine betaine from choline.
B.subtilis contains two L-asparaginase isoenzymes: L-asparaginase I, a low-affinity enzyme located in the cytoplasm, and L-asparaginase II, a high-affinity secreted enzyme.
Produced in 2 x SG medium but not in 2 x YT medium.
Produced in 2 x YT medium but not in 2 x SG medium.
Part of the ABC transporter complex GlnHMPQ involved in glutamine transport. Probably responsible for the translocation of the substrate across the membrane (By similarity).
Major intracellular protease produced by Bacillus subtilis.
Immunity component of one of 6 LXG toxin-immunity modules in this strain. They promote kin selection, mediate competition in biofilms, and drive spatial segregation of different strains, indicating that LXG toxins may help avoid warfare between strains in biofilms. Mediates intercellular competition during biofilm formation; disruption of the operon disadvantages the bacteria, but overexpression of the cognate immunity protein restores growth in competition with wild-type. In situ neutralizes the toxic effect of cognate toxin YeeF (PubMed:34280190). Probably neutralizes the ability to inhibit growth of cognate toxin YeeF. Probably does not have immunity protein activity on other LXG toxins (Probable).
Interacts with cognate toxin YeeF but not with non-cognate toxin YobL. The interaction probably inhibits the toxic activity of YeeF (PubMed:22200572). May bind with a stoichiometry of 2:2 to YeeF (By similarity).
Plays a central role in the sigma-K checkpoint which coordinates gene expression during the later stages of spore formation. The protease is activated by trans cleavage of the zymogen precursor producing SpoIVB-45 kDa. This undergoes further trimming by cis cleavage to form SpoIVB-43 kDa and SpoIVB-42 kDa. The protease then cleaves the C-terminus of the SpoIVFA metalloprotease activating the latter.
The PDZ domain mediates interaction with another SpoIVB protein during transactivation. Also mediates interaction with BofA during cleavage of SpoIVFA.
The zymogen is inhibited from undergoing autoactivation by BofC. The protease is inactivated by proteolytic cleavage.
Transcribed in low amounts by sigma-F. Transcribed during stage III of sporogenesis by sigma-G.
Belongs to the heme-copper respiratory oxidase family.
Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.
Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Co I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme a of subunit 1 to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer.
Forms fibers (PubMed:20080671, PubMed:29531041). Fibers have variable length and are 10-15 nm width (PubMed:20080671). Interacts with obg (AC P20964) in pull-down experiments (PubMed:12429099).
In laboratory strains, is a transition-phase protein that is expressed early in spore formation, as cells enter stationary phase (PubMed:10049401, PubMed:10368135, PubMed:10464223). Expression can occur as cells enter stationary phase even under sporulation-repressing conditions (PubMed:10464223).
Mutation impairs colony surface architecture (PubMed:16430695). Mutant forms pellicles with less extracellular material (PubMed:16430696). Deletion of the gene results in the production of asymmetric spores that accumulate misassembled material in one pole and have a greatly expanded undercoat and an altered outer coat structure (PubMed:10368135).
Part of the tapA-sipW-tasA operon (PubMed:10464223). Expression is directly repressed by the DNA-binding protein master regulator of biofilm formation SinR and activated by the extracellular matrix regulatory protein RemA (PubMed:16430695, PubMed:23646920). Also positively regulated by the sporulation transcription factors sigma H and Spo0A and repressed by the transition phase regulatory protein AbrB, probably indirectly (PubMed:10049401, PubMed:10368135, PubMed:10464223).
TasA is the major protein component of the biofilm extracellular matrix (PubMed:16430696, PubMed:20080671). It forms amyloid fibers that bind cells together in the biofilm (PubMed:20080671). Exhibits an antibacterial activity against a variety of Gram-positive and Gram-negative bacteria (PubMed:10049401). In laboratory strains, is also involved in proper spore coat assembly (PubMed:10368135).
Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.
Mycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH.
B.subtilis contains five chromosomal type I signal peptidases: SipS, SipT, SipU, SipV and SipW. They have different, but overlapping, substrate specificities and have different transcription patterns.
Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
May be involved in the production of the exopolysaccharide (EPS) component of the extracellular matrix during biofilm formation. EPS is responsible for the adhesion of chains of cells into bundles.
Belongs to the Rieske iron-sulfur protein family.
Component of the menaquinol:cytochrome c reductase complex. The Rieske protein is a high potential 2Fe-2S protein.
The main subunits of the menaquinol:cytochrome c complex are a Rieske-type iron-sulfur protein (QcrA), a cytochrome b (QcrB) and a cytochrome c (QcrC).
Forms a beta-barrel structure that may accommodate hydrophobic ligands.
Belongs to the bacterial ribosomal protein bL33 family.
Part of the 50S ribosomal subunit (PubMed:30126986). Interacts with VmlR (PubMed:30126986).
Activated by SigB in response to ethanol stress.
Specifically hydrolyzes gamma-D-glutamyl-L-lysine bonds in murein peptides, releasing L-Ala-D-Glu.
Binds 1 Mn(2+) or Fe(2+) ion per subunit.
Iron uptake repressor. Acts on the transcription of ferri-siderophore uptake genes.
Belongs to the LysR transcriptional regulatory family.
Could be a positive regulator of bsdBCD expression in response to salicylic acid.
Belongs to the SIS family. PHI subfamily.
By formaldehyde, under the control of HxlR. Not induced by methanol, formate, or methylamine.
Catalyzes the isomerization between 3-hexulose 6-phosphate and fructose 6-phosphate. Together with HxlA, may act as a formaldehyde detoxification system.
Negative regulator of FtsZ ring formation; modulates the frequency and position of FtsZ ring formation. Inhibits FtsZ ring formation at polar sites. Interacts either with FtsZ or with one of its binding partners to promote depolymerization.
Suppresses temperature-sensitive mutation in FtsZ, in a wild-type FtsZ background increases the number and alters the position of FtsZ rings (PubMed:10449747). In minimal medium cells elongate and occasionally form minicells. Double dynA-ezrA mutants have longer cells with more double septa than either deletion alone (PubMed:23249255).
Member of the two-component regulatory system DctS/DctR. Probably activates DctR by phosphorylation (By similarity). Essential for expression of dctP.
Preferentially expressed in cells competent for DNA transformation; that is 5-15% of the population (PubMed:17630974).
Belongs to the TrkH potassium transport family. Ktr (TC 2.A.38.4) subfamily.
Homodimer. Part of the KtrAB complex formed by an octameric catalytic ring of KtrA and a membrane associated dimer of KtrB forming a potassium channel.
Integral membrane subunit of the KtrAB potassium uptake transporter. The 2 major potassium transporter complexes KtrAB and KtrCD confer resistance to both suddenly imposed and prolonged osmotic stress.
Modulates the activity of the potassium/proton antiporter KhtU (PubMed:14987767). Involved in protection of the cell from methylglyoxal, a toxic by-product of glycolysis (PubMed:24330391).
Part of the khtSTU operon. Induced by salt stress at alkaline pH.
Belongs to the ATPase epsilon chain family.
F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c (Probable). The F(1)F(0) complex interacts with SpoIIIJ and YqjG; YqgA is found in the same complex.
F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c.
Produces ATP from ADP in the presence of a proton gradient across the membrane.
Belongs to the glutaminase PdxT/SNO family.
Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
In the presence of PdxS, forms a dodecamer of heterodimers. Only shows activity in the heterodimer.
Involved in branched-chain amino acid transport.
Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD).
Belongs to the glycosyl hydrolase 105 family.
Catalyzes the hydrolysis of unsaturated rhamnogalacturonan disaccharide to yield unsaturated D-galacturonic acid and L-rhamnose. It cannot act on unsaturated glucuronyl hydrolase (UGL) substrates containing unsaturated D-glucuronic acid at the non-reducing terminus, although the active pockets of YesR and UGL are very similar.
Up-regulated by growth on type I rhamnogalacturonan.
Activity is partially inhibited by the competence and sporulation stimulating factor (CSF), encoded by phrC (PubMed:9238025). Phosphatase activity is abolished in the presence of EDTA (PubMed:11923303). Insensitive to vanadate (PubMed:9843420).
Can also use Mg(2+), Ca(2+) and Zn(2+), with lower efficiency.
Homodimer (PubMed:11923303). Interacts with Spo0F (PubMed:9843420).
Involved in the regulation of sporulation (PubMed:8001132, PubMed:9843420). Acts as a phosphatase that specifically dephosphorylates the sporulation initiation phosphotransferase Spo0F and inhibits its activity (PubMed:8001132, PubMed:11923303, PubMed:9843420).
Belongs to the cytochrome ubiquinol oxidase subunit 1 family.
May have a role in sporulation. Can compensate for the loss of cytochrome aa3.
Catalyzes the deformylation of the formylaminopyrimidine N-formyl-4-amino-5-aminomethyl-2-methylpyrimidine (FAMP) to give the corresponding aminopyrimidine.
Belongs to the autoinducer-2 exporter (AI-2E) (TC 2.A.86) family.
The M ring may be actively involved in energy transduction.
The basal body constitutes a major portion of the flagellar organelle and consists of two rings, one in the peptidoglycan layer and one in the plasma membrane.
Belongs to the flagella basal body rod proteins family.
The basal body constitutes a major portion of the flagellar organelle and consists of four rings (L,P,S, and M) mounted on a central rod. The rod consists of about 26 subunits of FlgG in the distal portion, and FlgB, FlgC and FlgF are thought to build up the proximal portion of the rod with about 6 subunits each (By similarity).
The basal body constitutes a major portion of the flagellar organelle and consists of four rings (L,P,S, and M) mounted on a central rod. The rod consists of about 26 subunits of FlgG in the distal portion, and FlgB, FlgC and FlgF are thought to build up the proximal portion of the rod with about 6 subunits each.
Belongs to the amino acid-polyamine-organocation (APC) superfamily. L-type amino acid transporter (LAT) (TC 2.A.3.8) family.
Exhibits an obligate exchange activity for serine, threonine and aromatic amino acids.
Probably involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism.
Belongs to the SIMIBI class G3E GTPase family. ZNG1 subfamily.
No effect in wild-type, but required for optimal growth in strains lacking the ZnuABC zinc uptake system.
Zinc chaperone that directly transfers zinc cofactor to target proteins, thereby activating them (By similarity). Zinc is transferred from the CXCC motif in the GTPase domain to the zinc binding site in target proteins in a process requiring GTP hydrolysis (By similarity). Contributes to optimal growth under starvation for zinc (PubMed:12426338).
Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.
Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate.
In bacteria displays feedback inhibition by L-serine.
Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.
Catalyzes two reactions in de novo purine nucleotide biosynthesis. Catalyzes the breakdown of 5-aminoimidazole- (N-succinylocarboxamide) ribotide (SAICAR or 2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate) to 5-aminoimidazole-4-carboxamide ribotide (AICAR or 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide) and fumarate, and of adenylosuccinate (ADS or N(6)-(1,2-dicarboxyethyl)-AMP) to adenosine monophosphate (AMP) and fumarate (PubMed:15182182). Influences the affinity of glutamyl--tRNA ligase for its substrates and increases its thermostability.
Homotetramer. Residues from neighboring subunits contribute catalytic and substrate-binding residues to each active site.
Altered S5 proteins have been identified in a number of mutants. Some mutations in S5 have been shown to increase translational error frequencies.
Belongs to the universal ribosomal protein uS5 family.
Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body.
Part of the 30S ribosomal subunit (PubMed:30126986). Contacts proteins S4 and S8 (By similarity).
Part of the 30S ribosomal subunit. Contacts proteins S4 and S8.
The N-terminal domain interacts with the head of the 30S subunit; the C-terminal domain interacts with the body and contacts protein S4. The interaction surface between S4 and S5 is involved in control of translational fidelity.
With S4 and S12 plays an important role in translational accuracy.
With S4 and S12 plays an important role in translational accuracy; many suppressors of streptomycin-dependent mutants of protein S12 are found in this protein, some but not all of which decrease translational accuracy (ram, ribosomal ambiguity mutations).
Although strongly related to the 'phage' integrase family this protein lacks the conserved Tyr at position 318 suggesting it has no recombinase activity.
Deletion of the gene increases sensitivity to the amphomycin derivative MX2401, which binds UndP in the outer leaflet of the cytoplasmic membrane and prevents its recycling (PubMed:36450357). Deletion of the gene sensitizes B.subtilis to reduced levels of UndP synthesis (PubMed:36450357). The double mutant uptA-ykoX exhibits increased sensitivity to the amphomycin derivative MX2401, but has no discernible growth or morphological defects (PubMed:36450357).
Expression is regulated by the ECF sigma factor SigM.
Flippase that catalyzes the transport of undecaprenyl phosphate (UndP) across the cytoplasmic membrane, from the external side to the cytoplasmic side (PubMed:36450357). Is involved in UndP recycling during peptidoglycan synthesis (PubMed:36450357).
Belongs to the metallo-dependent hydrolases superfamily. TatD-type hydrolase family.
Binds 2 divalent metal cations per subunit.
Belongs to the D-alanine--D-alanine ligase family.
Binds 2 magnesium or manganese ions per subunit.
Asymmetrically hydrolyzes Ap4p to yield AMP and ATP.
Asymmetrically hydrolyzes Ap4p to yield AMP and ATP. Does not hydrolyze Ap2a or Ap6A. Also has an ATPase activity. Was shown to dephosphorylate phosphotyrosine but not phosphoserine or phosphothreonine from phosphorylated peptides. Involved in spore germination by controlling expression of genes coding for GerA and GerK receptors.
Nickel. 100-fold less efficiency with manganese.
Belongs to the 5'(3')-deoxyribonucleotidase family.
Dephosphorylates nucleoside monophosphates such as the 5' and 2'(3')-phosphates of deoxyribonucleotides in vitro. Also catalyzes the dephosphorylation of coenzyme A (CoA), pyridoxal-5'-phosphate (PLP), riboflavine-5-phosphate (FMN) and nicotinamide adenine dinucleotide phosphate (NADP) in vitro.
Belongs to the chorismate synthase family.
Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
Negatively regulated by the two-component system YycFG.
Belongs to the Mrp/NBP35 ATP-binding proteins family.
Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP.
Homodimer (By similarity). Interacts with BrxC (PubMed:33722570).
Negatively regulates the expression of hpr/scoC. The effect on hpr/scoC may be indirect.
C-terminal Cys can react with bacillithiol (BSH) to form mixed disulfides. S-bacillithiolation protects Cys residues against overoxidation by acting as a redox switch in response to oxidative stress.
S-bacillithiolation is the formation of mixed disulfide bonds between protein thiols and the general thiol reductant bacillithiol (BSH) under oxidative stress. BSH is an equivalent of glutathione (GSH) in Firmicutes. This protein is a NADPH-dependent bacilliredoxin reductase, which debacillithiolates (removes BSH) the S-bacillithiolated BrxB (BrxB-SSB), and to a lesser extent BrxC (BrxC-SSB). Involved in a redox cascade increasing the efficacy of BrxB function by reducing BrxB-SSB and thus reactivating it. Has NADPH-dependent oxidase activity under aerobic conditions producing hydrogen peroxide (H(2)O(2)).
Binds 1 heme c group covalently per subunit.
Induced during exponential growth. Repressed by glucose.
Present in very low amounts in the cell.
Catalyzes the NADPH-dependent reduction of scyllo-inosose (SIS) to scyllo-inositol (SI) in vitro, but is unable to dehydrogenate scyllo-inositol and myo-inositol. Is less efficient than the functional paralog IolW. Under physiological conditions, may primarily function as an NADPH-dependent oxidoreductase that reduces carbonyl group(s) in its substrates. Cannot use NADH instead of NADPH.
Is not induced in the presence of scyllo-inositol or myo-inositol.
Part of the bacABCDEFG operon responsible for the biosynthesis of bacilysin, an irreversible inactivator of the glutaminase domain of glucosamine synthetase. Catalyzes the formation of alpha-dipeptides from various L-amino acids in the presence of ATP. In vivo catalyzes the ligation of L-alanine and L-anticapsin (epoxycyclohexanonyl-Ala) to produce the final bacilysin antibiotic (L-Ala-L-4S-cyclohexenonyl-Ala dipeptide). The substrate specificity is restricted to small amino acids such as L-Ala, for the N-terminal end of the dipeptide, whereas a wide range of hydrophobic amino acids such as L-Phe, L-Tyr and L-Met are recognized for the C-terminal end.
The compound guanosine 5'-diphosphate 3'-diphosphate (ppGpp) is essential for the transcription of the bacABCDE operon and GTP regulates the transcription of both this operon and ywfH via the CodY-mediated regulation system.
Binding to DNA is allosterically inhibited by the effector glucosamine-6-phosphate (GlcN6P). N-acetylglucosamine-6-phosphate (GlcNAc6P) and glucose-6-phosphate (Glc6P) have no effect.
Transcriptional repressor of genes involved in glucosamine transport and utilization. Represses the expression of the gamAP operon by binding to the gamA-gamR intergenic region.
The phosphoserine observed at Ser-1003 in PubMed:17218307 may result from the secondary neutral loss of pantetheine from the phosphodiester linked cofactor.
Belongs to the chromate ion transporter (CHR) (TC 2.A.51) family.
Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
The spacing between the conserved Cys residues used for the 4Fe-4S cluster is unusual (C-X11-CXXC instead of C-X3-CXXC); it is therefore unclear whether this protein will bind the cofactor.
Belongs to the type III secretion exporter family.
May be involved in the export of flagellum proteins.
Required for formation of the rod structure in the basal body of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin.
Homodimer, upon Fe(2+) binding (PubMed:20087498). Interacts with the SufS/SufU complex (PubMed:27382962). Interacts with CpfC (PubMed:25826316).
Plays an essential role in iron intracellular trafficking to iron cofactor biogenesis systems including iron-sulfur cluster (Fe-S) or heme assembly (PubMed:21744456, PubMed:25826316). Promotes the biosynthesis of iron-sulfur clusters by delivering Fe to the complex composed of the cysteine desulfurase SufS and the zinc-dependent sulfurtransferase SufU (PubMed:27382962). Also plays a critical role in coproporphyrin-dependent heme b biogenesis and thus provides an essential function for the bacterial global metabolism.
Reduced growth in rich medium, unable to grow in minimal medium. Reduced activity of Fe-S-dependent aconitase (citB). Reactive oxygen species are drastically reduced. No bacillibactin (BB), an endogenous siderophore, produced. 20% higher intracellular iron concentrations.
Belongs to the MurCDEF family. MurF subfamily.
Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.
Expression is regulated by the sporulation transcription factor sigma G.
Cells lacking this gene are blocked in YukE secretion.
Cells lacking this gene exhibit significantly reduced growth in rich and minimal medium.
Monomer, homodimer or homotetramer; in equilibrium. Low salt concentration favors oligomerization, while high salt concentration favors the monomeric form.
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaB; this reaction does not require ATP in vitro. TsaE seems to play an indirect role in the t(6)A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD. Displays ATPase activity in vitro, which is modulated by the oligomeric status of the protein.
The four proteins YwlC, TsaD, TsaB and TsaE are necessary and sufficient for tRNA(NNU) t(6)A37 threonylcarbamoyladenosine biosynthesis in vitro in B.subtilis.
The well-known t(6)A modification appears to be a hydrolyzed artifact of natural cyclic t(6)A (ct(6)A) that occurs during the preparation and handling of tRNA in B.subtilis and many other species (PubMed:23242255). In these species, the t(6)A modification is processed further by dehydration into ct(6)A, a reaction catalyzed by TcdA.
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.
Belongs to the small heat shock protein (HSP20) family.
Deletion of the gene increases sensitivity toward salt stress.
Forms homodimers, homotetramers and higher oligomers.
Part of the cellular protein quality control system with a specific role in salt stress response. May facilitate protein homeostasis, together with chemical chaperones that accumulate during the salt stress response. Increased levels of YocM protects against both heat and salt stress. In vitro, displays an unusual aggregase chaperone activity.
Induced by lichenan, lichenan hydrolysate and cellobiose. Subject to carbon catabolite repression.
The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane.
The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. This system is involved in lichenan transport.
Belongs to the concentrative nucleoside transporter (CNT) (TC 2.A.41) family.
Induced by deoxyadenosine and thymidine. Repressed by DeoR and glucose.
Transport of the pyrimidine nucleoside uridine.
Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). It confers resistance to triclosan.
Cells lacking this gene exhibit a 250-fold decrease in the triclosan MIC.
Cells lacking this gene have no defect in lipoteichoic acid or wall teichoic acid synthesis.
Cells lacking this gene are unable to grow with mannose as the sole carbon source.
Positively regulates the expression of the mannose operon that consists of three genes, manP, manA, and yjdF, which are responsible for the transport and utilization of mannose. Also activates its own expression.
The regulatory activity of ManR is modulated by phosphorylation and dephosphorylation of the various ManR domains. It becomes activated via phosphoryl group transfer from PEP, EI and HPr on the two conserved histidine residues in the PRD 2 domain, whereas phosphorylation of the EIIA-like domain on His-570 by the PTS EIIB-Man domain of ManP inactivates ManR (PubMed:23551403).
Up-regulated by mannose. Is subject to carbon catabolite repression (CCR) by glucose.
YkvU and stoA are cotranscribed under the control of sigma E.
Belongs to the 5-formyltetrahydrofolate cyclo-ligase family.
Belongs to the HAD-like hydrolase superfamily. Cof family.
Catalyzes the dephosphorylation of the riboflavin precursor 5-amino-6-(5-phospho-D-ribitylamino)uracil and of flavin mononucleotide (FMN) in vitro (PubMed:26316208).
Probably part of the binding-protein-dependent transport system YurMNO. Probably responsible for the translocation of the substrate across the membrane.
Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division (By similarity).
Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division.
Belongs to the ZapA family. Type 2 subfamily.
Homodimer. Interacts with FtsZ (By similarity).
Homodimer. Homodimerization may be required to stabilize the binding of ScpA to the Smc head domains. Component of a cohesin-like complex composed of ScpA, ScpB and the Smc homodimer, in which ScpA and ScpB bind to the head domain of Smc. The presence of the three proteins is required for the association of the complex with DNA.
Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpA that pull DNA away from mid-cell into both cell halves.
Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate.
Belongs to the aspartate/glutamate racemases family.
Provides the (R)-glutamate required for cell wall biosynthesis.
Acetyl-CoA carboxylase is a heterohexamer of biotin carboxyl carrier protein, biotin carboxylase and the two subunits of carboxyl transferase in a 2:2 complex.
Leu-235 is present instead of the conserved His which is expected to bind ATP.
This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
Activated by SigB in response to stress due to ethanol.
May contribute to protect cells against stress due to ethanol and related compounds.
Appears to be involved in spore cortex formation.
Could be the product of a pseudogene. The N-terminus is about 275 residues shorter than orthologs.
Belongs to the enoyl-CoA hydratase/isomerase family.
Required for production of the modified peptide YydF (Probable). May process the precursor form of YydF to release the active peptide (Potential).
Suggested to be part of an ABC transporter complex YydIJ involved in export of the modified peptide YydF.
The complex is composed of 2 ATP-binding proteins (YydI), two transmembrane proteins (YydJ).
Belongs to the histone deacetylase family.
Monomer. Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits.
Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Part of the ABC transporter complex TcyJKLMN involved in L-cystine import. Is also involved in cystathionine, djenkolate, and S-methylcysteine transport.
Required for production of the modified peptide YydF (Probable). May activate a metalloenzyme (Potential).
Belongs to the ATP-dependent AMP-binding enzyme family. DltA subfamily.
Catalyzes the first step in the D-alanylation of lipoteichoic acid (LTA), the activation of D-alanine and its transfer onto the D-alanyl carrier protein (Dcp) DltC. In an ATP-dependent two-step reaction, forms a high energy D-alanyl-AMP intermediate, followed by transfer of the D-alanyl residue as a thiol ester to the phosphopantheinyl prosthetic group of the Dcp. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall.
Allows the coupling of early and late flagellar synthesis through the repression of RNA polymerase sigma-D factor-dependent transcription.
Belongs to the bacterial solute-binding protein 8 family.
Induced by iron starvation, repressed by fur.
Part of the ABC transporter complex YfiYZ/YfhA/YusV involved in import of the iron-hydroxamate siderophores schizokinen, arthrobactin and corprogen. Binds the siderophores and delivers them to the surface of YfiZ/YfhA (Probable).
Strains lacking this gene show a reduction in growth stimulation by the iron-hydroxamate siderophores schizokinen and arthrobactin compared to wild-type.
The complex is composed of one ATP-binding protein (YusV), two transmembrane proteins (YfiZ and YfhA) and a solute-binding protein (YfiY). Interacts with FloT (PubMed:23651456).
Belongs to the short-chain dehydrogenases/reductases (SDR) family. FabI subfamily.
Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism.
Is expressed only during vegetative growth.
Sporulation is not significantly affected.
Belongs to the glycosyltransferase 4 family.
Catalyzes the formation of undecaprenyl-PP-N-acetylglucosamine. Involved in the synthesis of anionic cell-wall polymers as it mediates the initiation of the linkage unit formation that appears to be common to the two types of teichoic acids attached to the peptidoglycan of B.subtilis; may also be involved in teichuronic acid biosynthesis (Probable).
Belongs to the universal ribosomal protein uL3 family.
One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit (By similarity). Strongly stimulates 23S rRNA precursor processing by mini-ribonuclease 3 (MrnC); 20-30% DMSO can replace L3, suggesting the protein may alter rRNA conformation.
One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
Part of the 50S ribosomal subunit (PubMed:30126986). Forms a cluster with proteins L14 and L19 (By similarity). Interacts with RNA helicase CshA (PubMed:23175651).
Part of the 50S ribosomal subunit. Forms a cluster with proteins L14 and L19.
Homotrimer (PubMed:17001076, PubMed:25691471). Under poor nitrogen source such as nitrate, the complex between GlnK and AmtB, which are the transmembrane ammonium transporter and its cognate regulator, respectively, interacts with TnrA (PubMed:17001076, PubMed:21435182, PubMed:25691471). GlnK-ATP complex are not able to bind TnrA (PubMed:21435182).
In the absence of nitrogen source, cells lacking this gene do not show degradation of TnrA, which is entirely soluble.
Member of the two-component regulatory system GlnK/GlnL that positively regulates the expression of the glsA-glnT operon in response to glutamine (PubMed:11717295, PubMed:15995196). It seems that autophosphorylated GlnK transfers a phosphoryl group to GlnL, which positively regulates the expression of the glsA-glnT operon (PubMed:11717295, PubMed:15995196). Interaction between GlnK-AmtB complex and TnrA protects TnrA from proteolytic degradation (PubMed:17001076, PubMed:21435182).
Detected in exponentially growing cells, the 50 and 30 kDa processing products disappear upon entry into stationary phase with the concomitant appearance of a 20 kDa products. The 50 kDa form persists in the absence of extracellular proteases (PubMed:11987133).
Disruption of the cwlO gene affects neither the vegetative cell growth rate, cell morphology, motility, sporulation frequency nor the germination frequency.
Expressed during the early stage of the vegetative growth phase (PubMed:16233686). Not detected in stationary phase (PubMed:11987133).
Identified in the extracellular proteome as a number of processing products of about 50 and 30 kDa.
Positively regulated by the two-component system YycFG.
The C-terminal part of CwlO shows a cell wall hydrolytic DL-endopeptidase activity.
The N-terminal part of CwlO was shown to have no cell wall-binding activity.
Expression controlled by a sigma-E-regulated promoter which needs the sigma-E factor for the binding of the RNA polymerase and subsequent transcription.
Member of the two-component regulatory system NatK/NatR that positively regulates the expression of the natAB operon. Potentially phosphorylates NatR.
Belongs to the cytidine and deoxycytidylate deaminase family.
Catalyzes the deamination of adenosine to inosine at the wobble position 34 of tRNA(Arg2).
In cells missing this gene some GerQ multimers are present, indicating that tgl is not essential. Heat treatment for 20 minutes at 60 degrees Celsius, which maximally activates the Tgl enzymatic activity, causes cross-linking of GerQ in isolated yabG-deleted spores but not in tgl/yabG double-mutant spores. Additionally, the germination frequency of the tgl/yabG double-mutant spores in the presence of L-alanine with or without heat activation at 60 degrees Celsius is lower than that of wild-type spores.
Probably plays a role in the assembly of the spore coat proteins by catalyzing epsilon-(gamma-glutamyl)lysine cross-links.
Probably plays a role in the assembly of the spore coat proteins by catalyzing epsilon-(gamma-glutamyl)lysine cross-links. In wild-type spores at 37 degrees Celsius, tgl mediates the cross-linking of GerQ in higher molecular mass forms, probably in cooperation with YabG.
Probably a dodecamer composed of six biotin-containing alpha subunits and six beta subunits.
Expression is induced by bacitracin, via the two-component regulatory system BceS/BceR.
Part of the ABC transporter complex BceAB (TC 3.A.1.123.5) involved in bacitracin export. Responsible for energy coupling to the transport system.
The complex is composed of two ATP-binding proteins (BceA) and two transmembrane proteins (BceB).
Belongs to the radical SAM superfamily. SPL family.
Binds 1 S-adenosyl-L-methionine per subunit.
Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Expressed at stage III of sporulation in the forespore compartment of the developing sporangium.
Involved in repair of UV radiation-induced DNA damage during spore germination. Can repair thymine dimer 5-thyminyl-5,6-dihydrothymine (known as spore photoproduct (SP)) by in situ monomerization of SP to two thymines.
Belongs to the bacterial ribosomal protein bL28 family.
Accelerates the release of ammonia from reactive enamine/imine intermediates of the PLP-dependent threonine dehydratase (IlvA) in the low water environment of the cell. It catalyzes the deamination of enamine/imine intermediates to yield 2-ketobutyrate and ammonia. It is required for the detoxification of reactive intermediates of IlvA due to their highly nucleophilic abilities. Involved in the isoleucine biosynthesis.
Was originally (PubMed:10368157) thought to have a role in the purine repressor-mediated regulation of purA or the pur operon. The effect of yabJ (now ridA) on regulation of purA was due to the orientation of the marker gene downstream of purR in the yabJ mutant strain used in PubMed:10368157.
Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2B subfamily.
Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
Involved in the biosynthesis of pulcherrimin, a red extracellular pigment. It uses activated amino acids in the form of aminoacyl-tRNAs (aa-tRNAs) as substrates to catalyze the ATP-independent formation of cyclodipeptides which are intermediates in diketopiperazine (DKP) biosynthetic pathways. Catalyzes the formation of cyclo(L-Leu-L-Leu) (cLL) from L-leucyl-tRNA(Leu). Can also incorporate various nonpolar residues, such as L-phenylalanine, L-leucine and methionine, into cyclodipeptides.
B.subtilis possesses two minimal, substrate-specific, Tat translocases: TatAd-TatCd and TatAy-TatCy, each one composed of a TatA and a TatC protein. TatA is bifunctional and performs the function of both the TatA and TatB proteins of Gram-negative organisms.
Depletion of TatCd results in a drastic reduction of TatAd.
Expressed under conditions of phosphate starvation.
Forms a complex with TatAd. Two types of complexes exist: one composed of TatAd and TatCd, and another composed only of TatAd.
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes.
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Required for PhoD secretion. TatCd promotes membrane localization of TatAd via domain specific interactions. TatCd is required for stabile production of TatAd as well as for its maintenance.
Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated.
This enzyme catalyzes only one turnover and therefore is not strictly catalytic. According to one definition, an enzyme is a biocatalyst that acts repeatedly and over many reaction cycles.
Up-regulated by methylated AdaA in response to the exposure to alkylating agents such as MNNG.
Interacts (via N-terminal region) with GTP-bound FlhF homodimer (via NG domain).
Involved in the placement and assembly of flagella (By similarity). Activates the SRP-GTPase activity of FlhF.
Belongs to the prolyl-tRNA editing family. YbaK/EbsC subfamily.
Cells lacking this gene show a growth-defective phenotype under copper deprivation as well as a reduced intracellular content of copper.
Highly induced under copper-limiting conditions. Down-regulated by YcnK, especially under high copper concentrations. Down-regulated by CsoR.
In the C-terminal section; belongs to the CopD family.
In the N-terminal section; belongs to the CopC family.
Involved in uptake of extracellular oxidized copper under copper-limiting conditions.
Antitoxin component of a type II toxin-antitoxin (TA) system. Antitoxin that binds cognate toxin SpoIISA and neutralizes its toxic activity; unlike most antitoxins it does not seem to be highly labile upon expression in E.coli.
Belongs to the SpoIISB antitoxin family.
Decreases sporulation efficiency by 4 orders of magnitude. A double spoIISA-spoIISB disruption sporulates normally, suggesting its only role is to neutralize SpoIISA.
Expressed during exponential growth and sporulation. A member of the spoIISA-spoIISB operon, it also has its own promoter.
The isolated protein is unfolded; X-ray data suggests the inactive complex forms a heterotetramer of SpoIISA(2)-SpoIISB(2), which inactivates the toxic activity of SpoIISA.
Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism.
Probable thioesterase involved in the biosynthesis of surfactin.
Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35) family.
Homopentamer. In the absence of Mg(2+), interactions between subunits are weakened, and dimers, trimers and tetramers can be observed in vitro (By similarity). Homotetramer (PubMed:15231793).
Mediates influx of magnesium ions. Alternates between open and closed states. Activated by low cytoplasmic Mg(2+) levels. Inactive when cytoplasmic Mg(2+) levels are high.
The central ion permeation pathway is formed by the first transmembrane domain from each of the five subunits. Mg(2+) binding strengthens interactions between subunits and leads to the formation of a symmetrical homopentamer surrounding a closed ion permeation pathway. Low Mg(2+) concentrations trigger both a conformation change within each subunit and a loosening of the interactions between subunits. This results in an open ion conduction pathway. In addition, this results in a less symmetrical shape of the whole complex.
Involved in the system for phosphate transport across the cytoplasmic membrane.
Part of the ABC transporter complex PstSACB involved in phosphate import.
Belongs to the ABC-4 integral membrane protein family.
Part of the ABC transporter complex YxdLM which could be involved in peptide resistance.
The complex is composed of two ATP-binding proteins (YxdL) and two transmembrane proteins (YxdM).
Transcriptionally regulated by YxdJ. Induced by the antibacterial protein LL-37, probably via YxdJ.
Cotranscribed with sigma-M and yhdK. YhdL and yhdK negatively regulate sigma-M.
The N-terminus of YhdL interacts with sigma-M. YhdL interacts specifically with YhdK.
Cells lacking this gene show up-regulated sigma X activity.
Belongs to the iron/manganese superoxide dismutase family.
By heat shock, salt stress, oxidative stress, glucose limitation and oxygen limitation.
Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Belongs to the class-I aminoacyl-tRNA synthetase family.
Belongs to the transferase hexapeptide repeat family.
Catalyzes the acetylation of serine by acetyl-CoA to produce O-acetylserine (OAS).
Belongs to the IPP isomerase type 2 family.
Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP).
Probably part of an ABC transporter complex.
The complex is composed of two ATP-binding proteins (YvrA), two transmembrane proteins (YvrB) and a solute-binding protein (YvrC).
Belongs to the carbohydrate kinase PfkB family.
Catalyzes the phosphorylation of 5-dehydro-2-deoxy-D-gluconate (2-deoxy-5-keto-D-gluconate or DKG) to 6-phospho-5-dehydro-2-deoxy-D-gluconate (DKGP).
Belongs to the metallo-beta-lactamase superfamily. Glyoxalase II family.
Inhibition of RapA requires a free carboxylate group at the C-terminal end of the PhrA pentapeptide (PubMed:11587784). A free C-terminal carboxylic acid PhrA pentapeptide inhibits RapA phosphatase activity at a 1:1 ratio and is approximately 200 fold more active than a C-terminal amide peptide (PubMed:11587784).
Interacts with RapA and inhibits its interaction with Spo0F.
Secreted with a propeptide domain, which is cleaved in the cell wall by the secreted serine proteases subtilisin and Vpr to produce a mature signaling peptide (PubMed:17666034). Contains a predicted signal peptide cleavage site in the N-terminal region, however the propeptide is probably subject to only one processing event, at the N-terminal end of the mature peptide (Probable).
Signaling molecule involved in the regulation of sporulation (PubMed:8643670, PubMed:9238025). Secreted during production, but the mature peptide acts intracellularly, indicating that it needs to be imported into the cell to function (PubMed:9200610, PubMed:8643670, PubMed:9238025). Inhibitor of the RapA phosphatase activity (PubMed:8643670, PubMed:9238025, PubMed:11923303, PubMed:22267516). Does not act on RapB (PubMed:9238025).
Belongs to the bacterial ribosomal protein bS20 family.
Belongs to the universal ribosomal protein uS14 family.
Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site.
Contacts proteins S3 and S10 (By similarity). Part of the 30S ribosomal subunit.
Non-essential protein. A second form of uS14, it can integrate into the 30S subunit where it partially compensates for loss of the major uS14 protein (AC P12878) in restoring 70S formation, although it does not seem to be incorporated into the ribosome as well as the major uS14.
Part of the 30S ribosomal subunit. Contacts proteins S3 and S10.
Repressed by the zinc-specific metallo-regulatory protein zur.
Belongs to the SecD/SecF family. SecD subfamily.
Belongs to the SecD/SecF family. SecF subfamily.
Cells lacking this gene show a cold-sensitive phenotype and a filamentous morphology.
Forms a complex with SecD. Part of the essential Sec protein translocation apparatus which comprises SecA, SecYEG and auxiliary proteins SecDF. Other proteins may also be involved.
Forms a complex with SecF. Part of the essential Sec protein translocation apparatus which comprises SecA, SecYEG and auxiliary proteins SecDF. Other proteins may also be involved.
In the C-terminal section; belongs to the SecD/SecF family. SecF subfamily.
In the N-terminal section; belongs to the SecD/SecF family. SecD subfamily.
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA (By similarity).
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Part of the essential Sec protein translocation apparatus which comprises SecA, SecYEG and auxiliary protein SecDF. Other proteins may also be involved (By similarity).
Required for efficient translocation of secretory pre-proteins under conditions of hypersecretion but is not required for the release of mature proteins from the membrane.
Shows maximal expression at the beginning of post-exponential growth phase and increased expression by glucose in the post-exponential growth phase when cells are cultured on rich medium. Expressed constitutively during growth in minimal medium.
Member of the two-component regulatory system ResD/ResE involved in the global regulation of aerobic and anaerobic respiration. Probably phosphorylates ResD.
Oligomerizes, probably forms homodimers. Interacts in vivo with FloT, colocalizes with FloT-only membrane rafts. Oligomerization is assisted by FloT (PubMed:26297017, PubMed:25909364). Another study shows only minor colocalization with FloT membrane assemblies (PubMed:27362352).
Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
Expression is controlled by a sigma-E-regulated promoter which needs the sigma-E factor for the binding of the RNA polymerase and subsequent transcription.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family.
Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
Bifunctional enzyme with both malic and malolactic enzyme activities (PubMed:33824210). In the absence of NADPH, catalyzes the reversible decarboxylation of malate to pyruvate (PubMed:16788182, PubMed:33824210). Can use NAD and NADP, but with a very strong preference for NADP (PubMed:16788182). In the presence of excess NADPH, catalyzes the non-oxidative decarboxylation of malate to lactate (PubMed:33824210). During growth on glucose, contributes to NADPH balancing via oxidation of the NADPH produced in excess by other enzymatic reactions (PubMed:33824210). Can also catalyze the decarboxylation of oxaloacetate (PubMed:16788182).
Divalent metal cations. Prefers magnesium or manganese.
Mutant shows wild-type growth on glucose but a much slower growth rate on malate, fumarate, or succinate plus glutamate (PubMed:16788182). Overexpression of the other three malic enzymes, mleA, maeA or malS cannot compensate for the ytsJ deletion (PubMed:16788182). The ATP concentrations in the mutant grown in minimal medium with glucose are similar to the wild-type level. ATP concentrations decrease by about 20% in malate minimal medium (PubMed:23136871). NADPH overproduction is virtually abolished in the deletion mutant (PubMed:33824210).
NADPH is a strong modulator that switches activity from a pyruvate-producing malic enzyme to a lactate-generating malolactic enzyme.
Transcribed at a high level under all of the conditions tested.
Probably involved in ribonucleotide reductase function.
Belongs to the RNA polymerase beta chain family.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
RNAP is composed of a core of 2 alpha, a beta and a beta' subunit. The core is associated with a delta subunit, and at least one of epsilon or omega (PubMed:6802805, PubMed:18289874, PubMed:21710567). When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription (PubMed:18289874).
The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta' and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription.
Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines.
Belongs to the azoreductase type 1 family.
Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones (Probable). Contributes to resistance to 2-methylhydroquinone (2-MHQ) and catechol (PubMed:18208493).
Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones.
Repressed by YodB. Induced by thiol specific stress conditions, such as exposure to 2-methylhydroquinone (2-MHQ), catechol or diamide. Not induced by oxidative stress due to hydrogen peroxide.
Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.
Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction. Appears to favor the formation of acetate. Involved in the secretion of excess carbohydrate.
Induced by glucose excess, the induction may be mediated by CcpA transcriptional regulator.
Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Belongs to the type III pantothenate kinase family.
Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis. Cannot utilize a phosphoryl donor other than ATP.
Monovalent cations. Ammonium or potassium.
Not regulated by feedback inhibition by CoA and its thioesters as described for many other pantothenate kinases. Not inhibited by N-pentylpantothenamide (N5-Pan), and this compound cannot act as a substrate either.
Belongs to the GHMP kinase family. Homoserine kinase subfamily.
Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Interacts with PcrA. The interaction is not essential for cell viability or repair of UV-induced lesions.
Belongs to the phage portal family. PBSX subfamily.
Belongs to the isocitrate lyase/PEP mutase superfamily. Methylisocitrate lyase family.
Catalyzes the thermodynamically favored C-C bond cleavage of (2R,3S)-2-methylisocitrate to yield pyruvate and succinate.
Involved in the methylcitric acid cycle. Catalyzes the cleavage of 2-methylisocitrate to yield pyruvate and succinate.
Belongs to the LytR/CpsA/Psr (LCP) family.
May catalyze the final step in cell wall teichoic acid biosynthesis, the transfer of the anionic cell wall polymers (APs) from their lipid-linked precursor to the cell wall peptidoglycan (PG).
Single mutant has no effect on cell growth or morphology under normal growth conditions. Triple disruption of tagTUV genes is not viable.
Belongs to the glycosyltransferase 2 family. GtrB subfamily.
Positively regulated by WalR. Expressed mainly during exponential growth and rapidly shut off as cells enter the stationary phase.
Belongs to the bacterial ribosomal protein bS21 family.
Belongs to the ketopantoate reductase family.
Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
Belongs to the eukaryotic ribosomal protein eL8 family.
Found associated with the 50S subunit of the ribosome during exponential growth but not during stationary phase.
None; has no effect on viability, growth or sporulation at low, normal or elevated temperatures.
RNA-binding protein that recognizes the K-turn motif present in ribosomal RNA, but also in box C/D and box C'/D' sRNAs.
May act as a pilot protein, directing MinCD to the polar septation sites or by inhibiting MinCD at the midcell site of division. Required for polar localization of the chromosome during sporulation.
Misplacement of the septum during cell division, resulting in the formation of small, circular, anucleate minicells.
Oligomers. Interacts with FtsZ, MinD, MinJ and Spo0J. The association with Spo0J is transient and occurs at a specific point during development.
Member of the two-component regulatory system YesM/YesN.
Belongs to the CitM (TC 2.A.11) transporter family.
Transports the free citrate anion. Probably cotransports citrate and at least three or four protons. The citrate uptake is inhibited by the presence of magnesium ions.
Cell wall hydrolase that cleaves gamma-D-glutamate-meso-diaminopimelate bonds in peptidoglycan. LytF is necessary and sufficient for vegetative daughter cell separation, and also seems to play a role in cell autolysis.
Cells from an undomesticated strain (3610) lacking this gene grow predominantly as chains, whereas wild-type cells grow as separate individuals. They do not show a reduction in the rate of swarming motility.
Expressed in the vegetative growth phase under exclusive control of sigma-D (SigD). Expression of lytF is heterogeneous in the exponentially growing cell population; it is ON in single cells and OFF in long chains. The same subpopulation of cells that express lytF also express flagellin.
In domesticated laboratory strains (168 and derivatives), lytF is not expressed in a majority of the growing cells. These cells form a subpopulation that grows in multicellular, nonmotile chains. Undomesticated strains (3610) express lytF in a majority of the population, that grows as separate individual motile cells (PubMed:19542270).
Is inhibited in vitro by para-hydroxymercuribenzoate, a sulfydryl inhibitor.
The N-terminal domain contains LysM domains that are thought to be involved in peptidoglycan binding, while the C-terminal domain is endowed with the catalytic activity.
Degrades abnormal exported proteins and responsible for the propeptide processing of a natural pro-protein and for the maturation of a native protein. It also plays a prominent role in stress (heat shock, ethanol, puromycin and NaCl) resistance during active exponential growth (Probable).
In contrast to other bacteria, in which inactivation of serine protease leads to thermosensitivity, inactivation of HtrB leads to an increased thermotolerance and an increased tolerance to hydrogen peroxide. Inactivation of both HtrA and HtrB leads to growth defects and to thermosensitivity.
Inactivation results in compensating overexpression of YkdA, especially during stress conditions.
Induced by heat shock during exponential growth and by heterologous amylases at the transition phase of the growth cycle. Negatively regulates its own expression.
By ferulic, p-coumaric and caffeic acids (at protein level) (PubMed:9546183). Cells extracts from caffeic acid-induced cells exhibited lower activity on the three acids, which indicates that caffeic acid could be a less efficient inducer (PubMed:9546183). Up-regulated by salicylate (PubMed:17295427).
Involved in the decarboxylation and detoxification of phenolic derivatives. It is able to catalyze the decarboxylation of ferulic, p-coumaric and caffeic acids.
No longer metabolizes ferulic acid (PubMed:26658822).
Might be involved in the polymerization of teichuronic acid repeating units after their translocation to the outer surface of the membrane.
The nature of the anionic polymer present in the cell wall of B.subtilis depends on phosphate availability. Under phosphate-replete growth conditions teichoic acids are present, whereas under phosphate-depleted conditions, at least part of the wall teichoic acid is replaced with teichuronic acid, a non-phosphate containing anionic polymer. The synthesis of teichuronic acid is accompanied by degradation of teichoic acid and reutilization of liberated phosphate for other cellular processes such as nucleic acid synthesis.
Belongs to the peptidase M20A family. N-acetyldiaminopimelate deacetylase subfamily.
Catalyzes the conversion of N-acetyl-diaminopimelate to diaminopimelate and acetate.
Cells lacking this gene are unable to grow with mannose as the sole carbon source. Deletion of manP results in constitutive expression from both the manP and manR promoters, indicating that the phosphotransferase system (PTS) component EII-Man has a negative effect on regulation of the mannose operon and manR.
The EIIA domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the EIIB domain.
The EIIB domain is phosphorylated by phospho-EIIA on a cysteinyl or histidyl residue, depending on the transported sugar. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the EIIC domain. The EIIB domain is also able to transfer its phosphoryl group to a specific histidine residue in ManR, which leads to its inactivation.
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in mannose transport.
Up-regulated by mannose. Is under the control of ManR. Is subject to carbon catabolite repression (CCR) by glucose. Forms part of an operon with manA and yjdF.
Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily.
Member of the two-component regulatory system DegS/DegU, which plays an important role in the transition growth phase. Involved in the control of expression of different cellular functions, including production of degradative enzymes such as the neutral and alkaline proteases, flagellum formation, biofilm formation, and competence for DNA uptake. Positively or negatively regulates expression of many different genes. The phosphorylated form is required for synthesis of degradative enzymes, flagellum formation and biofilm formation. The unphosphorylated form is required for expression of genetic competence, via induction of comK.
Phosphorylated DegU activates its own expression.
Phosphorylated and dephosphorylated by DegS.
Phosphorylated and unphosphorylated forms are both active and have different functions. A low concentration of phospho-DegU is sufficient to activate transcription of flagellar genes, but a higher concentration of phospho-DegU is required for transcription of other genes. Phosphorylated DegU is stabilized by DegR.
The N-terminal region acts as an inhibitor, whereas the C-terminal region carries enhancing activity.
Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
Contains 1 molecule of FAD per monomer. The role of this cofactor is not clear considering that the reaction does not involve redox chemistry (By similarity).
Nitric oxide-responsive transcriptional regulator. It represses the expression of flavohemoprotein hmp and the nitrite reductase nasD. Probably plays a role in the up-regulation of the resDE regulon in the presence of nitric oxide.
Interacts with a complex composed of YknX, YknY and YknZ.
Part of an unusual four-component transporter, which is required for protection against the killing factor SdpC (sporulation-delaying protein). Has a role in the assembly of the YknXYZ complex.
Disruption results in severely reduced transformation frequency, but has no detectable effect on either the frequency or the location of division septa.
Required for post-transcription initiation control of the comE operon. Promotes the accumulation of its target comE mRNA to septal and polar sites.
Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.
Encoded in a 48-kb, phage-like element known as skin.
The antisense RNA ratA acts as an antitoxin by annealing to the mRNA of txpA and causing its degradation, protecting the cell from TxpA by blocking the production of the toxin. A type I toxin-antitoxin (TA) system, where expression of the proteinaceous toxin is controlled by an antisense sRNA.
Toxic component of a type I toxin-antitoxin (TA) system (PubMed:16166525). Overexpression of txpA causes cell lysis; the TxpA protein has been suggested to act on the cell membrane or might possibly block cell wall synthesis (PubMed:16166525). Overexpression in E.coli is not toxic (PubMed:16166525).
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB; this reaction does not require ATP in vitro. TsaD likely plays a direct catalytic role in this reaction.
Transcriptional repressor of xylose-utilizing enzymes.
Cells lacking this gene show only slightly increased sensitivity to DNA-damaging agents. However, cells lacking RecJ and with a mutated AadAB enzyme were extremely sensitive to these agents, as sensitive as recA deletion strains. The doubly mutated strain shows 10-fold impaired growth in the absence of these agents.
Putative single-stranded-DNA-specific exonuclease (By similarity). RecA thread formation during DNA double-strand break repair requires RecJ or AadAB.
Each stator complex is composed of 4 MotA and 2 MotB subunits. 2 A subunits and 1 B subunit are thought to form a single ion channel, so that each stator complex contains two channels (By similarity).
MotA and MotB comprise the stator element of the flagellar motor complex. Required for the rotation of the flagellar motor. Might be a linker that fastens the torque-generating machinery to the cell wall (By similarity).
Belongs to the cytochrome c oxidase bacterial subunit 4 family.
Belongs to the UDP-N-acetylglucosamine 2-epimerase family.
Catalyzes the conversion of UDP-N-acetylglucosamine into UDP-N-acetylmannosamine, a precursor of the teichoic acid linkage unit.
Belongs to the universal ribosomal protein uS3 family.
Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation.
Part of the 30S ribosomal subunit (PubMed:30126986). Forms a tight complex with proteins S10 and S14 (By similarity).
Part of the 30S ribosomal subunit. Forms a tight complex with proteins S10 and S14.
Belongs to the prephenate decarboxylase family.
Part of the bacABCDEF operon responsible for the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin, composed of L-alanine and L-anticapsin. Bacilysin is an irreversible inactivator of the glutaminase domain of glucosamine synthetase (PubMed:15609023, PubMed:20052993). BacA is an unusual prephenate decarboxylase that avoids the typical aromatization of the cyclohexadienol ring of prephenate (PubMed:20052993)(PubMed:22483065). BacA catalyzes the protonation of prephenate (1-carboxy-4-hydroxy-alpha-oxo-2,5-cyclohexadiene-1-propanoic acid) at C6 position, followed by a decarboxylation to produce the endocyclic-delta(4),delta(8)-7R-dihydro-hydroxyphenylpyruvate (en-H2HPP) (PubMed:20052993, PubMed:22483065, PubMed:22765234). En-H2HPP is able to undergo a slow nonenzymatic isomerization to produce the exocyclic-delta(3),delta(5)-dihydro-hydroxyphenylpyruvate (ex-H2HPP) (PubMed:20052993)(PubMed:22483065). BacA isomerizes only the pro-R double bond in prephenate (PubMed:22483065).
The compound guanosine 5'-diphosphate 3'-diphosphate (ppGpp) is essential for the transcription of the bacABCDEF operon and BacG, and GTP regulates the transcription of both this operon and ywfH via the CodY-mediated regulation system.
Belongs to the class I-like SAM-binding methyltransferase superfamily. TrmB family.
Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Negatively regulated by an overlapping cis-acting antisense RNA which itself is positively regulated by extracytoplasmic sigma factors SigM and SigX; when both sigma factors are deleted expression of the yabE mRNA is detected.
No visible phenotype during recovery from stationary phase or sporulation efficiency.
Suggested to be involved in cell wall modification.
Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
Cells lacking this gene do not grow on minimal medium or on 4-methyl-5-(2-hydroxyethyl) thiazole, a thiamine precursor molecule. They do not synthesize 2-methyl-4-amino-5-hydroxymethylpyrimidine.
Repressed by thiamine and 2-methyl-4-amino-5-hydroxymethylpyrimidine.
Association with RNAP core increases during H(2)O(2), NaOH, rifampicin stress and during sporulation (at protein level).
Monomer (PubMed:7602586). Interacts transiently with the RNAP core (Probable).
Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released. This alternative sigma factor is required for the transcription of the flagellin and motility genes as well as for wild-type chemotaxis. Associates with the RNAP core during all growth phases with a peak at the transition to stationary phase (PubMed:21710567).
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released.
Seems to be required for the assembly of the CotSA protein in spores.
Contains an N-terminal nucleotide-binding domain and a C-terminal acceptor-binding domain.
Glycosyltransferase implicated in the synthesis of the spore coat.
Belongs to the PTPS family. QueD subfamily.
Catalyzes the conversion of 7,8-dihydroneopterin triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde.
The active site is at the interface between 2 subunits. The proton acceptor Cys is on one subunit, and the charge relay system is on the other subunit (By similarity).
Positively regulates the expression of ytmI operon in response to the availability of sulfur sources.
Probably part of an ABC transporter complex. Probably responsible for energy coupling to the transport system (By similarity).
Can bind copper. It does not affect DNA binding but it inhibits zinc-mediated regulation.
Metal-responsive transcriptional regulator that represses transcription of cadA and the czcD-trkA operon by binding specifically to their promoter. Binding of zinc causes the repressor to dissociate from the DNA.
Belongs to the DEAD box helicase family. CshB subfamily.
DEAD-box RNA helicase that plays a role in 70S ribosome assembly. May work in conjunction with the cold shock proteins to ensure proper initiation of transcription at low and optimal temperatures.
Induced by cold shock (PubMed:12399512). In rich medium highest expression in logarithmic growth, expression decreases and then disappears in stationary phase (at protein level) (PubMed:20572937, PubMed:23175651). Protein level not increased at 16 degrees Celsius. Not detected in minimal medium (at protein level) (PubMed:20572937).
Interacts with CspB when cells are transcriptionally active. May interact with RNA helicases CshA and DbpA (DeaD), may be a component of a possible RNA degradosome complex composed of rny, rnja, rnjb, pnp, pfkA and eno (although rnjA and rnjB's presence is unclear). Specifically interacts with pnp and rny (PubMed:20572937).
No difference in growth at 37 or 15 degrees Celsius (PubMed:16352840), decreased growth at 16 degrees Celsius (PubMed:23175651). The presence of CshA or CshB is essential for viability; in a cshA disruption mutant further depletion of cshB stops growth after 1 cell duplication (PubMed:16352840). Others show a quadruple disruption of all RNA helicases (cshA, cshB, deaD, yfmL) was not lethal at 37 degrees Celsius, although both 50S and 70S ribosomes are decreased, but growth stops at 16 degrees (PubMed:23175651). A double cshB-cspB disruption mutant cannot be made. A double cshB-cspD mutant grows slowly at 15 degrees Celsius (PubMed:16352840). Decreased amounts of 70S ribosomes (PubMed:23175651).
Probable DEAD-box RNA helicase. May work in conjunction with the cold shock proteins to ensure proper initiation of transcription at low and optimal temperatures.
Expressed during sporulation, around the time of spore coat synthesis and assembly, in mother cell compartment.
Expression is sigma K-dependent and negatively regulated by GerE.
Required for the formation of functionally normal spores. Could be involved in the establishment of normal spore coat structure and/or permeability, which allows the access of germinants to their receptor.
Growing cells lacking this gene have an unchanged spontaneous mutation frequency, even in triple mutT/yjhB/yvcI disruptions (PubMed:12483591), however they are more sensitive to DNA-damaging agents such as H(2)O(2) or t-BHP (PubMed:16513759). A double ytkD/mutT disruption has a greater mutation frequency than the ytkD disruption, as well as an increased sensitivity to DNA-damaging agents (PubMed:16513759). These properties are also seen in stationary phase cells (PubMed:19011023).
May be involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine, 8-oxo-dGTP) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions. MutT specifically degrades 8-oxo-dGTP to the monophosphate (By similarity). Functions, in conjunction with ytkD, to protect vegetatively growing cells from DNA-damaging agents such as H(2)O(2) or t-BHP (t-butylhydroperoxide). The 2 proteins do not however protect spores.
Citrate synthase is found in nearly all cells capable of oxidative metabolism.
Might regulate the synthesis and function of enzymes involved in later enzymatic steps of Krebs cycle. Loss in activity results in sporulation defect.
Belongs to the WXG100 family. sagEsxA-like subfamily.
Cells lacking this gene display an increased bacteriophage SPP1 resistance phenotype (PubMed:15576783). Loss of delivery of LXG type toxins to target cells (PubMed:34280190).
Positively regulated by phosphorylated DegU.
Required to deliver LXG toxins to target cells.
The WXG motif and the C-terminal tail are crucial for secretion.
Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
Member of the two-component regulatory system YrkQ/YrkP. Probably activates YrkP by phosphorylation.
Homodimer. Dimerization is essential for activity as both monomers contribute to the formation of the active site.
Key element in the phosphorelay regulating sporulation initiation. Acts on spo0A. Mediates reversible phosphoryl transfer from spo0F to spo0A.
Belongs to the ATPase alpha/beta chains family.
Probable catalytic subunit of a protein translocase for flagellum-specific export, or a proton translocase involved in local circuits at the flagellum.
Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily.
Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
Belongs to the HAD-like hydrolase superfamily. CbbY/CbbZ/Gph/YieH family.
Catalyzes the interconversion of D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), and forming beta-D-glucose 1,6-(bis)phosphate (beta-G16P) as an intermediate. The beta-phosphoglucomutase (Beta-PGM) acts on the beta-C(1) anomer of G1P. It plays a key role in the regulation of the flow of carbohydrate intermediates in glycolysis and the formation of the sugar nucleotide UDP-glucose (By similarity).
The catalysis proceeds via a phosphoenzyme formed by reaction of an active-site nucleophile with the cofactor glucose 1,6-diphosphate (G1,6-diP). The phosphorylated mutase binds either G1P or G6P and transfers the phosphoryl group to the C(6)OH or C(1)OH, respectively (By similarity).
Belongs to the KHG/KDPG aldolase family.
Induced by galacturonate and negatively regulated by the KdgR repressor. Is subject to catabolite repression by glucose involving the ccpA gene.
Degrades both double-stranded linear and covalently closed circular DNA. Likely to play a scavenging role in order to supply nutrients under starvation conditions.
Has an important morphogenetic role. Involved in the assembly of at least five coat proteins, including CotB, CotG, CotS, CotSA and CotW. Required for appearance of a morphologically normal outer coat. To a large degree, CotO and CotH act at a late stage of coat assembly from within the outer coat to direct maturation of this structure.
Largely but not entirely controlled by CotE.
Belongs to the low molecular weight phosphotyrosine protein phosphatase family.
By ethanol stress. Expression is sigma B-dependent.
Dephosphorylates the phosphotyrosine-containing proteins. Involved in ethanol stress resistance.
Efficiently inhibited by Cu(2+) ion, Zn(2+) ion and N-ethylmaleimide, while the addition of Mg(2+), Ca(2+) or Fe(3+) ions has minimal effect. Inhibited in a competitive manner by vanadate.
Coordinates cortex and coat assembly during sporulation (PubMed:22463703, PubMed:8231808). Associates with the spore coat protein SpoIVA and with the outer forespore membrane, thereby serving as a membrane anchor that tethers SpoIVA and the entire spore coat to the forespore surface (PubMed:17427285). May also serve as a competitive inhibitor of FtsH activity during sporulation (PubMed:9287010).
Expressed during sporulation and is regulated by the mother cell-specific transcription factors sigma E and SpoIIID (PubMed:8231808). There is a lag-phase of approximately 2 hours between the onset of transcription and translation (PubMed:18820968). The 5' untranslated region negatively influences its own translation (PubMed:18820968).
Interacts with SpoIVA (PubMed:17427285). May interact with the ATP-dependent protease FtsH (PubMed:9287010).
Nanomolar concentrations inhibit biofilm formation in situ, in S.aureus and in P.aeruginosa, suggesting it might be useful controlling bacterial infections.
Preferentially localizes to slightly convex membranes (PubMed:25825747, PubMed:29102609). This preferential adsorption is accurately modeled as a two-step 'dash-and-recruit' mechanism: first, an initial binding event occurs with a faster on rate, then cooperative recruitment of additional SpoVM molecules follows (PubMed:29102609).
Residues in the N-terminal region are required for proper localization.
Positive regulator of sigma-B activity. Dephosphorylates RsbV in response to environmental stress conveyed from the RsbXST module.
Stimulated by a long-lived interaction with RsbT.
(Microbial infection) Interacts with Bacillus phage SP01 Gp46; the interaction replaces dsDNA from the hbs-DNA complex.
Belongs to the bacterial histone-like protein family.
Constitutively transcribed with 2 transcripts of 0.54 and 0.38 kb.
Essential, it cannot be deleted; upon depletion cell growth slows.
Histone-like DNA-binding protein which introduces negative supercoils in relaxed plasmid DNA in the presence of topoisomerase I. There are at least 20,000 monomers/cell (PubMed:8439548). Capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions. Binds evenly across chromosome, does not display a preference for AT content (PubMed:21085634). Binds ss- and dsDNA in a sequence non-specific manner; 8 nucleotides are sufficient to bind protein (PubMed:3595600).
Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family.
Involved in the type II fatty acid elongation cycle (PubMed:11325930). Catalyzes the elongation of a wide range of acyl-ACP by the addition of two carbons from malonyl-ACP to an acyl acceptor (PubMed:11325930). Can efficiently catalyze the conversion of palmitoleoyl-ACP (cis-hexadec-9-enoyl-ACP) to cis-vaccenoyl-ACP (cis-octadec-11-enoyl-ACP), an essential step in the thermal regulation of fatty acid composition (By similarity).
Involved in the type II fatty acid elongation cycle. Catalyzes the elongation of a wide range of acyl-ACP by the addition of two carbons from malonyl-ACP to an acyl acceptor. Can efficiently catalyze the conversion of palmitoleoyl-ACP (cis-hexadec-9-enoyl-ACP) to cis-vaccenoyl-ACP (cis-octadec-11-enoyl-ACP), an essential step in the thermal regulation of fatty acid composition.
In the mid-exponential phase of growth under acidic conditions. Positively autoregulated, in the presence of RsoA. Down-regulated by YvrL under nonstress conditions.
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Together with its coactivator RsoA, positively regulates the expression of at least three operons, including oxdC-yvrL, sigO-rsoA and yvrJ. Required for the acid stress-dependent induction of the oxalate decarboxylase oxdC.
Degrades RNA oligonucleotides with a length of 5 nucleotides in a 3'- to 5'-direction. Less active on shorter RNA oligonucleotides and on those with a length of 24 nucleotides. Prefers RNA oligonucleotides containing adenines rather than cytosines.
No visible phenotype. Cells show normal growth.
Essential for the phosphorelay during initiation of sporulation. May control the level of phosphorylated spo0A through spo0E activity during sporulation.
Belongs to the Orn/Lys/Arg decarboxylase class-I family.
In the C-terminal section; belongs to the PHP family.
In the N-terminal section; belongs to the DNA polymerase type-X family.
Probably binds 2 divalent metal cations per N-terminal polymerase domain. Mn(2+) is more effective than Mg(2+) for DNA polymerase activity.
Probably binds 3 Mn(2+) ions per C-terminal exonuclease domain. Mg(2+) cannot replace Mn(2+) for 3'-5' exonuclease activity.
Strictly DNA-template-directed DNA polymerase, preferentially acting on DNA structures containing gaps from one to a few nucleotides and bearing a phosphate group at the 5' end of the downstream DNA. The fact that PolX is able to conduct filling of a single-nucleotide gap, allowing further sealing of the resulting nick by a DNA ligase, points to a putative role in base excision repair (BER) during the B.subtilis life cycle. Moreover, also possesses a 3'-5' exonuclease activity able to edit unpaired 3'-termini in a gapped DNA substrate and likely involved in resecting unannealed 3'-termini during DNA repair. The same PolX molecule could perform the subsequent gap-filling step. Does not display 5'-deoxyribose 5'-phosphate (dRP) lyase activity, as predicted by the lack of the lysine and tyrosine residues responsible for the dRP lyase activity in some other PolX members.
The 3'-5' exonuclease activity resides in the C-terminal PHP domain.
The polymerization activity is inhibited in the presence of 2'-3'-dideoxynucleoside 5'-triphosphate (ddNTP).
Catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein MoaD.
Homodimer. Forms a stable heterotetrameric complex of 2 MoeB and 2 MoaD during adenylation of MoaD (By similarity).
Belongs to the glycosyltransferase 28 family. UgtP subfamily.
Cells displayed reduced and abnormal cell size/shape, no effect on flotillin cluster numbers or size.
Processive glucosyltransferase involved in the biosynthesis of both the bilayer- and non-bilayer-forming membrane glucolipids. Is able to successively transfer up to three glucosyl residues to diacylglycerol (DAG), thereby catalyzing the formation of beta-monoglucosyl-DAG (3-O-(beta-D-glucopyranosyl)-1,2-diacyl-sn-glycerol), beta-diglucosyl-DAG (3-O-(beta-D-glucopyranosyl-beta-(1->6)-D-glucopyranosyl)-1,2-diacyl-sn-glycerol) and beta-triglucosyl-DAG (3-O-(beta-D-glucopyranosyl-beta-(1->6)-D-glucopyranosyl-beta-(1->6)-D-glucopyranosyl)-1,2-diacyl-sn-glycerol). Beta-diglucosyl-DAG is the predominant glycolipid found in Bacillales and is also used as a membrane anchor for lipoteichoic acid (LTA).
Processive glucosyltransferase involved in the biosynthesis of both the bilayer- and non-bilayer-forming membrane glucolipids. Is able to successively transfer up to three glucosyl residues to diacylglycerol (DAG), thereby catalyzing the formation of beta-monoglucosyl-DAG (3-O-(beta-D-glucopyranosyl)-1,2-diacyl-sn-glycerol), beta-diglucosyl-DAG (3-O-(beta-D-glucopyranosyl-beta-(1->6)-D-glucopyranosyl)-1,2-diacyl-sn-glycerol) and beta-triglucosyl-DAG (3-O-(beta-D-glucopyranosyl-beta-(1->6)-D-glucopyranosyl-beta-(1->6)-D-glucopyranosyl)-1,2-diacyl-sn-glycerol). Beta-diglucosyl-DAG is the predominant glycolipid found in Bacillales and is also used as a membrane anchor for lipoteichoic acid (LTA). Also seems to be able to form beta-tetraglucosyl-DAG, although this glycolipid has not been found in B.subtilis membrane. UgtP can only use UDP-glucose as sugar donor.
Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily.
In contrast to other bacteria, in which inactivation of serine protease leads to thermosensitivity, inactivation of HtrA leads to an increased thermotolerance and an increased tolerance to hydrogen peroxide. Inactivation of both HtrA and HtrB leads to growth defects and to thermosensitivity.
Inactivation results in compensating overexpression of YtvA, especially during stress conditions.
Transcription is CssS dependent. Induced by heat shock during exponential growth and by heterologous amylases at the transition phase of the growth cycle. Negatively regulates its own expression during exponential growth and during heat shock.
Part of the SufBCD complex that contains SufB, SufC and SufD.
The SufBCD complex acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS. The SufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation (By similarity).
Catalyzes the addition of a single glycerol phosphate residue to the prenoldiphosphate-linked disaccharide, as a primer for polymerisation by TagF.
Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
Inner spore coat protein which seems to play a role in germination.
Present in an increased level in yabG mutant spores.
Transcription factor involved in regulation of membrane lipid biosynthesis by repressing genes involved in fatty acid and phospholipid metabolism. Binds to the 5'-TTAGTANNNNNTANTAA-3' consensus sequence found in the promoter of fabHAF operon (containing fabHA and fabF genes), yhdO and fapR genes and prevents their expression. Its action is probably modulated by malonyl-CoA.
Transcriptional factor involved in regulation of membrane lipid biosynthesis by repressing genes involved in fatty acid and phospholipid metabolism.
By formaldehyde and methylgloxal, under the control of AdhR. Encoded in an operon with yraA.
Cells lacking this gene show significantly reduced growth in the presence of formaldehyde but not methylglyoxal.
Functions in the protection against aldehyde-stress.
Autoproteolytically processed. The inactive tetrameric zymogen termed p46 autoprocesses to a smaller form termed p41, which is active only during spore germination.
GPR transcription occurs during sporulation in forespore first by sigma-F and then by sigma-G.
Initiates the degradation of small, acid-soluble proteins during spore germination.
Initiates the rapid degradation of small, acid-soluble proteins during spore germination.
Belongs to the RNA methyltransferase TrmD family.
Specifically methylates guanosine-37 in various tRNAs.
Belongs to the anti-sigma-factor family.
Binds to sigma F and blocks its ability to form an RNA polymerase holoenzyme (E-sigma F). Phosphorylates SpoIIAA on a serine residue. This phosphorylation may enable SpoIIAA to act as an anti-anti-sigma factor that counteracts SpoIIAB and thus releases sigma F from inhibition.
Interaction with SpoIIAB inhibits sigma F activity throughout the cell before the formation of the asymmetric septum; after septation the interaction is confined to the mother cell, and sigma F activity is released in the prespore.
Mild sensitivity to cumene hydroperoxide (CHP) as indicated by growth inhibition assay. No effect on growth after NaOCl treatment.
S-bacillithiolation is the formation of mixed disulfide bonds between protein thiols and the general thiol reductant bacillithiol (BSH) under oxidative stress. BSH is an equivalent of glutathione (GSH) in Firmicutes. This protein is a dithiol bacilliredoxin, which debacillithiolates (removes BSH) the S-bacillithiolated OhrR (OhrR-SSB) in vitro and in vivo NaOCl-generated S-bacillithiolated MetE (MetE-SSB). Involved in maintaining redox homeostasis in response to disulfide stress conditions (PubMed:24313874). Has a redox potential of -130 mV. Displays weak protein disulfide isomerase activity in vitro (PubMed:19653655).
Belongs to the FAD-dependent oxidoreductase 2 family. NadB subfamily.
Catalyzes the oxidation of L-aspartate to iminoaspartate, the first step in the de novo biosynthesis of NAD(+) (PubMed:18959769). Can use either oxygen or fumarate as electron acceptors, which allows the enzyme to be functional under aerobic and anaerobic conditions (PubMed:18959769).
Expression is repressed in the presence of nicotinic acid.
Mutant requires exogenous nicotinic acid for growth.
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in beta-glucoside transport (By similarity).
Monocistronically transcribed in the late sporulation phase and cotranscribed with mutY and/or fabL during exponential growth. However, sspE is not translated during this period.
SASP are proteins degraded in the first minutes of spore germination and provide amino acids for both new protein synthesis and metabolism. These proteins may be involved in dormant spore's high resistance to UV light.
Cells lacking this gene and ftsX, the next gene in the operon, delay sporulation onset, as a result of which they form a medial rather than polar septum at the onset of sporulation. This is presumably due to slower phosphorylation and activation of the spo0A transcriptional regulator. However, at later time points these cells undergo polar division and eventually form smaller than wild-type mature spores.
Homodimer. Forms a membrane-associated complex with FtsX.
Part of the ABC transporter FtsEX involved in cellular division.
Part of the ABC transporter FtsEX involved in sporulation. May act as an importer, possibly at the top of a hierarchical cascade leading to the correct temporal initiation of sporulation. Acts upstream of the histidine kinases KinA, KinB and KinC, the RapA phosphatase and the Spo0A sporulation protein.
Belongs to the NAD-dependent DNA ligase family. LigA subfamily.
DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
Deletion of this gene has no effect on mannose utilization.
Up-regulated by mannose. Is under the control of ManR. Is subject to carbon catabolite repression (CCR) by glucose. Forms part of an operon with manP and manA.
Belongs to the purine nucleoside phosphorylase YfiH/LACC1 family.
Purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine and hypoxanthine. Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate. Also has adenosine deaminase activity.
Belongs to the 6-phosphogluconate dehydrogenase family.
May act as NAD-dependent 6-P-gluconate dehydrogenase.
Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. EngB GTPase family.
Essential for growth, it cannot be disrupted. In depletion experiments cells become over 3-fold longer, are abnormally curved and nucleoids condense.
Estimated to be present at 1000 copies per cell.
Necessary for normal cell division and for the maintenance of normal septation.
Sensor protein that up-regulates translation of the secondary membrane protein insertase (MisCB/YqjG) when activity of the primary membrane protein insertase (MisCA/SpoIIIJ) is limited. Acts as a ribosome-nascent chain complex. When the primary membrane protein insertase activity or level is reduced, the membrane insertion of MifM is impaired, which induces arrest of MifM translation and unfolding of the mRNA hairpin. Unfolding leads to translation of the downstream gene, which encodes the secondary membrane protein insertase MisCB/YqjG. Translation arrest of MifM is mediated by interaction of its C-terminal domain with the ribosomal polypeptide exit tunnel. Undergoes multisite stalling, which may allow a sufficient duration of ribosomal stalling and consequently sufficient levels of MisCB/YqjG.
Belongs to the polysaccharide lyase 1 family.
Catalyzes the depolymerization of pectins of methyl esterification degree from 13 to 75%, with an endo mode of action. Cannot degrade polygalacturonate (By similarity).
100-fold decrease in homologous recombination efficiency.
By mitomycin, requires an intact dinR gene (PubMed:1657879). An SOS-independent induction of dinR occurs during competence, does not require an intact dinR gene (PubMed:1657879).
Expressed during the entire cell cycle with at least a threefold increase when cells develop competence.
Following treatment with mitomycin C protein levels begin to decrease after a 5-min lag and do not return to their original levels for at least 90 min.
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Represses dinA, dinB, dinC, recA genes and itself by binding to the 14 bp palindromic sequence 5'-CGAACNNNNGTTCG-3'; some genes have a tandem consensus sequence and their binding is cooperative (PubMed:1657879, PubMed:8969214, PubMed:9555905). In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair; autocleavage is maximal at pH 11 in the absence of RecA and ssDNA (PubMed:8969214).
May be involved in the secretion of the autolysin BlyA.
Binds 3 Mn(2+); 2 Mn(2+) for polymerase/primase activity and 1 for ligase activity.
In the C-terminal section; belongs to the ATP-dependent DNA ligase family.
In the N-terminal section; belongs to the LigD polymerase family.
LigD has variable architecture. In Bacillus lacks the 3'-phosphoesterase domain (PE) found in Mycobacteria and some Gammaproteobacteria.
Stationary-phase cells lacking this gene are more sensitive to ionizing radiation (IR) than cells lacking Ku (YkoV); a double mutant is not more sensitive than the ku knockout. Spores lacking this gene are more sensitive to UV, IR, ultrahigh vacuum, and dry heat.
The preference of the polymerase domain for rNTPs over dNTPs may be advantageous in dormant cells, where the dNTP pool may be limiting.
Transcriptionally regulated by SpoVT and sigma-G factor.
With Ku forms a non-homologous end joining (NHEJ) DNA repair enzyme, which repairs dsDNA breaks with reduced fidelity (Probable). Probably involved in DNA repair during spore germination.
Belongs to the PheA/TfdB FAD monooxygenase family.
Was originally (PubMed:8969503, PubMed:9384377) predicted to be the product of two different genes yfkA and yfkB.
Belongs to the bacterial ribosomal protein bL12 family.
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
Homodimer. Part of the 50S ribosomal subunit; present in 4 copies per ribosome. Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Forms a pentameric L10(L12)2(L12)2 complex, where L10 forms an elongated spine to which 2 L12 dimers bind in a sequential fashion.
Homodimer. Part of the ribosomal stalk of the 50S ribosomal subunit. Forms a multimeric L10(L12)X complex, where L10 forms an elongated spine to which 2 to 4 L12 dimers bind in a sequential fashion. Binds GTP-bound translation factors.
Repressed by YetL (PubMed:19329649). Induced by several flavonoids (PubMed:19329649).
Belongs to the DNA polymerase type-C family. DnaE subfamily.
DNA polymerase III contains a core (composed of alpha, epsilon and theta chains) that associates with a tau subunit. This core dimerizes to form the POLIII' complex. PolIII' associates with the gamma complex (composed of gamma, delta, delta', psi and chi chains) and with the beta chain to form the complete DNA polymerase III complex.
DNA polymerase III contains a core (composed of alpha, epsilon and theta chains) that associates with a tau subunit. This core dimerizes to form the PolIII' complex. PolIII' associates with the gamma complex (composed of gamma, delta, delta', psi and chi chains) and with the beta chain to form the complete DNA polymerase III complex (By similarity).
DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain is the DNA polymerase (By similarity).
DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain is the DNA polymerase.
Belongs to the urease beta subunit family.
Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha) subunits. Three heterotrimers associate to form the active enzyme.
Belongs to the fosfomycin resistance protein family. FosB subfamily.
Metallothiol transferase which confers resistance to fosfomycin by catalyzing the addition of a thiol cofactor to fosfomycin. L-cysteine is probably the physiological thiol donor.
Belongs to the peroxiredoxin family. BCP/PrxQ subfamily.
The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this atypical 2-Cys peroxiredoxin, C(R) is present in the same subunit to form an intramolecular disulfide. The disulfide is subsequently reduced by thioredoxin.
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events.
Belongs to the gamma-glutamylcyclotransferase family.
Putative gamma-glutamylcyclotransferase.
This protein is a component of an oligopeptide permease, a binding protein-dependent transport system. This APP system can completely substitute for the OPP system in both sporulation and genetic competence, though, unlike OPP, is incapable of transporting tripeptides. Probably responsible for the translocation of the substrate across the membrane (By similarity).
Belongs to the radical SAM superfamily. KamA family.
Catalyzes the interconversion of L-alpha-lysine and L-beta-lysine.
Deletion of the genomic region encompassing the entire yodT-yodS-yodR-yodQ-yodP-kamA gene cluster has no noticeable effect on growth either in rich or minimal medium, does not affect sporulation, and does not cause osmotic sensitivity or influence the compatible solute pool of this soil bacterium.
The use of KamA and YodP from B.subtilis for N6-acetyl-beta-lysine synthesis opens the bottleneck for the large-scale production of N6-acetyl-beta-lysine to investigate its properties as a compatible solute.
Belongs to the catalase family. HPII subfamily.
Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide. Involved in sporulation.
Serves to protect cells from the toxic effects of hydrogen peroxide.
Catalyzes the phosphorylation of a range of fructosamines to fructosamine 6-phosphates.
Belongs to the aldolase class II family. MtnB subfamily.
Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).
4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by sfp.
Belongs to the tRNA pseudouridine synthase TruA family.
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Belongs to the alkylbase DNA glycosidase AlkA family.
Disruption of this gene sensitizes cells to the alkylating agent N-propyl-N'-nitro-N-nitrosoguanidine.
Is involved in the adaptive response to alkylation damage in DNA caused by alkylating agents. Catalyzes the hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine and 7-methylguanine from the damaged DNA polymer formed by alkylation lesions.
Overproduction of this gene renders cells highly resistant to the alkylating agent N-propyl-N'-nitro-N-nitrosoguanidine.
Up-regulated by methylated AdaA in response to the exposure to alkylating agents.
Expressed in mother cell during sporulation.
Can transport glucose, mannose, 2-deoxyglucose and methyl alpha-glucoside, but not galactose.
Induced by glucose. Induction depends upon the integrity of the glucose-specific PTS system.
Belongs to the class-II aminoacyl-tRNA synthetase family.
Belongs to the RNA polymerase alpha chain family.
Homodimer. RNAP is composed of a core of 2 alpha, a beta and a beta' subunit. The core is associated with a delta subunit, and at least one of epsilon or omega (PubMed:6802805, PubMed:18289874, PubMed:21710567). When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription (PubMed:18289874).
Homodimer. The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta' and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription.
The N-terminal domain is essential for RNAP assembly and basal transcription, whereas the C-terminal domain is involved in interaction with transcriptional regulators and with upstream promoter elements.
Belongs to the aldo/keto reductase family. Aldo/keto reductase 2 subfamily.
Cells lacking this gene show a purine auxotrophic phenotype and an accumulation of FGAR due to defective FGAM synthetase activity.
Homodimer or homotetramer. Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits.
Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits.
Has a role in exoprotein production, sporulation and competence.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily.
By hydrogen peroxide. Repressed by PerR.
Couples the hydrolysis of ATP with the transport of zinc into the cell. Plays an important role in protecting cells against oxidative stress. ZosA-mediated zinc transport is required for post-transcriptional control of comK and competence development.
Disruption results in low transformability, which can be rescued by the addition of excess zinc.
Belongs to the vitamin uptake transporter (VUT/ECF) (TC 2.A.88) family. Thiamine transporter subfamily.
Cells display deregulation of thiamine biosynthesis and impaired export of thiamine products from the cell.
Forms a stable energy-coupling factor (ECF) transporter complex composed of a membrane-embedded substrate-binding protein (S component), two ATP-binding proteins (A components) and a transmembrane protein (T component).
Probably a thiamine-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. The substrates themselves are bound by transmembrane, not extracytoplasmic soluble proteins (By similarity).
Member of the two-component regulatory system DesR/DesK, responsible for cold induction of the des gene coding for the Delta5 acyl-lipid desaturase. Acts as a sensor of the membrane fluidity. Probably activates DesR by phosphorylation.
Belongs to the dTDP-4-dehydrorhamnose reductase family.
Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate (By similarity). Interacts with BrxC (PubMed:33722570).
By heat shock, salt stress, oxidative stress, glucose limitation and oxygen limitation. Expression is sigma B-dependent.
Involved in organic hydroperoxide resistance.
This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Tyr and Thr as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The Thr residue is further converted to the D-allo-isomer form. The activation sites for these amino acids consist of individual domains.
Belongs to the type IA topoisomerase family.
Monomer. Interacts with the RNA polymerase core (PubMed:21710567).
Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.
Expressed at about stage III of sporulation. Specifically enriched in stage IV forespores but not in stage IV mother cells (PubMed:3933484, PubMed:3080407).
Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors (PubMed:3933484). Required specifically for the synthesis of the spore form of peptidoglycan (cortex) (Probable).
Activated by D-ribose and 2-deoxy-D-ribose. Slightly activated by kanamycin and gentamicin.
Belongs to the aminoglycoside phosphotransferase family.
Cells lacking this gene are slightly thinner and longer, but no anucleate cells are present and they have a growth rate similar to wild-type cells. Significantly decreased DNA replication initiation rate (PubMed:34373624). Susceptible to a broad range of DNA damage including mitomycin C (MMC), methyl methanesulfonate (MMS), ciprofloxacin, phleomycin and UV irradiation. Significant induction of the DNA damage response (SOS). Not sensitive to kanamycin or gentamicin (PubMed:35576203).
Monomer in solution. Interacts with DnaA (via domains I (1-82) and III (111-326)). Interacts with DnaB (PubMed:35576203). Interacts with FtsZ (By similarity).
Plays a role in cell cycle regulation and chromosome integrity. Activates DnaA-dependent chromosomal DNA replication initiation ensuring that the chromosome is replicated at the right time during the cell cycle (By similarity). May regulate replication initiation through phosphorylation of a possible second messenger or metabolite, and by interacting with replication initiation proteins. Has ATPase activity with D-ribose and 2-deoxy-D-ribose in vitro, but not with choline. Involved in DNA damage response (PubMed:35576203).
Belongs to the glycosyl hydrolase 73 family.
Cell wall hydrolase not involved in cell autolysis, competence, sporulation or germination. It hydrolyzes the beta-1,4 glycan bond between the N-acetylglucosaminyl and the N-acetylmuramoyl residues in the glycan chain.
Cells lacking this gene show no motility changes on swarm plates; however in combination with an amidase deletion (lytC, AC Q02114) greatly reduced motility is seen.
In stationary phase (PubMed:11987133); under control of SigD (PubMed:7581999).
Inhibited by diethyl pyrocarbonate, slightly by EDTA. Not inhibited by PMSF, diisopropyl fluorophosphate, 2-mercaptoethanol or N-ethylmaleimide.
Catalyzes the high-affinity uptake of extracellular proline. Important for the use of proline as a sole carbon and energy source or a sole nitrogen source.
Deletion of the putBCP operon abolishes L-proline utilization.
The expression of the putBCP operon is induced in a PutR-dependent fashion by very low concentrations of L-proline in the growth medium. CodY represses the operon by displacing PutR from DNA.
Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
Normally not expressed. Its expression is induced when that of thrS is reduced.
Belongs to the EPSP synthase family. MurA subfamily.
Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. Essential for cell growth.
Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.
Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit.
The alpha chain is the actual site of nitrate reduction.
Required for the initiation of sporulation and for normal chromosome segregation. Antagonizes sporulation inhibition by Soj. It probably interacts with a specific DNA site and other proteins involved in partitioning and cell division, and antagonizes Soj in response to cell cycle events related to chromosome partitioning.
Inactivation of the gene leads to a reduction in sporulation efficiency.
Signaling molecule involved in the regulation of sporulation (PubMed:10629174). Secreted during production, but the mature peptide acts intracellularly, indicating that it needs to be imported into the cell to function (Probable). Inhibitor of the RapE phosphatase activity (PubMed:10629174). Does not inhibit the phosphatase activity of RapA and RapB (PubMed:10629174). Probably plays a dispensable role in the overall context of sporulation initiation (PubMed:10629174).
Transcription occurs independently of the rapE promoter and is controlled by the Spo0A-AbrB pair of transcriptional regulators.
The PTS EIIB type-3 domain is phosphorylated by phospho-EIIA on a cysteinyl residue. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the PTS EIIC type-3 domain.
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II GmuABC PTS system is involved in the transport of oligo-glucomannans such as cellobiose or mannobiose.
Up-regulated by konjac glucomannan and by cellobiose and mannobiose, the possible degradation products of glucomannan. Repressed by glucose via the carbon catabolite repression system. Also repressed by GmuR.
Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
Cells lacking CheV are somewhat reduced in chemotactic proficiency, but a double mutant lacking both CheV and CheW has a strong tumble bias, does not respond to addition of attractant, shows essentially no accumulation in capillary assays, and has greatly reduced methyl turnover on the methyl-accepting chemotaxis proteins (MCPs).
Consists of two domains: an N-terminal CheW-like coupling domain and a C-terminal two-component receiver domain.
Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. Chemotaxis involves both a phosphorylation-dependent excitation and a methylation-dependent adaptation. CheV and CheW are involved in the coupling of the methyl-accepting chemoreceptors to the central two-component kinase CheA; they are both necessary for efficient chemotaxis. Moreover, CheA-dependent phosphorylation of CheV is required for adaptation to attractants during B.subtilis chemotaxis.
Peak expression is seen in early stationary phase.
Belongs to the flavin monoamine oxidase family. FIG1 subfamily.
Involved in the activation of the KinB signaling pathway of sporulation.
No effect on sporulation as single mutant, but when associated with deletion of kinA, sporulation efficiency is significantly decreased.
Homodimer; disulfide-linked. A minor fraction of ComGG is found as a disulfide-bonded homodimer.
Partial processing of ComGG in competent cells requires ComC.
Required for transformation and DNA binding.
Involved in cell lysis upon induction of PbsX.
Belongs to the purine/pyrimidine phosphoribosyltransferase family. Xpt subfamily.
Converts the preformed base xanthine, a product of nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so it can be reused for RNA or DNA synthesis.
Converts the preformed base xanthine, a product of nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so that it can be reused for RNA or DNA synthesis.
Highly specific for xanthine, with a strong discrimination against hypoxanthine and guanine as substrates.
Repressed during growth on purines as a nitrogen source.
Aggregate of 4 catalytic active heterodimers, consisting of a large and a small subunit.
Belongs to the glutamate synthase family.
The gltAB operon is positively regulated by GltC and negatively regulated by TnrA under nitrogen-limited conditions.
Forms a stable heterotetramer with KinA (comprising two molecules of each protein), by binding to the KinA dimerization/phosphotransfer domain.
Mediates a developmental checkpoint inhibiting initiation of sporulation (by preventing phosphorylation of spo0A) in response to defects in the replication initiation machinery. Inhibits autophosphorylation of the histidine protein kinase KinA, forming a molecular barricade that prevents productive interaction between the ATP-binding site in the catalytic domain and the phosphorylatable His in the phosphotransfer domain of KinA. Probably also inhibits the activity of KinB, but has relatively little effect on KinC. Has at least one target in vivo in addition to KinA as sda does not require KinA to inhibit sporulation.
Belongs to the uroporphyrinogen-III synthase family.
Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
Although this enzyme can be purified from B.subtilis, the bacteria is sensitive to streptomycin in vivo.
Could be used as a selectable marker in B.subtilis if strongly expressed, could be used as a selectable marker in E.coli (Ref.7). Streptidine restores the antibiotic effectiveness of streptomycin in bacterial strains in which they both are co-administered together with a simultaneous overexpression of this enzyme (PubMed:17609790).
Mediates bacterial resistance to streptomycin (PubMed:3137862, PubMed:17609790). Adenylates streptomycin on the O-6 residue (PubMed:3137862, PubMed:15984036, PubMed:17609790). Adenylates streptidine on the O-6 residue (PubMed:17609790). Does not act on spectinomycin, neomycin-B or kanamycin (Ref.5, PubMed:15984036). Specific for ATP and GTP nucleotides incorporating a purine ring. No reaction with CTP or UTP (PubMed:15984036).
Very slight reduction in streptomycin MIC.
Belongs to the COX15/CtaA family. Type 1 subfamily.
Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A.
Mutations alter both cytochrome aa3 formation and sporulation.
The N-half (TM1-TM4) and C-half (TM5-TM8) domains are connected by an intracellular loop. Each domain is formed from four-helix bundles and they align in a pseudo twofold symmetry manner. The N-half domain is the substrate-heme binding domain and the C-half domain is the cofactor heme binding domain.
Essential, at least the last 3 genes of the locus cannot be deleted; could be due to polar effects on downstream ymaB.
Part of the probable nrdI(ymaA)-nrdE-nrdF-ymaB operon. Expression is constitutive but low, dramatically induced by thymidine starvation which requires recA.
Involved in the biosynthesis of pulcherrimin, a red extracellular pigment. Catalyzes the oxidation of cyclo(L-Leu-L-Leu) (cLL) to yield pulcherriminic acid which forms pulcherrimin via a nonenzymic reaction with Fe(3+). Substrates with small alkyl groups (cAA, cLG, cLP) exhibit weaker binding to CYP134A1, but substrates with larger hydrophobic side chains bind in a similar regime to cLL.
Involved in arsenical resistance. Thought to form the channel of an arsenite pump.
Member of the two-component regulatory system PhoP/PhoR involved in the regulation of alkaline phosphatase genes phoA and phoB and of phosphodiesterase.
Global transcriptional regulator that activates transcription of bmr and blt by binding directly to their promoter. Stimulates also the expression of the mta gene itself, ydfK and ymfE.
The central dimerization domain of the first subunit forms a two-helix antiparallel coiled coil with the dimerization domain of the second subunit.
Belongs to the zinc-associated anti-sigma factor (ZAS) superfamily.
The interaction between YlaC and YlaD may be regulated by the redox state of YlaD.
Disruption of the gene results in loss of cell width control (PubMed:11290328). Depletion leads to a strong defect in chromosome segregation (PubMed:14588250, PubMed:15745453). It also leads to the formation of enlarged cells, to the loss of mid cell localization of the replication machinery and to growth arrest (PubMed:15745453). Double dynA-mreB deletions have strong cell shape defects (PubMed:23249255).
Forms membrane-associated dynamic filaments that are essential for cell shape determination (PubMed:11290328, PubMed:15745453, PubMed:17064365, PubMed:19117023, PubMed:19659933). Acts by regulating cell wall synthesis and cell elongation, and thus cell shape (PubMed:19659933). A feedback loop between cell geometry and MreB localization may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature (By similarity). Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on MreB polymerization (PubMed:21636745, PubMed:21636744). The active movement of the MreB cytoskeleton stimulates diffusion of membrane proteins (PubMed:24603761). Organizes peptidoglycan synthesis in the lateral cell wall (PubMed:19659933). Also required for proper chromosome segregation (PubMed:14588250, PubMed:15745453, PubMed:17064365). Membrane fluidity influences MreB movement; in rich medium MreB movement is significantly decreased in a floA-floT mutant (PubMed:32662773).
Forms polymers (PubMed:11290328, PubMed:15745453, PubMed:17064365, PubMed:19117023). Forms a complex with Mbl and MreBH (PubMed:17064365, PubMed:19659933).
Polymerizes in the presence of millimolar divalent cations in a protein concentration-dependent manner. Polymerization is favored by decreasing pH and inhibited by monovalent salts and low temperatures.
Belongs to the universal ribosomal protein uS7 family.
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA.
Part of the 30S ribosomal subunit (PubMed:30126986). Contacts proteins S9 and S11 (By similarity). Interacts with VmlR (PubMed:30126986).
Part of the 30S ribosomal subunit. Contacts proteins S9 and S11.
Belongs to the branched chain amino acid transporter family.
Branched-chain amino acid transport system which is involved in the uptake of isoleucine and valine (PubMed:25645558). Probably does not transport leucine (PubMed:25645558). Together with BcaP and BraB, plays an important role in the activation of CodY, a branched-chain amino acid-responsive transcriptional regulator that controls the expression of several dozen transcription units in B.subtilis (PubMed:25645558).
Component of the transport system for branched-chain amino acids.
Controls the expression of the cellular protein quality control genes clpC, clpE and clpP, as well as mcsA and mcsB. Acts as a repressor of these class III stress genes by binding to a directly repeated heptanucleotide operator sequence (A/GGTCAAA NAN A/GGTCAAA). After heat shock, CtsR is degraded by the ClpCP and ClpEP proteolytic systems, ensuring the derepression of clpE, clpP and the clpC operon. CtsR negatively autoregulates its own synthesis.
CtsR autoinduces its own synthesis by derepression of the clpC operon after heat shock.
Is degraded by ClpXP at 37 degrees Celsius, which maintains a basal level of the regulator within the cell. Is phosphorylated on Arg residues by McsB.
Repressor activity is controlled via phosphorylation on arginine residues. Unphosphorylated CtsR binds with high affinity to its DNA consensus site and inhibits transcription of downstream genes, whereas the McsB-phosphorylated CtsR repressor is not able to bind to DNA, thus allowing heat-shock gene expression (By similarity).
Belongs to the DsbB family. BdbC subfamily.
Important but not absolutely essential for the production of the lantibiotic sublancin 168, it may also be required for the stability of other secreted proteins. Not required for competence for DNA uptake.
Required for disulfide bond formation in some proteins.
Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family. TrmL subfamily.
Could methylate the ribose at the nucleotide 34 wobble position in tRNA.
Belongs to the ATP-dependent AMP-binding enzyme family. MenE subfamily.
Converts 2-succinylbenzoate (OSB) to 2-succinylbenzoyl-CoA (OSB-CoA).
Belongs to the metallophosphoesterase superfamily.
Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. OAT subfamily.
Catalyzes the interconversion of ornithine to glutamate semialdehyde.
Cells lacking this gene do not grow in minimal medium containing either arginine or ornithine as sole nitrogen source.
Part of the rocDEF operon. Expression is sigma L dependent, induced by arginine, ornithine, ctirulline or proline. Ammonium and glutamine strongly repress induction of the rocD by proline, and only glutamine represses weakly induction by arginine.
Catalyzes the hydrolysis of the trilactone cycle of ferri-bacillibactin (ferri-BB) complex, leading to the formation of bacillibactin monomers and to cytosolic iron release, thus making iron available for metabolic use. Can also hydrolyze bacillibactin (BB), however the catalytic efficiency for ferri-BB hydrolysis is much higher than for BB.
Impaired growth during iron limitation conditions and a strong accumulation of intracellular ferri-bacillibactin.
Association with RNAP core increases slightly during late sporulation but not tested stresses (at protein level).
Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released. This sigma factor is responsible for the expression of the levanase operon. The open complex (sigma-54 and core RNA polymerase) serves as the receptor for receipt of the melting signal from the remotely bound activator protein LevR for the expression of the levanase operon. Associates with the RNAP core only in stationary phase cells (PubMed:21710567).
Catalyzes two reactions: the first one is the production of beta-formyl glycinamide ribonucleotide (GAR) from formate, ATP and beta GAR; the second, a side reaction, is the production of acetyl phosphate and ADP from acetate and ATP.
Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate.
Although its sequence similarity with the glycerol phosphate lipoteichoic acid synthase LtaS, it cannot restore staphylococcal growth and LTA synthesis after ltaS depletion.
Belongs to the glycosyltransferase group 1 family.
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.
B.subtilis is a well-characterized soil and water saprophyte, but it is also found in enteric flora of many species, including humans (Probable). In this environment, CSF can be transported into human intestinal epithelia via OCTN2, a host cell membrane transporter, and can induce cytoprotective heat shock proteins contributing to intestinal homeostasis (PubMed:18005709).
By mid-exponential phase, CSF accumulates to concentrations that stimulate ComA-dependent gene expression (PubMed:10464187). Upon entry into stationary phase, CSF reaches high concentrations that stimulate sporulation and inhibit ComA-dependent gene expression (PubMed:10464187).
In addition, in non-domesticated swarming strains of B.subtilis, the residual propeptide exposed on the exterior of the cytoplasmic membrane may have an extracellular role in swarming (PubMed:19202088). This function is probably not dependent on CSF (PubMed:19202088).
Interacts with RapC and inhibits its interaction with ComA.
Null mutant produces no detectable CSF activity, but null mutation has modest effects on competence gene expression (PubMed:8769645). Deletion of the gene results in decreased expression of genes activated by ComA, and significantly changes the expression of 66 operons (PubMed:16816200). In non-domesticated strains, the mutant is blocked early in swarming, forming stunted dendrites, with abnormal dendrite initiation morphology (PubMed:19202088). Mutant exhibits a specific migration defect that cannot be trans-complemented by CSF in a mixed swarm (PubMed:19202088).
Part of the rapC-phrC operon, which is controlled by the P1 promoter (PubMed:10464187). Transcription from the P1 promoter is activated by high cell density through the phosphorylated form of ComA (PubMed:10464187). PhrC is part of an autoregulatory loop, and it positively regulates its own expression (PubMed:10464187). In addition, transcription of phrC is also regulated by a P2 promoter, which directs transcription of phrC only and is controlled by the sigma-H factor (PubMed:10464187).
Secreted with a propeptide domain, which is cleaved in the cell wall by the secreted serine proteases subtilisin, Epr and Vpr to produce a mature signaling peptide (PubMed:17666034, PubMed:18689487). Contains a predicted signal peptide cleavage site in the N-terminal region, however the propeptide is probably subject to only one processing event, at the N-terminal end of the mature peptide (Probable).
Signaling molecule that serves as a cell density signal for both genetic competence development and sporulation (PubMed:8769645, PubMed:9200610). Secreted during production, but the mature peptide acts intracellularly, indicating that it needs to be imported into the cell to function (PubMed:8769645, PubMed:9200610). At low concentrations, CSF stimulates expression of the genes controlled by ComA, a transcriptional factor that regulates the development of genetic competence (PubMed:8769645, PubMed:9200610, PubMed:10464187). It includes the srfA operon, which encodes a small protein, ComS, required for competence development, and the surfactin biosynthetic enzymes (PubMed:8769645, PubMed:9200610, PubMed:10464187). Acts by inhibiting RapC, which regulates the activity of ComA (PubMed:8769645, PubMed:12950917). At high concentrations, it inhibits expression of those same ComA-controlled genes, maybe by inhibiting activity of the kinase ComP (PubMed:8769645, PubMed:9200610, PubMed:10464187). In addition, high concentrations of CSF can stimulate sporulation under some conditions (PubMed:8769645, PubMed:9200610). Also inhibits RapB activity, with lower efficiency, but does not act on RapA (PubMed:9238025). Is probably involved in the quorum sensing control of sporulation (Probable). CSF is a species-specific signaling molecule that partially compensates for the lack of ComX-mediated communication between different strains of B.subtilis (PubMed:18375560).
Chaperone required for proper molybdenum cofactor insertion and final assembly of the membrane-bound respiratory nitrate reductase.
Deletion of the gene induces changes of proteins involved in cellular processes depending on iron availability. In iron-rich medium, mutants overproduce a red pigment after entry into the stationary growth phase.
Expression increases during entry into stationary phase.
Represses the expression of the yvmC-cypX operon, which is involved in pulcherriminic acid biosynthesis. Also negatively regulates yvmA, yvnB and its own expression. Positively regulates yisI expression. Acts by binding specifically to a 14-bp palindromic motif, the YvmB box, which is present in the promoter region of the target genes.
Up-regulated in response to iron starvation. Negatively autoregulated. Also repressed by CcpA in stationary growth phase.
The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Belongs to the universal ribosomal protein uL2 family.
One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome.
Part of the 50S ribosomal subunit (PubMed:10781545, PubMed:30126986). Forms a bridge to the 30S subunit in the 70S ribosome (By similarity).
Part of the 50S ribosomal subunit. Forms a bridge to the 30S subunit in the 70S ribosome.
Transcriptional regulation of the polyketide synthase operon.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.
Monomer (By similarity). Interacts with BrxC (PubMed:33722570).
Phosphorylated on Thr-385 in vitro by PrkC in the presence of poly-L-lysine or myelin basic protein, dephosphorylated by PrpC.
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Induced by iron starvation, partially repressed by fur.
Provides the ATPase subunit for at least 2 ABC transporter complexes; YfiYZ/YfhA/YusV involved in import of the iron-hydroxamate siderophores schizokinen, arthrobactin and corprogen (Probable), and FeuABC/YusV involved in import of the catecholate siderophores bacillibactin and enterobactin (Probable). Probably responsible for energy coupling to the transport system (By similarity).
Strains lacking this gene show a reduction in growth stimulation by the iron-hydroxamate siderophores schizokinen and arthrobactin compared to wild-type. They also show a reduction in growth stimulation by the catecholate siderophores enterobactin and bacillibactin.
The iron-hydroxamate siderophore complex is composed of one ATP-binding protein (YusV), two transmembrane proteins (YfiZ and YfhA) and a solute-binding protein (YfiY); the catechoplate siderophore complex is composed of one ATP-binding protein (YusV), two transmembrane proteins (FeuB and FeuC) and a solute-binding protein (FeuA).
Autophosphorylation on threonine residue(s) and serine residue considerably increases the kinase activity of the protein. Dephosphorylated in vitro by PrpC.
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.
Bryostatin activates PrkC activity and induces germination, whereas staurosporine inhibits PrkC and significantly reduced peptidoglycan-dependent germination. Kinase activity of isolated N-terminus stimulated by poly-L-lysine or myelin basic protein (PubMed:19246764).
Protein kinase that is responsible for triggering spore germination in response to muropeptides, signaling bacteria to exit dormancy. PrkC is thus a germination receptor that binds peptidoglycan fragments containing m-Dpm (meso-diaminopimelate), which act as spore germinants. Autophosphorylates and phosphorylates EF-G (elongation factor G, fusA); the latter modification is likely necessary for germination in response to peptidoglycan (PubMed:12399479). Another group did not detect phosphorylation of EF-G (PubMed:19246764). PrkC is a substrate in vitro of the cotranscribed phosphatase PrpC, which suggests that they form a functional couple in vivo. Might also be involved in sporulation and biofilm formation. Does not seem to be involved in stress response.
PubMed:18984160 shows that peptidoglycan fragments serve as a novel mechanism of interspecies bacterial signaling that likely indicates the presence of growing bacteria and thus serve as a signal for dormant cells that growth-promoting conditions exist.
Spores lacking this gene fail to germinate in the presence of peptidoglycan fragments or purified GlcNAc-MurNAc tripeptides and tetrapeptides. They still respond to the nutrient germinant L-alanine and to the chemical germinant Ca(2+)-dipicolinic acid, indicating that the spores are still capable of germinating and that PrkC is not involved in nutrient or chemical germination.
The cytoplasmic domain has Ser/Thr kinase activity (PubMed:12406230). The C-terminal extracellular domain containing the PASTA repeats binds peptidoglycan.
Interacts directly with DivIVA and MinD.
Mutants show defects in homologous recombination, swarming motility and cell division.
The main function of the Min system is to promote the disassembly of the cytokinetic ring after cell division, thereby ensuring that division occurs only once per cell cycle. MinJ acts as a bridge between DivIVA and MinD. May modulate activity and localization of MinD and MinC through direct interaction with MinD.
Belongs to the anti-sigma-factor antagonist family.
Monomer (Probable). In stressed cells, forms a complex with RsbW. The predominant form of this complex has a stoichiometry of 2:2 (one dimer of RsbW is bound by two monomers of RsbV). Binds to RsbW in the presence of low levels of ATP or under conditions of energy or environmental stress (through dephosphorylation by RsbP or RsbU).
Phosphorylated by RsbW on a serine residue. Dephosphorylated by RsbP or RsbU.
Positive regulator of sigma-B activity. Non-phosphorylated RsbV binds to RsbW, preventing its association with sigma-B. When phosphorylated, releases RsbW, which is then free to complex with and inactivate sigma-B.
Growth rate decreased by 4-fold when grown in presence of taurine as sulfur source.
Induced by glutathione but not sulfate (at protein level). Induced by methionine and taurine. Positively regulated by YtlI under supply of glutathione as sulfur source.
Involved in a cysteine salvage pathway from S-alkylcysteine. Catalyzes the first step in this pathway, i.e. the amine acetylation of an S-alkylcysteine with a preference for S-benzyl-L-cysteine over S-methyl-L-cysteine. This pathway is likely important in the catabolism of alkylated cysteine generated by proteolysis of alkylated glutathione formed in the detoxification of a wide range of electrophiles.
Autophosphorylated. Phosphorylated in vitro at Ser-76 by the serine/threonine-protein kinase YbdM, which stimulates the phosphate transfer to DegU.
Member of the two-component regulatory system DegS/DegU, which plays an important role in the transition growth phase.
Member of the two-component regulatory system DegS/DegU, which plays an important role in the transition growth phase. Involved in the control of expression of different cellular functions, including production of degradative enzymes such as the neutral and alkaline proteases, flagellum formation and biofilm formation. Acts as both a protein kinase that undergoes autophosphorylation and subsequently transfers the phosphate to DegU, and a protein phosphatase that dephosphorylates phospho-DegU.
Regulated via serine phosphorylation of its input domain. Phosphotransfer from DegS to DegU is stimulated by phosphorylation on Ser-76 and by DegQ.
Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Synthesis starts during germination and outgrowth, and is highest at the end of exponential growth. Present in dormant spores.
Belongs to the CbbQ/NirQ/NorQ/GpvN family.
Belongs to the methyltransferase superfamily. RsmD family.
May catalyze the S-adenosyl-L-methionine-dependent methylation of a specific base in rRNA.
Involved in a multicomponent binding-protein-dependent transport system for glycine betaine. Probably responsible for energy coupling to the transport system.
The complex is composed of two ATP-binding proteins (OpuAA), two transmembrane proteins (OpuAB) and a solute-binding protein (OpuAC).
In response to low temperature and salt stress.
Unknown. Might be involved in poly(glycerol phosphate) teichoic acid biosynthesis.
Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome (By similarity).
Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
Belongs to the ETF alpha-subunit/FixB family.
Heterodimer of an alpha and a beta subunit.
The electron transfer flavoprotein serves as a specific electron acceptor for other dehydrogenases. It transfers the electrons to the main respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (By similarity).
This protein catalyzes the committed step to the synthesis of the acidic phospholipids.
RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs.
Belongs to the metallo-beta-lactamase superfamily.
Expression is under strict control of the medium composition. Induced by citrate, probably via the two-component regulatory system CitT/CitS. Repressed by rapidly metabolized carbon sources like glucose, glycerol and inositol, via the carbon catabolite repression system. Is also repressed by succinate and glutamate, albeit to a lesser extent.
Controls the expression of spo0A and is required to pass the morphological stage 0 of sporulation.
Expression controlled by a sigma-H-regulated promoter which needs the sigma-H factor for the binding of the RNA polymerase and subsequent transcription.
Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family. CsbX subfamily.
Expressed during the stationary phase of cell growth.
Probable member of the two-component regulatory system YxjM/YxjL.
Cells show no growth phenotype even at acidic pH.
It is uncertain whether Met-1 or Met-5 is the initiator.
Needs to interact with NrgA in order to localize correctly to the membrane.
Required for full induction of the nrgAB operon under conditions of ammonium limitation.
The nrgAB operon is activated by TnrA under nitrogen-limited conditions.
Needed for flagellar regrowth and assembly.
Cells lacking this gene grow normally in minimal medium or in high-osmolarity environments, and exhibit the same survival capacity as the wild-type strain upon a drastic osmotic downshift. They sporulate and germinate normally.
May play a role in resistance to osmotic downshock.
Belongs to the methyltransferase superfamily.
Member of the two-component regulatory system YvcQ/YvcP. Probably activates YvcP by phosphorylation.
Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family. RsmA subfamily.
Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Belongs to the diaminopimelate epimerase family.
Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
Belongs to the rhamnose mutarotase family.
Involved in the anomeric conversion of L-rhamnose.
Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
Belongs to the flotillin-like FloA family.
Few foci are seen on rich media, when cells are grown in minimal medium more foci are seen (at protein level) (PubMed:22753055). Constitutively expressed in rich and sporulation/biofilm-inducing media, not controlled by spo0A (at protein level) (PubMed:25909364).
Found in functional membrane microdomains (FMM) that may be equivalent to eukaryotic membrane rafts FMMs are highly dynamic and increase in number as cells age. Flotillins are thought to be important factors in membrane fluidity.
Found in functional membrane microdomains (FMM) that may be equivalent to eukaryotic membrane rafts. FMMs are highly dynamic and increase in number as cells age. FloA and FloT function is partially redundant; double deletions have marked synthetic phenotypes (PubMed:20713508, PubMed:22753055, PubMed:25909364, PubMed:27362352). Flotillins are thought to be important factors in membrane fluidity, especially during periods of rapid growth in rich media (Probable). Whether specific proteins are associated with FMMs is controversial; in one study FloT rafts have been shown to include proteins involved in adaptation to stationary phase, while FloA-FloT rafts include proteins involved in differentiation including sporulation, biofilm formation and DNA uptake competence (PubMed:25909364). Another (more finely resolved) study only showed association of NfeD2 with FloT rafts of all the proteins examined (PubMed:27362352). Involved in spatial organization of membranes, perhaps recruiting proteins to specific membrane regions (PubMed:23651456). Simultaneous overexpression of both FloA and FloT leads to defects in cell division and differentiation, in part caused by stabilization of FtsH and its subsequent increased ability to degrade proteins. Cells make more biofilm, are about half as long, have less EzrA and more frequent Z-rings (PubMed:24222488).
Homooligomerizes (PubMed:25909364). Interacts with FloT (PubMed:23651456, PubMed:25909364, PubMed:26297017). Interacts with FtsH midcell (Probable). Interacts with PhoR, colocalizes with PhoR in FloA-only membrane rafts (PubMed:25909364).
No effect on KinC activity, a double floT-floA deletion decreases the number of proteins in the DRM, blocks the ability of KinC to stimulate biofilm formation (PubMed:20713508). Single floA deletion has no change in FloT localization. Double floA-floT mutants have marked defects in cell morphology, motility, and transformation efficiency (PubMed:22753055). Single floA deletion sporulates less well. Double floA-floT deletion makes no biofilm, has greatly reduced FtsH, sporulates less than either single mutant (PubMed:22882210). Single mutation has a decrease in membrane fluidity, 25% decrease in protein secretion, double floT-floA deletion a stronger decrease in membrane fluidity and 35% decrease in protein secretion (PubMed:23651456). Double floA-floT deletion has reduced oligomerization of KinC (PubMed:26297017). Double floA-floT deletion cells are somewhat elongated, the site of cell wall synthesis is affected, increasing at division septa. The speed of MreB movement around the cell is significantly decreased in rich medium (PubMed:32662773).
The last 95 residues are required for correct localization (PubMed:22753055). The C-terminus determines the oligomerization state of the protein; there are many small foci for FloA. Swapping with the C-terminus of FloT leads to fewer large foci (PubMed:25909364). N-terminally tagged, purified protein lacking the first 10 residues oligomerizes, with 12mer to about 50mer complexes found (PubMed:27362352).
Belongs to the ABC transporter superfamily. Methionine importer (TC 3.A.1.24) family.
Part of the ABC transporter complex MetNPQ involved in methionine import (PubMed:14990259). Responsible for energy coupling to the transport system (Probable). It has also been shown to be involved in methionine sulfoxide transport (PubMed:14990259).
Strongly and specifically induced by organic peroxides. Repressed by OhrR.
Belongs to the mannitol dehydrogenase family. UxaB subfamily.
Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.
In B.subtilis succinate dehydrogenase forms part of an enzyme complex containing three subunits: a flavoprotein, an iron-sulfur protein and cytochrome b-558. Interacts with FloT (PubMed:23651456).
Member of the two-component regulatory system CitT/CitS. Regulates the expression of the citM-yflN operon. Functions probably as a membrane-associated protein kinase that phosphorylates CitT in response to environmental citrate or Mg(2+)-citrate complex.
Putative NADPH-dependent oxidoreductase.
May bind long-chain fatty acids, such as palmitate, and may play a role in lipid transport or fatty acid metabolism.
Deletion mutant lacking both trhP1 and trhP2 shows reduced 5-methoxyuridine (mo5U) formation in tRNAs.
Involved in prephenate-dependent formation of 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs, the first step in 5-methoxyuridine (mo5U) biosynthesis.
Involved in muropeptide recycling. Hydrolyzes the amide bond between N-acetylmuramic acid (MurNAc) and the L-alanine residue of the stem peptide. Cannot hydrolyze muropeptides containing N-acetylglucosamine (GlcNAc) at the non-reducing end.
Member of the two-component regulatory system YcbM/YcbL.
Expressed during sporulation, under the control of SigK and GerE. Transcription begins 4 hours (T4) after the onset of sporulation.
Incorporated into the coat in two steps. First, independently of CotE, assembles into foci associated with the forespore. Next, in a CotE-dependent manner, spreads around the developing spore to form a stable contiguous shell.
Induced in late sporulation stage by sigma K. Repressed by GerE.
Involved in spore germination; probably required at the earliest stage of germination.
Belongs to the universal ribosomal protein uS13 family.
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites.
Part of the 30S ribosomal subunit (PubMed:30126986). Forms a loose heterodimer with protein S19. Forms two bridges to the 50S subunit in the 70S ribosome (By similarity).
Part of the 30S ribosomal subunit. Forms a loose heterodimer with protein S19. Forms two bridges to the 50S subunit in the 70S ribosome.
Belongs to the transferase hexapeptide repeat family. DapH subfamily.
Catalyzes the transfer of an acetyl group from acetyl-CoA to tetrahydrodipicolinate.
Expressed in the forespore compartment of the developing sporangium.
Forms a complex at the inner spore membrane which acts as a receptor for L-alanine, thus is involved in the stimulation of germination in response to alanine. Can stimulate germination in the absence of GerD and GerK gene products (fructose and glucose receptors, respectively), but the response is improved in their presence.
Encoded in an operon with groES, groEL, ydiN, ydiO and ydiP. This operon is heat-inducible.
No BsuMI restriction or methylation-related phenotype.
To B.subtilis YqxC and T.hyodysenteriae hemolysin TlyA.
Expressed in cells competent for DNA transformation; that is 5-20% of the population (PubMed:16009133).
Expression activated by ComK (PubMed:11918817).
Needed for both DNA binding and transport. It is absolutely required for the uptake of transforming DNA but not for binding. Its role in binding may be indirect.
Catalyzes the synthesis of activated sulfate.
Belongs to the helicase family. UvrD subfamily.
May be involved in the generation of recombinogenic substrates for the subsequent action of RecA.
Anti-sigma factor for SigI. Negatively regulates SigI activity through direct interaction.
Cells lacking this gene exhibit normal cell morphology and growth rate at 37 degrees Celsius, however cell diameter is slightly decreased.
Interacts (via RsgI N-terminal anti-sigma domain) with SigI.
Part of the sigI-rsgI operon, which is transiently induced by heat stress. Expression is positively regulated by SigI via the sigma-I promoter (PubMed:17185538). In exponentially growing cells, expression is regulated by the WalRK two-component system, which represses the sigma-I promoter and activates the sigma-A promoter, leading to the formation of a basal level of RsgI (PubMed:23199363). WalRK can also positively and directly regulate transcription of the operon under heat stress through a binding site located upstream of the sigma-I promoter (PubMed:24125693). Repressed by glucose (PubMed:17185538).
Belongs to the oxygen-dependent FAD-linked oxidoreductase family.
Belongs to the drug/metabolite transporter (DMT) superfamily. Small multidrug resistance (SMR) (TC 2.A.7.1) family.
Belongs to the drug/metabolite transporter (DMT) superfamily. Small multidrug resistance (SMR) (TC 2.A.7.1) family. YkkC/YkkD subfamily.
Deletion of both gdnC and gdnD leads to a decrease in the concentration of guanidine required to inhibit bacterial growth.
Probably involved in guanidinium transport (PubMed:27989440). In vitro, confers resistance to a broad range of toxic compounds such as cationic dyes, neutral and anionic antimicrobials (PubMed:10735877).
The efflux pump is composed of GdnC and GdnD.
Transcriptionally regulated by guanidine, via a guanidine-sensing riboswitch.
In contrast to other members of the family, it lacks one conserved zinc-binding site and the active site.
Does not affect the localization of SigE.
Probable aspartic protease that is responsible for the proteolytic cleavage of the RNA polymerase sigma E factor (SigE/spoIIGB) to yield the active peptide in the mother cell during sporulation. Responds to a signal from the forespore that is triggered by the extracellular signal protein SpoIIR.
Self-associates. Interacts with SigE (Probable). Interacts with SpoIIR.
Self-associates. Interacts with SigE. Interacts with SpoIIR.
This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Pro, Gln and Tyr as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The Tyr residue is further epimerized to the D-isomer form. The activation sites for these amino acids consist of individual domains.
Involved in a cysteine salvage pathway from S-alkylcysteine. Catalyzes the reduction of N-acetyl-S-hydroxy-L-cysteine (N-acetyl-L-cysteine sulfenic acid) to N-acetyl-L-cysteine. This pathway is likely important in the catabolism of alkylated cysteine generated by proteolysis of alkylated glutathione formed in the detoxification of a wide range of electrophiles.
Monomer at sub-stoichiometric copper concentrations. Homodimer at higher copper concentrations. Forms a heterodimer (electrostatic interactions) with CopZ during the transfer of Cu(+).
The copZA operon is activated by CueR and indirectly repressed by YfmP.
Directly regulates the major intracellular proteinase (ISP-1) activity in vivo. Inhibits ISP-1 in the early stages of sporulation. It may be then inactivated by a membrane-bound proteinase.
Functions in the protection against aldehyde-stress, possibly by degrading damaged proteins.
No aldehyde-stress related phenotype; when combined with a yfkM disruption shows significantly reduced growth in the presence of formaldehye and methylglyoxal.
The adhR-yraA operon is induced by formaldehyde and methylgloxal, under the control of AdhR (PubMed:19170879). A second yraA-specific transcription unit is not induced by formaldehyde or methylglyoxal and is not controlled by AdhR (PubMed:19170879). Transcribed under partial control of SigM ECF sigma factor (PubMed:17434969).
Alpha(8)-beta(8). The alpha component is a flavoprotein, the beta component is a hemoprotein (By similarity).
Cells lacking the cysIJ genes are unable to use sulfate, sulfite or butanesulfonate as sole sulfur source, grow poorly with sulfide, but can still grow with thiosulfate, cysteine or methionine.
Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component (Probable).
Up-regulated by sulfate and the transcriptional regulator CysL.
Constitutively expressed at very low levels. Induced in response to overproduction of RapI or treatment with DNA-damaging agent mitomycin C (MMC).
Required for the excision of the integrative and conjugative element ICEBs1. Excision of ICEBs1 requires two sites, attL and attR, at the left and right ends of the integrated ICEBs1.
Belongs to the octanoyltransferase LipL family.
Catalyzes the amidotransfer (transamidation) of the octanoyl moiety from octanoyl-GcvH to the lipoyl domain of the E2 subunit of lipoate-dependent enzymes.
Cells lacking this gene are unable to grow in minimal medium. Addition of lipoic acid only partially restores growth of the mutant strain but the double mutant strain lacking both lipL and lplJ fails to grow in minimal medium containing lipoic acid. Moreover, the lipL mutant cells grow as well as wild-type in minimal medium supplemented with acetate and BCFA precursors.
The reaction proceeds via a thioester-linked acyl-enzyme intermediate.
Catalyzes the dephosphorylation of the riboflavin precursor 5-amino-6-(5-phospho-D-ribitylamino)uracil and of flavin mononucleotide (FMN) in vitro (PubMed:26316208). To a lesser extent, may also catalyze the dephosphorylation of a broad range of substrates such as phosphorylated sugars and triphosphate nucleotides in vitro (PubMed:26316208, PubMed:25848029).
No visible phenotype during normal growth or under oxidative stress caused by diamide.
Belongs to the DNA polymerase type-Y family.
Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII (By similarity).
Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
Belongs to the AAA ATPase family. RarA/MGS1/WRNIP1 subfamily.
Member of the two-component regulatory system YhcY/YhcZ. Probably activates YhcZ by phosphorylation.
Deletion of the gene abolishes induction of the melREDCA operon the presence of melibiose and raffinose (PubMed:31138628). It does not affect growth in the presence of glucose and arabinose, but it has a negative effect on the ability of the mutant to grow on the alpha-1,5-arabinose oligomers alpha-1,5-arabinobiose, alpha-1,5-arabinotriose and alpha-1,5-arabinotetraose (PubMed:20693325). Deletion mutant cannot utilize pectin and galactan, and shows a slower but steady growth rate in the presence of type I rhamnogalacturonan or polygalacturonan (PubMed:29240795).
Expressed in the presence of either arabinose or arabinotriose. Repressed by glucose.
Required to energize different ABC-type saccharide transporters (PubMed:20693325, PubMed:29240795). Part of the MdxEFG-MsmX ABC transporter complex involved in maltodextrin import, of the AraNPQ-MsmX complex involved in arabinooligosaccharides import, of the GanPQS-MsmX complex involved in galactooligosaccharides import, and of the MelEDC-MsmX complex involved in melibiose, raffinose and stachyose import (PubMed:16707683, PubMed:20693325, PubMed:27501980, PubMed:29240795, PubMed:31138628). Is probably also part of the ABC transporter complex YtcQP-YteP-MsmX involved in polygalacturonan and rhamnogalacturonan type I import during pectin degradation (PubMed:29240795). Responsible for energy coupling to the transport system (Probable).
The complex involved in maltodextrin import is composed of two ATP-binding proteins (MsmX), two transmembrane proteins (MdxF and MdxG) and a solute-binding protein (MdxE) (PubMed:16707683). The complex involved in arabinooligosaccharides uptake is composed of two ATP-binding proteins (MsmX), two transmembrane proteins (AraP and AraQ) and a solute-binding protein (AraN) (PubMed:20693325). The complex involved in galactooligosaccharides uptake is composed of two ATP-binding proteins (MsmX), two transmembrane proteins (GanP and GanQ) and a solute-binding protein (GanS) (PubMed:27501980, PubMed:29240795). The complex involved in melibiose, raffinose and stachyose import is composed of two ATP-binding proteins (MsmX), two transmembrane proteins (MelC and MelD) and a solute-binding protein (MelE) (PubMed:31138628). The complex involved in polygalacturonan and rhamnogalacturonan type I uptake is probably composed of two ATP-binding proteins (MsmX), two transmembrane proteins (YtcP and YteP) and a solute-binding protein (YtcQ) (PubMed:29240795).
Antitoxin component of a type II toxin-antitoxin (TA) system. Antitoxin that directly inhibits activity of EndoA in vitro. Upon expression in E.coli counteracts inhibitory effect of endoribonuclease EndoA. The EndoA-EndoAI complex does not seem to bind its own promoter (PubMed:24120662).
Homodimer, forms a heterohexamer composed of alternating toxin and antitoxin homodimers which inhibits the toxin's endoribonuclease activity. Antitoxin prevents RNA binding to the endoribonuclease (PubMed:24120662).
Belongs to the manganese catalase family.
Catalyzes the decomposition of hydrogen peroxide into water and oxygen.
Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Member of the two-component regulatory system LytS/LytT that probably regulates genes involved in cell wall metabolism.
Belongs to the histidinol dehydrogenase family.
Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
Belongs to the drug/metabolite transporter (DMT) superfamily. Small multidrug resistance (SMR) (TC 2.A.7.1) family. EbrA/EbrB subfamily.
Part of a multidrug efflux pump. Confers resistance to cationic lipophilic dyes such as ethidium bromide, acriflavine, pyronine Y and safranin O. The efflux is probably coupled to an influx of protons (By similarity).
The efflux pump is composed of EbrA and EbrB.
Part of the binding protein-dependent transport system for oligopeptides. Probably responsible for energy coupling to the transport system. Required for sporulation and competence.
Belongs to the universal ribosomal protein uL10 family.
Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors (such as IF-2, EF-Tu, EF-G and RF3).
Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.
Part of the ribosomal stalk of the 50S ribosomal subunit. The N-terminus interacts with L11 and 23S rRNA to form the base of the stalk. The C-terminus forms an elongated spine to which L12 dimers bind in a sequential fashion forming a pentameric L10(L12)2(L12)2 complex.
Part of the ribosomal stalk of the 50S ribosomal subunit. The N-terminus interacts with L11 and the large rRNA to form the base of the stalk. The C-terminus forms an elongated spine to which L12 dimers bind in a sequential fashion forming a multimeric L10(L12)X complex.
Belongs to the ABC-4 integral membrane protein family. FtsX subfamily.
Cells lacking this gene and ftsE, the previous gene in the operon, delay sporulation onset, as a result of which they form a medial rather than polar septum at the onset of sporulation. This is presumably due to slower phosphorylation and activation of the spo0A transcriptional regulator. However, at later time points these cells undergo polar division and eventually form smaller than wild-type mature spores.
Interacts with FtsE (Probable). Interacts with FloT (PubMed:23651456).
Part of the ABC transporter FtsEX involved in asymmetric cellular division facilitating the initiation of sporulation.
Part of the ABC transporter FtsEX involved in asymmetric cellular division facilitating the initiation of sporulation. May act as an importer, possibly at the top of a hierarchical cascade leading to the correct temporal initiation of sporulation. Acts upstream of the histidine kinases KinA, KinB and KinC, the RapA phosphatase and the Spo0A sporulation protein.
Cells lacking this gene do not grow on arginine as a sole nitrogen source, but do grow on ornithine or ammonium chloride.
Part of the rocDEF operon. Expression is sigma L dependent, induced by arginine, ornithine or proline.
Belongs to the methylthiotransferase family. MtaB subfamily.
Catalyzes the methylthiolation of N6-threonylcarbamoyladenosine (t(6)A), leading to the formation of 2-methylthio-N6-threonylcarbamoyladenosine (ms(2)t(6)A) at position 37 in tRNAs that read codons beginning with adenine.
By cold shock (at protein level) (PubMed:8755892). Expression is sigma W-dependent; induced by alkali stress and by infection with phage SPP1 (PubMed:11454200).
Belongs to the anthranilate synthase component I family.
Heterotetramer consisting of two non-identical subunits: a beta subunit (TrpG) and a large alpha subunit (TrpE).
Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia (By similarity).
Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia.
Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
Belongs to the universal ribosomal protein uL22 family.
The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.
This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity).
This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g., L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.
Deletion of the yxiB-yxiC-yxiD-yxxD-yxxE operon has no visible growth phenotype, however it is out-competed by wild-type cells.
Inhibits the initiation of sporulation, Spo0J antagonizes this inhibition. Soj ultimately inhibits the activation (phosphorylation) of Spo0A.
Not required for sporulation or for chromosome partioning.
Belongs to the polysaccharide lyase 11 family.
Binds 10 calcium ions. The calcium may have a structural role.
Divalent metal cations. Has highest activity with Mn(2+), followed by Zn(2+) and Co(2+).
Pectinolytic enzyme that degrades type I rhamnogalacturonan from plant cell walls and releases disaccharide products (PubMed:17449691, PubMed:19193638). Degrades rhamnogalacturonan, polygalacturonic acid and pectic acid. Has very low activity on pectin (PubMed:17449691).
This enzyme is expected to be secreted, but there is no predicted signal sequence.
Belongs to the beta sliding clamp family.
Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP-independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of replication as well as for processivity of DNA replication.
Forms a ring-shaped head-to-tail homodimer (PubMed:25170813) around DNA which binds and tethers DNA polymerases and other proteins to the DNA. The DNA replisome complex has a single clamp-loading complex (3 tau and 1 each of delta, delta', psi and chi subunits) which binds 3 Pol III cores (1 core on the leading strand and 2 on the lagging strand) each with a beta sliding clamp dimer. Additional proteins in the replisome are other copies of gamma, psi and chi, Ssb, DNA helicase and RNA primase.
Forms a ring-shaped head-to-tail homodimer around DNA.
Catalyzes the isomerization of 5-dehydro-4-deoxy-D-glucuronate to 3-deoxy-D-glycero-2,5-hexodiulosonate.
Expressed only in the mother cell compartment of sporulating cells.
Expression is GerE and sigma K-dependent.
Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step in folate biosynthesis pathway.
Member of a high affinity multicomponent binding-protein-dependent transport system for choline.
Belongs to the class II fructose-bisphosphate aldolase family. IolJ subfamily.
Binds 2 Zn(2+) ions per subunit. One is catalytic and the other provides a structural contribution.
Produces dihydroxyacetone phosphate (DHAP or glycerone phosphate) and malonic semialdehyde (MSA or 3-oxopropanoate) from 6-phospho-5-dehydro-2-deoxy-D-gluconate (DKGP).
Belongs to the azoreductase type 2 family.
Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADPH, but not NADH, as an electron donor for its activity.
Part of the yhcYZ-yhdA operon that is induced by the two-component regulatory system LiaS/LiaR in response to cell envelope stress.
Belongs to the cytochrome c oxidase subunit 2 family.
Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
Inhibits cell division during the SOS response. Affects a later stage of the cell division protein assembly, after the assembly of the Z ring, by probably suppressing recruitment of FtsL and/or DivIC to the division machinery (By similarity).
Inhibits cell division during the SOS response. Affects a later stage of the cell division protein assembly, after the assembly of the Z ring, by probably suppressing recruitment of FtsL and/or DivIC to the division machinery.
Heme-containing signal transducer responsible for aerotaxis, the migratory response toward or away from oxygen.
Possible role in the secretion of LytB and LytC.
Cells lacking this gene have an increased sigma-B activity in response to salt and ethanol stress and also increased sigma-B activity in response to the energy stress associated with entry into stationary phase. These results indicate that this protein is a negative regulator of sigma-B activity.
Interacts with RsbRA and RsbS in the stressosome. The stressosome probably also contains RsbRC and RsbRD.
Belongs to the glycosyl hydrolase 16 family.
Beta-glucanases of Bacillus have a substrate range similar to lichenase of germinating barley.
Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
Constitutively expressed during exponential growth. Encoded in an operon with ydiS and ydjA.
Cells lacking this gene grow normally in minimal medium or in high-osmolarity environments, and exhibit the same survival capacity as the wild-type strain upon a drastic osmotic downshift. They sporulate and germinate normally. Combination with an MscL mutation enhances the osmosensitivity of MscL mutants subsequent to a hypo-osmotic shock.
Expression is sigma B-dependent. Induced by high salt concentrations.
Cells lacking this gene show no noteworthy improvement of beta-toxoid secretion.
Highly expressed in the late exponential phase.
Overexpression of ykoJ is lethal to B.subtilis.
Up-regulated under secretion stress conditions in a CssR/CssS-dependent manner.
High-affinity potassium transporter (PubMed:28420751, PubMed:32005818). Functions as a K(+)/H(+) symporter (PubMed:32005818).
Induced by low K(+) concentrations (PubMed:28420751). Expression is regulated by cyclic di-AMP (c-di-AMP), via the ydaO riboswitch (PubMed:20511502, PubMed:24141192, PubMed:28420751). High external concentrations of K(+) stimulate an increase in the production of c-di-AMP, which binds to the riboswitch and prevents kimA expression (PubMed:28420751).
Potassium uptake increases at lower external pH and is abolished by the proton ionophore carbonyl cyanide m-chlorophenylhydrazone (CCCP) (PubMed:32005818). Binds cyclic di-AMP (c-di-AMP), which inhibits the potassium transport activity (PubMed:31061098).
Belongs to the alpha-ketoglutarate dehydrogenase family.
E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
Homodimer. Part of the 2-oxoglutarate dehydrogenase (OGDH) complex composed of E1 (2-oxoglutarate dehydrogenase), E2 (dihydrolipoamide succinyltransferase) and E3 (dihydrolipoamide dehydrogenase); the complex contains multiple copies of the three enzymatic components (E1, E2 and E3).
Belongs to the aldehyde dehydrogenase family. RocA subfamily.
Expression is sigma L dependent and induced by arginine.
Belongs to the glycosyl hydrolase 13 family.
By ethanol, heat and salt via sigma B-dependent promoter.
Belongs to the GHMP kinase family. GalK subfamily.
Catalyzes the transfer of the gamma-phosphate of ATP to D-galactose to form alpha-D-galactose-1-phosphate (Gal-1-P).
Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.
Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.
Expression increases gradually during the log phase of growth.
Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.
Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines (PubMed:17284825). Can reduce methyl red (PubMed:17284825).
Deletion mutant is sensitive to 2-MHQ and catechol.
Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones (Probable). Contributes to resistance to 2-methylhydroquinone (2-MHQ) and catechol (PubMed:17725564, PubMed:18208493). Exhibits NADH-dependent 2,6-dichloroindophenol (DCIP) oxidoreductase activity (PubMed:17284825).
Repressed by MhqR. Induced by thiol specific stress conditions, such as exposure to 2-methylhydroquinone (2-MHQ), catechol or diamide. Not induced by oxidative stress due to hydrogen peroxide or methylglyoxal.
Strongly inhibited by Pb(2+) and weakly inhibited by Cu(2+), Hg(2+) and Fe(2+). Stable in presence of Ag(+).
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity).
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
Phosphorylated on threonine residue(s). Phosphorylated by PrkC and dephosphorylated by PrpC, in vitro.
Activates transcription of the putBCP operon. Requires proline as a coactivator.
Mutant loses the ability to utilize proline as either sole nitrogen or sole carbon source.
PrcR expression is not subject to autoregulation and proline induction.
MotA and MotB comprise the stator element of the flagellar motor complex. Required for rotation of the flagellar motor. Probable transmembrane proton channel (By similarity).
Belongs to the universal ribosomal protein uS2 family.
Part of the 30S ribosomal subunit (PubMed:30126986). Interacts with BrxC (PubMed:33722570).
Belongs to the uroporphyrinogen decarboxylase family.
Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Belongs to the iron-sulfur dependent L-serine dehydratase family.
Heterodimer of an alpha chain and a beta chain.
By Spo0A during nutrient starvation, through its direct negative control of AbrB (PubMed:12817086). Repressed by AbrB during regular growth when nutrients are plentiful, in association with the transcriptional repressor Abh (PubMed:17720793). Protein not detected during exponential growth, accumulates during stationary phase (at protein level) (PubMed:14568161).
Produces a 42-residue extracellular sporulation delaying protein (SDP) that collapses the proton motive force (probably both the membrane potential and pH gradient) across the cell membrane, which leads to autolysis; may form a proton channel (PubMed:22469514). Induces the lysis of other B.subtilis cells that have not entered the sporulation pathway, inducing cannibalism to provide a source of nutrients to support sporulation, and at the same time delaying commitment to the energetically expensive and irreversible onset of sporulation (PubMed:12817086). Addition of SDP to liquid cultures halts growth, leads to increased cell permeability and eventually cell lysis in a significant subset of the population, although some cells survive and resume growth after a lag period (PubMed:20805502). Effects of SDP are irreversible within 10 minutes (PubMed:22469514). Addition of SDP to solid cultures induces killing, it is much more effective than SKF (AC O31422) (PubMed:20805502). Has antibiotic action against Gram-positive Firmicutes (L.acidophilus, M.megaterium, P.polymyxa, S.aureus, S.epidermidis) but not Actinobacteria M.luteus or Gram-negative P.aeruginosa or K.pneumoniae (PubMed:20805502, PubMed:22469514). SDP induces expression of the sdpR-sdpI operon (PubMed:12817086). Its maturation is dependent on SdpA and SdpB. Also functions as a ligand, binds to SdpI triggering a signal transduction cascade that protects the cell against the toxic effects of its own SDP.
Production of active SDP (able to induce SdpI and kill cells) is a multi-step process that requires signal peptide cleavage (probably by SipS or SipT) (PubMed:14568161) as well as SdpA and SdpB. The disulfide bond is not required for maximum toxicity (PubMed:23687264).
Proprotein probably interacts with chaperone CsaA.
When the sdpA-sdpB-sdpC operon is deleted, increased rate of spore formation; a double operon deletion (sdpA-sdpC plus skfA-skfH) makes spores even faster (PubMed:12817086). In a single gene deletion no SDP is produced (PubMed:20805502, PubMed:23687264).
Belongs to the D-glutamate cyclase family.
Specifically adenylates L-threonine and, to a lesser extent, glycine and covalently loads both amino acids onto their corresponding peptidyl carrier domains.
The phosphoserine observed at Ser-996 in PubMed:17218307 undoubtedly results from the secondary neutral loss of pantetheine from the phosphodiester linked cofactor.
Belongs to the arsenical resistance-3 (ACR3) (TC 2.A.59) family.
Deletion of the arsB gene results in both an aresenite- and arsenate-sensitive phenotype in the absence of IPTG.
Seems to confer resistance to arsenite by allowing cells to extrude this compound. Could be part of an arsenite extrusion pump.
Belongs to the metallo-dependent hydrolases superfamily.
Member of the two-component regulatory system YhcY/YhcZ.
Together with RNA polymerase sigma factor SigO, positively regulates the expression of at least three operons, including oxdC-yvrL, sigO-rsoA and yvrJ. Required for the acid stress-dependent induction of the oxalate decarboxylase oxdC.
Activity is controlled at multiple levels (PubMed:22812682). Regulation includes a positive autoregulatory loop on mgsR transcription and a post-translational redox-sensitive activation step by an intramolecular disulfide bond formation in response to ethanol stress (PubMed:22812682). In addition, protein stability is strictly controlled by rapid proteolytic degradation by the ClpXP and ClpCP proteases (PubMed:22812682, PubMed:32477307). The McsB protein-arginine kinase might serve as a proteolytic adapter for the ClpX ATPase in the degradation mechanism of MgsR (PubMed:32477307).
Deletion of the gene results in differential expression of approximately 70 genes in response to ethanol stress compared with the wild-type strain.
Expression is sigma B-dependent (PubMed:11544224, PubMed:18643936). Induced by ethanol, heat and salt stress (PubMed:11544224, PubMed:18643936). Positively autoregulated (PubMed:22812682).
Regulates transcription of a subregulon within the general stress response (PubMed:18643936). Exerts positive and negative effects in response to ethanol stress (PubMed:18643936).
Activates transcription of the bmr gene in response to structurally dissimilar drugs. Binds rhodamine as an inducer.
Belongs to the ketol-acid reductoisomerase family.
Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. All amino acids serve as attractants in B.subtilis, they appear to cause an increase in the turnover methyl groups, leading to methylation of an unidentified acceptor, while repellents have been shown to cause a decrease in methyl group turnover. The methyl groups are added by a methyltransferase and removed by a methylesterase. McpB is required for taxis towards asparagine, aspartate, glutamine, and histidine.
Only chemotaxis towards asparagine is completely deficient in the absence of McpB.
Some glutamine residues are deamidated to glutamate by CheD and subsequently methylated.
The demethylation is selective. Gln-371 is demethylated only upon asparagine addition whereas Glu-637 is demethylated only upon asparagine removal. Glu-630 appears indiscriminate and is demethylated upon both addition and removal of asparagine.
Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD).
Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.
Inhibited by pyrrolidine dione antibiotics moiramide B (CPD1) and CPD2.
Belongs to the ClpA/ClpB family. ClpC subfamily.
Competence gene repressor; required for cell growth at high temperature. Negative regulator of comK expression. May interact with MecA to negatively regulate comK.
Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella and sporulation.
Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
Belongs to the ammonia transporter channel (TC 1.A.11.2) family.
Cells grow poorly at pH 5.5 and not at all at pH 5.0 with ammonium as their sole nitrogen source (PubMed:14600241). They are unable to transport the ammonium analog methylammonium, and thus probably also ammonium (PubMed:14600241). In the absence of nitrogen source, cells lacking this gene do not show degradation of TnrA, which is entirely soluble (PubMed:17001076, PubMed:21435182).
Functions as an ammonium and methylammonium transporter in the absence of glutamine (PubMed:14600241). Required for ammonium utilization at low concentrations or at low pH values, when ammonium is the single nitrogen source (PubMed:14600241). Required for binding of NrgB to the membrane (PubMed:14600241). Interaction between GlnK-AmtB complex and TnrA protects TnrA from proteolytic degradation (PubMed:17001076, PubMed:21435182).
Interacts with NrgB for a correct localization of the latter. GlnK-AmtB complex interacts with TnrA.
The nrgAB operon is activated by TnrA (PubMed:12823818). NrgB is required for full induction of the operon under conditions of ammonium limitation (PubMed:14600241, PubMed:10864496).
Belongs to the Mu gp47/PBSX XkdT family.
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
A double wapA-wapI deletion strain is growth inhibited when cocultured with wild-type cells. When wapI is reintroduced it restores growth in a cognate toxin-dependent fashion (PubMed:23572593). Growth inhibition by wild-type cells is strongest on LB medium and less effective on media that promote biofilm formation (MSgg and 2xSGG) (PubMed:34280190).
Belongs to the RHS/WapA nuclease family.
Constitutively and highly expressed on solid and in liquid medium, with or without biofilm formation, by 12 hours of culture. Repressed by DegU.
Detected in exponentially growing cells as many processing products, protein disappears upon entry into stationary phase with the concomitant appearance of smaller products. The large products persist in the absence of the extracellular serine protease Epr (PubMed:11987133).
Has two ligand-binding domains; the N-terminus has three 101 AA repeats which are responsible for cell wall binding; the C-terminus consists of two blocks of residues with a conserved motif repeated 31 times.
Identified in the extracellular proteome as many processing products ranging from over 85 kDa to about 30 kDa. One of these probably starts on Ser-1726. Two forms are known as CWBP62 and CWBP105 (PubMed:11987133).
Toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. A site-specific general tRNA nuclease, the C-terminus (residues 2201-2334) removes 2 or 4 nucleotides from the 3' end of at least 4 tRNAs (upon expression in E.coli), possibly endonucleolytically. The nuclease activity is neutralized by expression of the cognate immunity protein WapI from the same strain, but not its homolog from 2 other B.subtilis strains. The C-terminus cannot be expressed on its own in E.coli, however it can be cloned in the presence of its cognate immunity protein gene. Cell contact is necessary for growth inhibition (PubMed:23572593). Unlike the LXG toxin-immunity modules, WapAI mediates competition under shaking culture conditions (PubMed:34280190).
Binds 2 heme groups per subunit. Heme 1, called the proximal or heme Bp in, is located at the cytoplasmic interface, heme 2, called the distal or heme Bd, is located at the periplasmic interface. Electrons are transferred from the periplasmic to the cytoplasmic heme.
The gamma chain is a membrane-embedded heme-iron unit resembling cytochrome b, which transfers electrons from quinones to the beta subunit.
Belongs to the ribulose-phosphate 3-epimerase family.
Binds 1 divalent metal cation per subunit.
Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.
Disruption of the gene does not affect growth of the cell.
Enhanced expression can restore both growth and sporulation of a temperature-sensitive mutation in rplB, designated rplB142.
May assist in the assembly of the 50S subunit.
Monomer. Heterodimer consisting of two non-identical subunits: a glutamine amidotransferase subunit (PabA) and a aminodeoxychorismate synthase subunit (PabB) (By similarity).
Part of a heterodimeric complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p-aminobenzoate (PABA) and tetrahydrofolate. In the first step, a glutamine amidotransferase (PabA) generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by aminodeoxychorismate synthase (PabB) to produce ADC. PabA converts glutamine into glutamate only in the presence of stoichiometric amounts of PabB. Also involved in the biosynthesis of anthranilate (By similarity). Complements a glutamine amidotransferase-negative mutant (PubMed:2123867).
Requires tryptophan and has a partial requirement for p-aminobenzoic acid for growth.
Divalent metal cations; Mg(2+) > Mn(2+) > Ca(2+).
Not essential. Accumulation of precursor forms of 5S rRNA in total, ribosomes and polysome RNA preparations; smaller forms (126 and 135 nucleotides) are predominantly found in ribosomes and polysomes. Each of the 10 rrn operons gives rise to a different 5S rRNA precursor due to differences in their 3' ends.
Required for correct processing of both the 5' and 3' ends of 5S rRNA precursor. Cleaves both sides of a double-stranded region yielding mature 5S rRNA in one step.
Required for correct processing of both the 5' and 3' ends of 5S rRNA precursor. Cleaves both sides of a double-stranded region yielding mature 5S rRNA in one step. Releases 5'-phosphoryl and 3'-hydroxy termini.
Requires ribosomal protein L18 (rplR) for catalysis; it can be replaced by 30% dimethylsulfoxide suggesting L18 functions as an rRNA folding chaperone.
Belongs to the methyltransferase superfamily. RlmA family.
Member of the two-component regulatory system BceS/BceR involved in the regulation of bacitracin resistance. When activated by BceS, binds to the upstream region of the bceAB promoter and up-regulates the expression of these two genes.
Belongs to the metallo-dependent hydrolases superfamily. Allantoinase family.
Carboxylation allows a single lysine to coordinate two zinc ions.
Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring.
Expression is very low in excess nitrogen (glutamate plus ammonia) and is induced during limiting-nitrogen conditions (glutamate). Expression is further induced when allantoin or allantoate are added during limiting-nitrogen conditions.
Binds 1 divalent metal cation per subunit. Can use Mn(2+), Fe(2+) or Co(2+).
Involved in the reversible interconverion of 2-keto-myo-inositol (2KMI, inosose or 2,4,6/3,5-pentahydroxycyclohexanone) to 1-keto-D-chiro-inositol (1KDCI or 2,3,5/4,6-pentahydroxycyclohexanone).
Belongs to the AB hydrolase superfamily. Epoxide hydrolase family.
Belongs to the class-D beta-lactamase family.
Belongs to the glycosyl hydrolase 43 family.
Cleaves arabinose units from O-2- or O-3-monosubstituted xylose residues, thereby assisting in arabinoxylan (AX) and short-chain arabinoxylo-oligosaccharide (AXOS) degradation. Is more active on wheat bran AXOS than on wheat water-extractable AX and rye water-extractable AX. Does not display endoxylanase, xylosidase or arabinanase activity.
The CBM6 domain lost its carbohydrate binding capacity.
Belongs to the acyltransferase 3 family.
Involved in the biosynthesis of kanosamine (3-amino-3-deoxy-D-glucose), which is known to have antibiotic and antifungal properties, and to be a precursor of the antibiotic neotrehalosadiamine (3,3'-diamino-3,3'-dideoxy-alpha,beta-trehalose (NTD)). Catalyzes the dephosphorylation of kanosamine 6-phosphate to yield kanosamine. There is a trace amount of activity using glucosamine-6-phosphate.
The production of neotrehalosadiamine is dormant in the wild-type strain. A mutation in the beta subunit of RNA polymerase activates the production of the neotrehalosadiamine (PubMed:14612444).
Member of the two-component regulatory system YdfH/YdfI. May activate YdfI by phosphorylation.
Member of the two-component regulatory system BceS/BceR involved in the regulation of bacitracin resistance. Activates BceR in response to extracellular bacitracin.
Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
Homodimer; disulfide-linked, upon oxidation.
The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this typical 2-Cys peroxiredoxin, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide.
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
Constitutively expressed, part of the cdaA-cdaR-glmM-glmS operon (PubMed:23192352).
Involved in bacillithiol (BSH) biosynthesis. Catalyzes the second step of the pathway, the deacetylation of N-acetylglucosaminylmalate (GlcNAc-Mal) to glucosamine malate (GlcN-Mal).
Mutant shows a 2-fold reduction in bacillithiol levels. BshB1/bshB2 double mutant does not produce bacillithiol.
Belongs to the transglycosylase MltG family.
Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
Belongs to the radical SAM superfamily. MoaA family.
Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and the GTP-derived substrate.
Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate (By similarity). Required for both nitrate assimilation and respiration.
Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.
Homodimer. Heterotetramer of two MnmE and two MnmG subunits.
NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Cannot grow on sulfate, sulfite or butanesulfonate as sole sulfur source.
Transcriptional activator of the cysJI operon which is involved in sulfur assimilation. Also negatively regulates its own transcription.
Cells lacking this gene show no difference in growth under copper deprivation or copper excess conditions.
Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate (PubMed:28830929). In addition, is a potent inhibitor of the autophosphorylation reaction of kinase A (kinA) and its reverse reaction, but does not inhibit phosphate transfer to the Spo0F response regulator once kinase A is phosphorylated. Is an inhibitor of the catalytic domain of kinase A affecting the ATP/ADP reactions and not the phosphotransferase functions of this domain. The inhibition is non-competitive with respect to ATP (PubMed:9334321).
Deletion of the gene enhances sporulation (PubMed:9334321). Deletion mutant grows less well than wild type on minimal medium with ammonium as nitrogen source and cannot grow on 5-oxoproline. Mutant lacks 5-oxoprolinase activity and accumulates 5-oxo-L-proline (PubMed:28830929).
Forms a complex composed of PxpA, PxpB and PxpC (PubMed:28830929). Interacts with PxpC (KipA) (PubMed:9334321, PubMed:21050859, PubMed:28830929). Interaction with PxpC prevents the inhibitory action of PxpB (KipI) (PubMed:9334321, PubMed:21050859). Interacts with KinA. Two PxpB monomers bind via their C-domains at a conserved proline in the KinA dimerization and histidine-phosphotransfer (DHp) domain (PubMed:18823995).
Belongs to the CPA3 antiporters (TC 2.A.63) subunit B family.
Forms a heterooligomeric complex that consists of seven subunits: MrpA, MrpB, MrpC, MrpD, MrpE, MrpF and MrpG.
Mrp complex is a Na(+)/H(+) antiporter that is considered to be the major Na(+) excretion system in B.subtilis. Has a major role in Na(+) resistance and a minor role in Na(+)- and K(+)-dependent pH homeostasis as compared to TetB. MrpA may be the actual Na(+)/H(+) antiporter, although the six other Mrp proteins are all required for Na(+)/H(+) antiport activity and Na(+) resistance. MrpA is required for initiation of sporulation when external Na(+) concentration increases. Also transports Li(+) but not K(+), Ca(2+) or Mg(2+).
Mrp-dependent antiport apparently occurs by a secondary, proton motive force-dependent mechanism, but the similarity of several Mrp proteins to membrane-embedded subunits of energy-coupled NADH dehydrogenase complexes raises the possibility that there is a capacity for electron transport that could provide a primary energy coupling option for Mrp functions.
Involved in DNA repair and RecF pathway recombination.
Plays a role in DNA double-stranded break repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecR. Is recruited to repair centers, foci that are the site of double-strand break(s) after RecN and before RecF; may actively recruit RecF.
Recruited to foci following DNA damage; probably interacts with RecF.
Found in association with the 30S subunit of the ribosome.
Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)). Uses ammonia as nitrogen donor.
Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons.
Recruited to foci following DNA damage; probably interacts with RecO.
The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP.
The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP. Is recruited to repair centers, foci that are the site of double-strand DNA break(s) after RecN and RecO; recruitment may depend on RecO.
The TIR domain mediates NAD(+) hydrolase (NADase) activity. Self-association of TIR domains is required for NADase activity.
Contains an N-terminal zinc-binding domain, a central core domain that contains the primase activity, and a C-terminal DnaB-binding domain.
RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
Transcriptionally regulated by sigma-D factor.
Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.
Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Expressed under the control of the sigma-W factor.
May mediate a negative feedback loop that down-regulates the expression of the sigma-W regulon following the activation of sigma-W in response to conditions of cell envelope stress. Might interact with and inhibit the activity of the protease PrsW, or could bind to the anti-sigma-W factor RsiW and thereby protect it from PrsW-mediated cleavage.
Belongs to the trans-sulfuration enzymes family.
Catalyzes the formation of L-cystathionine from O-acetyl-L-homoserine and L-cysteine. Cannot use O-succinyl-L-homoserine as substrate. Also exhibits O-acetylhomoserine thiolyase activity, catalyzing the synthesis of L-homocysteine from O-acetyl-L-homoserine and sulfide.
Cells lacking this gene are unable to grow in the presence of sulfate or cysteine as sole sulfur source, whereas their growth in the presence of homocysteine, cystathionine or methionine is similar to that of the wild-type strain.
Up-regulated at the transcriptional level when sulfate, cysteine, cystathionine or homocysteine are the sulfur sources. Repressed by methionine.
Belongs to the bacterial sortase family.
Compared to other sortases, it is shorter and lacks the N-terminal membrane anchor. It may lack activity.
Mutation does not affect extracellular levels of the sortase substrate YfkN.
Preferentially expressed in the late stationary phase.
Seems not to play a major role if any as a sortase.
Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
Deletion mutant lacks the ac(4)C34 modification and displays a cold-sensitive phenotype.
Belongs to the radical SAM superfamily. Biotin synthase family.
Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine.
Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
Belongs to the beta-class carbonic anhydrase family.
Belongs to the AIR carboxylase family. Class I subfamily.
Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR).
Forms a complex with TatAy. Two types of complexes exist: one composed of TatAy and TatCy, and another composed only of TatAy.
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Required for YwbN secretion.
Deletion of the gene has a negative impact in the utilization of polygalacturonan and rhamnogalacturonan type I.
Involved in pectin degradation (PubMed:29240795). Part of the ABC transporter complex YtcQP-YteP involved in the uptake of polygalacturonan and rhamnogalacturonan type I (PubMed:29240795).
The complex is probably composed of two ATP-binding proteins (MsmX), two transmembrane proteins (YtcP and YteP) and a solute-binding protein (YtcQ).
Belongs to the purine-cytosine permease (2.A.39) family.
Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily.
Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile).
IleRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated valine is translocated from the active site to the editing site, which sterically excludes the correctly activated isoleucine. The single editing site contains two valyl binding pockets, one specific for each substrate (Val-AMP or Val-tRNA(Ile)).
Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate.
Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Prokaryotic clade 'B1' sub-subfamily.
Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Homotetramer. Component of a possible RNA degradosome complex composed of rny, rnjA, rnjB, pnp, pfkA and eno (PubMed:19193632) (although rnjA and rnjB's presence is unclear). Specifically interacts with RNase Y (rny, PubMed:21803996) and enolase (eno, PubMed:22198292). Interacts with BrxC (PubMed:33722570).
Activated by the cyclic di-AMP (c-di-AMP) receptor DarB in the absence of c-di-AMP (PubMed:35130724). Allosterically activated by acetyl-CoA (PubMed:4146915, PubMed:35130724). Inhibited by the biotin-complexing protein avidin (PubMed:4146915).
Catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second, leading to oxaloacetate production (PubMed:4146915). Fulfills an anaplerotic function in B.subtilis as it is necessary for growth on glucose, but is not required for sporulation (PubMed:4146915).
Catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second.
Homotetramer (Probable). At very low potassium concentrations, when intracellular levels of c-di-AMP are low, interacts with apo-DarB (PubMed:35130724). c-di-AMP inhibits the binding of DarB to PYC (PubMed:35130724). Does not bind directly c-di-AMP (PubMed:35130724).
Belongs to the FAD-binding oxidoreductase/transferase type 4 family.
Component of a complex that catalyzes the oxidation of glycolate to glyoxylate. Is also able to oxidize D-lactate ((R)-lactate). Does not link directly to O(2), and 2,6-dichloroindophenol (DCIP) and phenazine methosulfate (PMS) can act as artificial electron acceptors in vitro, but the physiological molecule that functions as primary electron acceptor during glycolate oxidation is unknown.
The glycolate oxidase likely consists of several subunits including GlcD and GlcF.
Expressed during the later stages of sporulation.
Expression is regulated by the mother cell-specific transcription factors sigma K and GerE.
Spore protein involved in the assembly of several components of the spore coat, including CotB, CotG and CotH, and in spore germination.
Spores of the null mutant show partial lack of assembly of several coat components, including CotB, CotG and CotH, and impairment of response during germination.
Regulator of the spore photoproduct lyase operon (splAB).
Repressed by presence of biotin, under control of BirA. Probably part of the bioY-yhfST operon.
Has 3 domains, the large (RuvB-L) and small ATPase (RuvB-S) domains and the C-terminal head (RuvB-H) domain. The head domain binds DNA, while the ATPase domains jointly bind ATP, ADP or are empty depending on the state of the subunit in the translocation cycle. During a single DNA translocation step the structure of each domain remains the same, but their relative positions change.
Homohexamer. Forms an RuvA(8)-RuvB(12)-Holliday junction (HJ) complex. HJ DNA is sandwiched between 2 RuvA tetramers; dsDNA enters through RuvA and exits via RuvB. An RuvB hexamer assembles on each DNA strand where it exits the tetramer. Each RuvB hexamer is contacted by two RuvA subunits (via domain III) on 2 adjacent RuvB subunits; this complex drives branch migration. In the full resolvosome a probable DNA-RuvA(4)-RuvB(12)-RuvC(2) complex forms which resolves the HJ (By similarity). Homohexamer which interacts with RecU (PubMed:19422832).
Homohexamer. Forms an RuvA(8)-RuvB(12)-Holliday junction (HJ) complex. HJ DNA is sandwiched between 2 RuvA tetramers; dsDNA enters through RuvA and exits via RuvB. An RuvB hexamer assembles on each DNA strand where it exits the tetramer. Each RuvB hexamer is contacted by two RuvA subunits (via domain III) on 2 adjacent RuvB subunits; this complex drives branch migration. In the full resolvosome a probable DNA-RuvA(4)-RuvB(12)-RuvC(2) complex forms which resolves the HJ.
The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. RuvB forms 2 homohexamers on either side of HJ DNA bound by 1 or 2 RuvA tetramers; 4 subunits per hexamer contact DNA at a time. Coordinated motions by a converter formed by DNA-disengaged RuvB subunits stimulates ATP hydrolysis and nucleotide exchange. Immobilization of the converter enables RuvB to convert the ATP-contained energy into a lever motion, pulling 2 nucleotides of DNA out of the RuvA tetramer per ATP hydrolyzed, thus driving DNA branch migration. The RuvB motors rotate together with the DNA substrate, which together with the progressing nucleotide cycle form the mechanistic basis for DNA recombination by continuous HJ branch migration. Branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves cruciform DNA.
Tetramer of two alpha and two beta chains.
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP. CheR is responsible for the chemotactic adaptation to repellents.
Part of the ABC transporter complex YxdLM which could be involved in peptide resistance. Responsible for energy coupling to the transport system (Probable).
Negatively regulates yodC and azoR1 which may contribute to the degradation of aromatic compounds. Probably positively regulates the catechol-specific transcription of mhqNOP, mhqED, and mhqA.
Repressed by 2-methylhydroquinone (2-MHQ), diamide and catechol stress.
Involved in the meta cleavage of catechol to 2-hydroxymuconic semialdehyde. Essential for growth and viability in the presence of catechol and probably involved in the detoxification of catechol.
Strongly induced by catechol, less strongly by 2-methylhydroquinone (2-MHQ) but only weakly by chromanon (6-brom-2-vinyl-chroman-4-on).
Cell wall formation. May be involved in outgrowth of the germinated spore or it could function in the synthesis of the germ cell wall.
Expression remains constant during vegetative growth, decreases during early sporulation, and is induced in the forespore during late sporulation.
In the C-terminal section; belongs to the transpeptidase family.
In the N-terminal section; belongs to the glycosyltransferase 51 family.
The PTS EIIA type-3 domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the PTS EIIB type-3 domain.
Part of an ABC transporter complex involved in the uptake of guanosine (PubMed:21926227). Responsible for energy coupling to the transport system (Probable). May be a nucleoside transporter of broad specificity but with various affinities for different substrates (PubMed:21926227).
Belongs to the ABC transporter superfamily. SunT family.
SunT (TC 3.A.1.112.4) is required for production of the lantibiotic sublancin-168, probably by both processing the signal peptide and exporting the resulting mature lantibiotic.
Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
Catalyzes the reversible deamination of L-leucine to 4-methyl-2-oxopentanoate.
Deletion of the yokI-yokJ operon has no visible growth phenotype, however it is out-competed by wild-type cells.
Expressed on rich and minimal solid media likely in early stationary phase; not dependent on DegSU. Not expressed in liquid LB, but only under conditions that promote biofilm formation.
Immunity component of one of 6 LXG toxin-immunity modules in this strain. They promote kin selection, mediate competition in biofilms, and drive spatial segregation of different strains, indicating that LXG toxins may help avoid warfare between strains in biofilms. Mediates intercellular competition during biofilm formation; disruption of the operon disadvantages the bacteria, but overexpression of the cognate immunity protein restores growth in competition with wild-type. In situ neutralizes the toxic effect of cognate toxin YokI (PubMed:34280190). Neutralizes the ability to inhibit growth of cognate toxin YokI upon expression in E.coli. Does not have immunity protein activity on other LXG toxins (PubMed:22200572).
Probably interacts with cognate toxin YokI but not with other non-cognate toxins. The interaction inhibits the toxic activity of YokI (Probable).
No visible phenotype, no effects on FloA or FloT membrane rafts.
ATPase activity is stimulated by interaction with RNA.
Belongs to the DEAD box helicase family. DbpA subfamily.
Contains an N-terminal domain that binds non-specifically to RNA and a C-terminal domain that binds specifically and tightly to hairpin 92 of 23S rRNA.
Contains an N-terminal domain that binds non-specifically to RNA and a C-terminal domain that binds specifically and tightly to hairpin 92 of 23S rRNA. Undergoes a conformation change in the helicase core upon binding of RNA and ATP.
DEAD-box RNA helicase involved in the assembly of the 50S ribosomal subunit. Has an RNA-dependent ATPase activity, which is specific for 23S rRNA, and a 3' to 5' RNA helicase activity that uses the energy of ATP hydrolysis to destabilize and unwind short rRNA duplexes (Probable).
DEAD-box RNA helicase involved in the assembly of the 50S ribosomal subunit. Has an RNA-dependent ATPase activity, which is specific for 23S rRNA, and a 3' to 5' RNA helicase activity that uses the energy of ATP hydrolysis to destabilize and unwind short rRNA duplexes.
May interact with RNA helicases CshA and CshB.
No visible effect at 37 or 16 degrees Celsius; no change in ribosome profiles. A quadruple disruption of all RNA helicases (cshA, cshB, deaD, yfmL) is not lethal at 37 degrees Celsius, although both 50S and 70S ribosomes are decreased, while growth stops at 16 degrees.
H(+)-stimulated, divalent metal cation uptake system.
H(+)-stimulated, divalent metal cation uptake system. Involved in manganese uptake. Can probably also transport cadmium, cobalt, copper and zinc, but not iron. May be the predominant transporter of manganese during logarithmic phase growth.
Repressed by MntR in the presence of manganese.
Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 1 subfamily.
Catalyzes the ATP-dependent phosphorylation of fructose-l-phosphate to fructose-l,6-bisphosphate.
B.subtilis strain 168 possesses two thymidylate synthases, a major form ThyA and a minor form ThyB.
Belongs to the thymidylate synthase family. Bacterial-type ThyA subfamily.
Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
Belongs to the sodium:neurotransmitter symporter (SNF) (TC 2.A.22) family.
Catalyzes the desulfonation of aliphatic sulfonates.
Belongs to the bacterial ribosomal protein bS18 family.
Binds as a heterodimer with protein bS6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit.
Part of the 30S ribosomal subunit (PubMed:30126986). Forms a tight heterodimer with protein bS6 (By similarity).
Part of the 30S ribosomal subunit. Forms a tight heterodimer with protein bS6.
Strongly expressed during exponential growth, decreases 2-4-fold in stationary phase, part of the rpsF-ssbA-rpsR operon (PubMed:14762004). The operon is induced by DNA damage by mitomycin C (PubMed:14762004).
Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family.
Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
Could serve either a nutritional or an osmotic protection function.
Belongs to the TRAFAC class YlqF/YawG GTPase family. MTG1 subfamily.
Essential protein that is required for a late step of 50S ribosomal subunit assembly. Has GTPase activity that is stimulated by interaction with the immature 50S ribosome subunit. Binds to the 23S rRNA. Required for the association of ribosomal proteins RplP and RpmA with the large subunit.
Interacts with ctc. Interacts with the immature 50S ribosome subunit. 2 molecules of RbgA bind to one 50S subunit.
Required for a late step of 50S ribosomal subunit assembly. Has GTPase activity.
Homotrimer (By similarity). Interacts with FloT (PubMed:23651456).
In the presence of glutamate in the medium, the expression is reduced two-fold, at high potassium concentration (5 mM). In the absence of glutamate, the expression is about two-fold increased at the increased potassium concentration.
This carrier protein is part of the Na(+)-dependent, binding-protein-independent glutamate-aspartate transport system.
Belongs to the major facilitator superfamily. DHA1 family. PbuE (TC 2.A.1.2.25) subfamily.
Involved in the efflux of purine ribonucleosides, such as guanosine, adenosine and inosine, as well as purine bases guanine, adenine and hypoxanthine, and purine base analogs 2,6-diaminopurine, 6-mercaptopurine and 2-fluoroadenine. Therefore plays a role in maintaining the cellular purine base pools and protecting cells against toxic purine base analogs. Modulates expression of the purR and G-box regulons.
Up-regulated by adenine, via the adenine-dependent riboswitch. Also up-regulated by hypoxanthine and guanine.
Belongs to the threonine synthase family.
Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine.
Catalyzes the phosphorylation of D-xylulose to D-xylulose 5-phosphate.
Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.
Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Belongs to the aspartate/ornithine carbamoyltransferase superfamily. OTCase family.
Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.
Functions as a ribosomal silencing factor. Interacts with ribosomal protein uL14 (rplN), blocking formation of intersubunit bridge B8. Prevents association of the 30S and 50S ribosomal subunits and the formation of functional ribosomes, thus repressing translation.
Interacts with ribosomal protein uL14 (rplN).
Belongs to the OXA1/ALB3/YidC family. Type 2 subfamily.
Disruption decreases genetic competence by about 50%, significant loss of expression of ComGC, no effect on sporulation. A double spoIIIJ-yqjG deletion is lethal.
Mostly monomeric, it may also form dimers. Interacts with SpoIIIAE. Forms a complex with the F(1)F(0) ATP synthase in which can be found the alpha, beta, gamma, delta and epsilon subunits of F(1) and a, b and subunits of F(0). YqgA is found in the same complex.
Predominantly expressed in vegetative cells.
Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins (By similarity). Also involved in protein secretion processes. It has an overlapping, although partly distinct, function compared to SpoIIIJ(MisCB).
Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins.
Probably part of the ABC transporter complex MntABCD involved in manganese import. Probably responsible for energy coupling to the transport system.
The complex is probably composed of two ATP-binding proteins (MntB), two transmembrane proteins (MntC and MntD) and a solute-binding protein (MntA).
Interacts with the N-terminal D1 domain of dynamin-like protein DynA.
Involved in the response to the germinative mixture of L-asparagine, glucose, fructose and potassium ions (AGFK). Cannot stimulate germination in the absence of gerD and gerK gene products (fructose and glucose receptors respectively).
Dipicolinate synthase likely consists of DpaA and DpaB, since both proteins are required for DPA synthesis.
Disruption of this gene has no effect on vegetative growth but causes a sporulation defect, characterized by heat-sensitive spores devoid of DPA, which can be cured by supplementation with dipicolinate.
Is not expressed during vegetative growth; is expressed at stage 5 of sporulation specifically in the mother cell compartment, under the control of the sigma-K factor. Is repressed by GerE.
Together with DpaB, catalyzes the conversion of dihydrodipicolinate to dipicolinate (DPA), which constitutes up to 10% of the dry weight of the spore.
Flagellar protein that affects chemotactic events.
Adenine glycosylase active on G-A mispairs.
Base excision repair (BER) glycosylase that initiates repair of A:oxoG to C:G by removing the inappropriately paired adenine base from the DNA backbone, generating an abasic site product. 8-oxoguanine (oxoG) is a genotoxic DNA lesion resulting from oxidation of guanine; this residue is misread by replicative DNA polymerases, that insert adenine instead of cytosine opposite the oxidized damaged base. Shows a powerful dicrimination of A versus C, since it does not cleave cytosine in oxoG:C pairs. May also be able to remove adenine from A:G mispairs, although this activity may not be physiologically relevant.
Binds 1 [4Fe-4S] cluster. The cluster has a structural role.
Cells lacking this gene have a 100-fold increased spontaneous mutation frequency. A double mutM/mutY disruption has a 1000-fold increased spontaneous mutation frequency (PubMed:12483591). Triple ytkD/mutM/mutY disrupted strains show increased mutation rates during exponential and stationary phase (PubMed:19011023).
Expressed during exponential growth. Expressed as both a monocistronic transcript and a mutY-fabL-sspE transcript.
Binds 1 dipyrromethane group covalently.
Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
The porphobilinogen subunits are added to the dipyrromethane group.
Catalyzes the dehydration of inosose (2-keto-myo-inositol, 2KMI or 2,4,6/3,5-pentahydroxycyclohexanone) to 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione (D-2,3-diketo-4-deoxy-epi-inositol).
Belongs to the PA-phosphatase related phosphoesterase family.
Catalyzes the dephosphorylation of phosphatidylglycerophosphate (PGP) to phosphatidylglycerol. Also has undecaprenyl pyrophosphate phosphatase activity, required for the biosynthesis of the lipid carrier undecaprenyl phosphate.
Belongs to the multi antimicrobial extrusion (MATE) (TC 2.A.66.1) family.
Binds cyclic di-AMP (c-di-AMP) and is probably involved in c-di-AMP-mediated signaling pathways. In vitro, can also bind cyclic GMP-AMP (3'3'-cGAMP), with lower affinity, but not c-di-GMP or 2'3'-cGAMP.
Binds three molecules of c-di-AMP, each in a pocket located between two subunits. c-di-AMP binding is accompanied by conformational changes of both the fold and the position of the B-loop.
To B.subtilis spore coat polysaccharide biosynthesis protein SpsA.
A mutant in the N-terminal obg domain (Asp-92) impairs growth and ribosome association but has no effect on sporulation or the general stress regulon (GSR). Replacing the last 22 amino acids has no effect on growth or ribosome association, but eliminates sporulation and reduces the GSR, showing for the first time that growth promotion and the GSR phenotypes are separable.
An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family.
Estimated to be present at 6000 copies per cell.
Inhibited by GDP; less than 20 uM ppGpp stimulates the GTPase, while higher concentrations inhibit.
Monomer. Interacts with TasA (AC P54507) in pull-down experiments.
Necessary for the transition from vegetative growth to stage 0 or stage II of sporulation, but sporulation subsequent to these stages is unaffected at 45 degrees Celsius. This ts effect is probably due solely to the E-79 mutation. Required for expression of early sporulation genes, further suggesting a role in the induction of sporulation. Depletion effects on sporulation can be partially suppressed by missense mutations in spo0A. Strains depleted for obg stop growing after about 3 hours and do not induce the sigma-B factor following ethanol stress. It cofractionates with the ribosome and upstream stress response regulators RsbR, RsbS and RsbT in size fractionation columns, suggesting the ribosome might serve as a possible mediator of the activity of obg and the stress induction of sigma-B. In glycerol gradients partially associates with ribosomes; this is stabilized by a nonhydrolyzable GTP-analog and to a lesser extent GTP and GDP.
Cells show impaired growth on arginine as the nitrogen source.
Part of a binding-protein-dependent transport system for arginine.
Belongs to the phospholipase D family. Cardiolipin synthase subfamily.
Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol.
Cells lacking this gene show a lack of cardiolipin (PubMed:14973018). Cells appear normal, no effect on flotillin cluster numbers or size (PubMed:27362352).
Belongs to the MnmG family. TrmFO subfamily.
Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
Cells lacking this gene grow normally in both LB and SG media, and no difference in sporulation frequency can be observed.
Protease able to cleave casein in vitro.
Protease activity can be inhibited in vitro by either a zinc specific chelator, 1,10-phenanthroline, or a metal chelator, EDTA. The enzyme is resistant to phenylmethylsulfonyl fluoride and iodoacetic acid.
Although the enzyme shows to be able to complement hemF hemN double mutant and to accumulate coproporphyrinogen-III when the gene is disrupted, no oxygen-independent coproporphyrinogen-III oxidase activity has been shown. The exact role of this protein is still unknown.
Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemZ subfamily.
Cells lacking this gene accumulate coproporphyrin-III only under anaerobic conditions, however no obvious respiratory growth phenotype is observed under anaerobic conditions. The hemN hemZ double mutant do not abolish aerobic and anaerobic respiratory growth, however a reduction of growth is observed.
HemZ is able to complement a S.typhimurium hemF hemN double mutant under aerobic and anaerobic conditions, however under anaerobic growth conditions, the double mutant complemented with hemZ grows significantly faster.
Induced under anaerobic conditions and by hydrogen peroxide stress. It is also dependent on induction by ResDE, Fnr and ArfM.
Involved in the biosynthesis of porphyrin-containing compound.
Belongs to the aspartate-semialdehyde dehydrogenase family.
Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate.
Cells lacking the operon including this gene (ytxGH-brxC) have increased S-bacillithiolation of glyceraldehyde-3-phosphate dehydrogenases (GAPDHs) GapA and GapB in cells with increased basal levels of oxidative stress due to concomitant deletion of genes encoding for catalase (katA) and alkyl hydroperoxide reductase (ahpCF).
Cys can react with bacillithiol (BSH) to form mixed disulfides. S-bacillithiolation protects Cys residues against overoxidation by acting as a redox switch in response to oxidative stress.
Interacts with AbrB, BdhA, Bdr, BrxB, FolD, GapA, GapB, GatA, PfkA, PyrAA, PyrAB, PyrE, PyrG, PyrH, RpsB, RpsK, RpsL, SalA, SucC, Tuf and YtsJ.
S-bacillithiolation is the formation of mixed disulfide bonds between protein thiols and the general thiol reductant bacillithiol (BSH) under oxidative stress. BSH is an equivalent of glutathione (GSH) in Firmicutes. This protein is a monothiol bacilliredoxin, which debacillithiolates (removes BSH) the S-bacillithiolated glyceraldehyde-3-phosphate dehydrogenases (GAPDHs) GapA and GapB in vivo and probably a number of other oxidized cytosolic proteins. Debacillithiolates the S-bacillithiolated Bdr (Bdr-SSB) and BrxB (BrxB-SSB) in vitro. Involved in maintaining redox homeostasis in response to disulfide stress conditions.
Normally needed for pro-sigma E processing during sporulation but can be bypassed in vegetative cells. Activates SpoIIAA by dephosphorylation.
Belongs to the glycosyltransferase 39 family.
May be involved in fatty acid metabolism.
Transcriptional repressor for the ans operon coding for L-asparaginase and L-aspartase. NH4(+) may influence this repression.
Belongs to the 'GDSL' lipolytic enzyme family.
Transcribed from stage t4 of sporulation. Expressed in the mother cell compartment at the late stage of sporulation and localizes around forespores in a CotE, SafA and SpoIVD-dependent manner.
Transcribed under the control of SigK and positively regulated by GerE.
Increases progressively during log phase, peaking at stationary phase of vegetative growth.
Involved in the polymerization of peptidoglycan. Plays a redundant role with PBP-2A (pbpA) in determining the rod shape of the cell during vegetative growth and spore outgrowth.
It is uncertain whether Met-1 or Met-20 is the initiator; if Met-20 then the protein would probably be secreted.
No visible phenotype during vegetative growth, sporulation or spore germination. No change in antibiotic resistance. Double pbpA-pbpH mutants cannot be made, suggesting the 2 proteins have redundant, essential roles in vegetative growth. Depletion of PbpH in the pbpA deletion leads to cell growth arrest after 3 generations; cells swell, round-up, many lyse and division septa are very irregular. Germinated spore are spherical and eventually lyse.
Belongs to the AP endonuclease 2 family.
Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family.
Carbamylation allows a single lysine to coordinate two nickel ions.
Carboxylation allows a single lysine to coordinate two nickel ions.
Belongs to the glycosyltransferase 26 family. TagA/TarA subfamily.
Catalyzes the conversion of GlcNAc-PP-undecaprenol into ManNAc-GlcNAc-PP-undecaprenol, the first committed lipid intermediate in the de novo synthesis of teichoic acid.
Not essential. Impaired growth. Looses rod shape of cells. No teichoic acid in cell walls.
May act at the level of sigma-G activity or its stability. SpoIID is probably required for engulfment.
Belongs to the inorganic phosphate transporter (PiT) (TC 2.A.20) family. Pit subfamily.
Low-affinity inorganic phosphate transporter.
Amino-acid racemase able to utilize a broad range of substrates. Preferentially catalyzes the epimerization of LL-diaminopimelate, as well as the racemization of D-lysine, L-arginine, L-ornithine, L-lysine and D-arginine. Has lower activity against D-ornithine, L-histidine, L-alanine, L-tyrosine, L-phenylalanine, L-serine, L-glutamine, L-methionine, L-asparagine and L-homoserine. Has weak activity against L-norleucine, L-aminobutyric acid and L-norvaline. Has no activity toward nine L-amino acids (Thr, Glu, Asp, Val, Leu, Ile, Trp, Cit and Aad) (PubMed:28894939). D-amino acids might be used as components of peptidoglycan and/or be involved in peptidoglycan metabolism and remodeling (PubMed:8491712, PubMed:28894939).
Weakly expressed during vegetative growth and significantly induced at the onset of sporulation.
Expressed only in the forespore compartment of sporulating cells.
Expressed only in the forespore compartment of sporulating cells. Expression is sigma G-dependent.
Was originally thought to be a spore coat protein.
Belongs to the Maf family. YhdE subfamily.
Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. Can also hydrolyze CTP and the modified nucleotides pseudo-UTP, 5-methyl-CTP (m(5)CTP) and 5-methyl-UTP (m(5)UTP) (PubMed:24210219). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids (PubMed:24210219).
Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Overexpression results in extensive filamentation caused by a disruption and subsequent inhibition of the septation process.
By methionine. Repressed by sulfate and cysteine.
Catalyzes the conversion of O-acetylserine and homocysteine to cystathionine.
Grows very slowly with methionine as sole sulfur source.
Expressed in cells competent for DNA transformation; that is 5-15% of the population (PubMed:11918817, PubMed:16009133, PubMed:17630974).
Expression activated by ComK (PubMed:11918817, PubMed:11948146).
Required for uptake of DNA by competent cells.
Transformation deficient (PubMed:16009133).
Forms an operon with yhdL and yhdK, maximally expressed during early to mid-exponential growth phases (PubMed:10216858). Transcription decreases during late exponential growth; positively autoregulated (PubMed:10216858). Negatively regulated by yhdL and yhdK (PubMed:10216858). Induced by 5% ethanol, 80 uM paraquat, pH 4.3, the antibiotics, inhibitors of cell wall, bacitracin, vancomycin and phosphomycin, heat shock of 10 minutes at 50 degrees Celsius (PubMed:12775685). No induction was observed with pH 9, H(2)O(2), monensin, and the detergents Triton X-100 and Tween 20 (PubMed:12775685). Induced 3-fold by the beta-lactam antibiotic cefuroxime (PubMed:22211522).
Interacts with the N-terminus of YhdL, which is probably its anti-sigma factor (PubMed:14993308). Interacts transiently with the RNAP core (Probable).
Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma factors are held in an inactive form by a cognate anti-sigma factor (YhdL) until released (PubMed:14993308). This sigma factor is involved in the maintenance of membrane and cell wall integrity in response to environmental stresses including salt, acid, ethanol and antibiotics stress (PubMed:22211522, PubMed:12775685). Partially regulates transcription from a number of genes including disA (PubMed:17434969). Associates with RNAP core under all growth phases (PubMed:21710567).
Strains insertionally inactivated in the sigM gene form aberrantly shaped cells that swell and lyse in medium containing high levels of different salts (PubMed:10216858). 70-fold increased sensitivity to the beta-lactam antibiotic cefuroxime (CEF), double sigM-sigX mutants have 130-fold increased sensitivity to CEF (PubMed:22211522). Also sensitive to other antibiotics (PubMed:22211522).
Activates the transcription of the gabTD operon. Is also a repressor of its own expression, both in the presence and absence of GABA. Binds specifically to the DNA region overlapping the -35 region of the gabT promoter and the -10 and +1 regions of the gabR promoter. Principally regulates the utilization of gamma-aminobutyrate.
In the C-terminal section; belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.
Chemotaxis is substantially impaired, with a 30-fold reduction in the efficiency of chemotaxis with aspartate and 11-fold reduction with 2-deoxyglucose. Inactivation of cheW appears to have a subtle effect on chemotactic behavior in the absence of chemoeffectors: the bacteria display a smooth swimming bias, with some tumbling. A double mutant lacking both CheV and CheW has a strong tumble bias, does not respond to addition of attractant, shows essentially no accumulation in capillary assays, and has greatly reduced methyl turnover on the methyl-accepting chemotaxis proteins (MCPs).
Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheV and CheW are involved in the coupling of the methyl-accepting chemoreceptors to the central two-component kinase CheA; they are both necessary for efficient chemotaxis.
Belongs to the class-II fumarase/aspartase family. Aspartase subfamily.
Expression is sigma D-dependent. Negatively regulated by ComK.
Stabilizes the phosphorylated form of DegU, leading to enhanced production of levansucrase, alkaline protease, and neutral protease.
Belongs to the octanoyltransferase LipM family.
Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domain of GcvH, an intermediate carrier during protein lipoylation.
Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domain of GcvH, an intermediate carrier during protein lipoylation. Is also able to catalyze the reverse reaction. Octanoyl-CoA can also act as a substrate although very poorly. Does not display lipoate protein ligase activity, despite its sequence similarity to LplA.
Cells lacking this gene are auxotrophic for lipoic acid when grown in minimal medium but grow as well as the wild-type strain in the presence of lipoic acid. The requirement for lipoic acid can be bypassed by addition of both acetate and branched-chain fatty acid (BCFA) precursors. The mutant cells are devoid of lipoylated proteins.
In the reaction, the free carboxyl group of octanoic acid is attached via an amide linkage to the epsilon-amino group of a specific lysine residue of lipoyl domains of lipoate-dependent enzymes. The reaction proceeds via an octanoyl-thioester enzyme intermediate.
Enables the recognition and targeting of unfolded and aggregated proteins to the ClpC protease or to other proteins involved in proteolysis. Acts negatively in the development of competence by binding ComK and recruiting it to the ClpCP protease. When overexpressed, inhibits sporulation. Also involved in Spx degradation by ClpC.
Expressed throughout growth. There is a slight decline of expression during exponential growth and a slight increase after T0.
The N-terminal domain has binding sites for ComK and ComS and probably for unfolded/aggregated proteins; the C-terminal domain interacts with ClpC.
The N-terminal domain has binding sites for ComK and probably for unfolded/aggregated proteins; the C-terminal domain interacts with ClpC.
Catalyzes the decarboxylation of malate to pyruvate. Is specific for NAD, cannot use NADP. Can also catalyze the decarboxylation of oxaloacetate (PubMed:16788182). Involved in keeping the ATP levels high (PubMed:23136871).
Mutant can use either a gluconeogenic carbon source or glucose as efficiently as the wild-type strain (PubMed:16788182). The ATP concentrations in the mutant grown in minimal medium with glucose are similar to the wild-type level. ATP concentrations slightly decrease in malate minimal medium. The mleA-maeA-malS triple mutant shows a decrease in ATP concentrations by about 20% and a moderate growth defect (PubMed:23136871). NADPH overproduction is roughly halved in the deletion mutant (PubMed:33824210).
Weakly expressed in glucose or malate minimal medium.
Secretion of subtilisin is associated with onset of sporulation, and many mutations which block sporulation at early stages affect expression levels of subtilisin. However, subtilisin is not necessary for normal sporulation.
Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides.
The propeptide functions as an intramolecular chaperone which is essential for the correct folding of the protease domain but is not required for enzymatic function of the folded protein. It is autoprocessed and degraded after completion of the folding process.
Belongs to the NADP-dependent oxidoreductase L4BD family.
Putative quinone oxidoreductase that may contribute to the degradation of aromatic compounds.
induced by stress due to exposure to 2-methylhydroquinone (2-MHQ).
Supplies heptaprenyl diphosphate, the precursor for the side chain of the isoprenoid quinone menaquinone-7 (MQ-7).
Deletion of the gene causes a decrease in the overall Spx levels, as well as a change in the dynamics of Spx accumulation.
Induced under cell wall stress, but not disulfide stress, and this induction requires the CssRS two-component system, which responds to both secretion stress and cell wall antibiotics. Phosphorylated CssR acts as an anti-repressor by antagonizing YuxN repression.
Inhibitor of Spx proteolytic control. Acts by interacting with SpxH/YjbH, which disrups interaction between SpxH and Spx, and inhibits SpxH-enhanced proteolysis of Spx by ClpXP (PubMed:21378193). Required for the stabilization of Spx and activation of Spx-regulated genes in response to cell wall stress (PubMed:30001325).
Belongs to the class II fructose-bisphosphate aldolase family.
Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis.
Belongs to the protein N5-glutamine methyltransferase family. PrmC subfamily.
Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Component of the Sec protein translocase complex. Heterotrimer consisting of SecY, SecE and SecG subunits. The heterotrimers can form oligomers, although 1 heterotrimer is thought to be able to translocate proteins. Interacts with the ribosome. Interacts with SecDF, and other proteins may be involved. Interacts with SecA (By similarity). Interacts with FloT (PubMed:23651456).
Component of the Sec protein translocase complex. Heterotrimer consisting of SecY, SecE and SecG subunits. The heterotrimers can form oligomers, although 1 heterotrimer is thought to be able to translocate proteins. Interacts with the ribosome. Interacts with SecDF, and other proteins may be involved. Interacts with SecA.
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Allosterically regulated; subject to end product regulation by purine nucleotides.
Binds 1 [4Fe-4S] cluster per subunit. The [4Fe-4S] cluster requires a potential lower than -600 mV for reduction.
Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine.
In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.
A possible homing endonuclease, it is entirely encoded within the YosP intron.
C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-adenylated (-COAMP) by MoeB, then thiocarboxylated (-COSH) by IscS.
Heterotetramer of 2 MoaD subunits and 2 MoaE subunits. Forms a stable heterotetrameric complex of 2 MoaD and 2 MoeB during adenylation of MoaD by MoeB. During catalysis MoaD shuttles between the two heterotetrameric complexes (By similarity).
Involved in sulfur transfer in the conversion of molybdopterin precursor Z to molybdopterin.
Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. This ferredoxin may act as a phosphodonor to cytochrome P450 BioI.
Contains a predicted signal peptide cleavage site in the N-terminal region, however the propeptide is probably subject to only one processing event, at the N-terminal end of the mature peptide.
Encoded by the mobile genetic element ICEBs1.
Expression is stimulated by conditions of low nutrient availability and high cell density.
Intercellular signaling molecule that inhibits excision of the mobile genetic element ICEBs1 when cells are crowded by cells that contain ICEBs1 and produce the PhrI peptide (PubMed:16105942). Secreted during production, but the mature peptide acts intracellularly, indicating that it needs to be imported into the cell to function (By similarity). Acts by inhibiting RapI activity (PubMed:16105942).
Belongs to the diacylglycerol/lipid kinase family.
Binds 1 Mg(2+) ion per subunit. This ion appears to have a structural role and is required for catalytic activity.
Catalyzes the phosphorylation of diacylglycerol (DAG) into phosphatidic acid. Is a key enzyme involved in the production of lipoteichoic acid by reintroducing DAG formed from the breakdown of membrane phospholipids into the phosphatidylglycerol biosynthetic pathway. Is more active toward long-chain DAG compared with short-chain DAG. Is not able to phosphorylate substrates other than DAG, such as monoacylglycerol, ceramide, undecaprenol, phosphatidylinositol, or sphingosine.
Cells lacking this gene are not viable. They exhibit accumulation of diacylglycerol, disappearance of phosphatidylglycerol, and the cessation of lipoteichoic acid formation.
Belongs to the SEDS family. MrdB/RodA subfamily.
Increased expression mediated by SigM is both necessary and sufficient to confer intrinsic resistance to moenomycin and viability to cells lacking aPBPs.
Peptidoglycan polymerase that is essential for cell wall elongation (PubMed:9622350, PubMed:27525505). Also required for the maintenance of the rod cell shape (PubMed:9622350).
Peptidoglycan polymerase that is essential for cell wall elongation.
May function as a transcriptional antiterminator.
Present in spore but not in vegetative cell.
Transcribed by SigG at time T3 of sporulation.
Constitutively and highly expressed on solid and in liquid medium, with or without biofilm formation by 12 hours of culture. Repressed by DegU.
Immunity protein component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. Neutralizes the tRNase activity of cognate toxin WapA upon expression in E.coli. Does not inhibit WapA from other strains of B.subtilis. The WapA C-terminus cannot be expressed on its own in E.coli, however it can be cloned in the presence of its cognate immunity protein gene. Cell contact is necessary for growth inhibition (PubMed:23572593). Unlike the LXG toxin-immunity modules, WapAI mediates competition under shaking culture conditions (PubMed:34280190).
Catalyzes the unwinding of duplex DNA in the 3' to 5' direction; this reaction is dependent on the hydrolysis of ATP.
Expression controlled by a sigma-Y-regulated promoter which needs the sigma-Y factor for the binding of the RNA polymerase and subsequent transcription.
Hydrogen and organic peroxide sensor. Represses the expression of a regulon of peroxide-inducible genes such as katA, ahpC, ahpF, the heme biosynthesis operon (hemAXCDBL), fur, perR, zosA and mrgA.
Possibly oxidized on a cysteine residue; the Cys-SOH formed in response to oxidative signaling may rapidly react with a Cys-SH to form a disulfide bond, leading to the loss of metal ion and inactivation of repressor function. Oxidized PerR can be further reduced by thiol reductants and repressor activity restored.
Belongs to the alanine or glycine:cation symporter (AGCS) (TC 2.A.25) family.
Cells accumulate precursors and mature forms of 23S rRNA with alternative 5' and 3' ends. Defects are more marked during exponential growth.
Involved in correct processing of both the 5' and 3' ends of 23S rRNA precursor. Processes 30S rRNA precursor transcript even in absence of ribonuclease 3 (Rnc); Rnc processes 30S rRNA into smaller rRNA precursors.
Involved in correct processing of both the 5' and 3' ends of 23S rRNA precursor. Processes 30S rRNA precursor transcript even in absence of ribonuclease 3 (Rnc); Rnc processes 30S rRNA into smaller rRNA precursors. Cleaves more efficiently on assembled 50S ribosomal subunits. Cleavage is strongly stimulated by ribosomal protein L3 (RplC); 20-30% DMSO can replace RplC, suggesting RplC may alter rRNA conformation.
No visible phenotype. Growth is not inhibited by 2-methylhydroquinone or catechol.
Activity is potassium and sulfate-independent.
Belongs to the low molecular weight phosphotyrosine protein phosphatase family. Thioredoxin-coupled ArsC subfamily.
Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)] (PubMed:16797027). In vitro, can dephosphorylate para-nitrophenyl phosphate (pNPP) (PubMed:11698660).
Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)].
Induced by arsenate, arsenite, and antimonite.
Mutant is sensitive to arsenate but is still resistant to arsenite.
Belongs to the methyltransferase superfamily. RNA methyltransferase RsmG family.
Specifically methylates the N7 position of guanine in position 535 of 16S rRNA.
Expression is sigma W-dependent. Induced by alkali stress. Strongly induced at the end of the exponential growth phase.
By heat shock, salt stress, oxidative stress and glucose limitation.
Homodimer; disulfide-linked, upon oxidation. 5 homodimers assemble to form a ring-like decamer.
The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this typical 2-Cys peroxiredoxin, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by AhpF.
Transcriptional regulator in fatty acid degradation. Represses transcription of genes required for fatty acid transport and beta-oxidation, including acdA, fadA, fadB, fadE, fadF, fadG, fadH, fadM, fadN, lcfA and lcfB. Binding of FadR to DNA is specifically inhibited by long chain fatty acyl-CoA compounds of 14-20 carbon atoms in length.
Cells fail to synthesize flagellin protein and grow as long filaments. They do not respond to attractants. CheC mutants showed overmethylation of the MCPs compared with wild-type strain.
Involved in restoring normal CheY-P levels following the addition of attractant by increasing the rate of CheY-P hydrolysis. Is only 6% as active as FliY, which indicates that CheC may function after addition of an attractant to cope with increased levels of CheY-P whereas FliY may function constitutively to remove CheY-P around the flagellar switch to maintain an optimal level of CheY-P. In addition, it was shown to prevent methylation of the methyl-accepting chemotaxis proteins (MCPs). Inhibits CheD.
Belongs to the universal ribosomal protein uS11 family.
Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome.
Part of the 30S ribosomal subunit (PubMed:30126986). Interacts with proteins S7 and S18. Binds to IF-3 (By similarity). Interacts with VmlR (PubMed:30126986). Interacts with BrxC (PubMed:33722570).
Part of the 30S ribosomal subunit. Interacts with proteins S7 and S18. Binds to IF-3.
Cells lacking this gene are constitutive in the expression of the trePA operon.
Probably induced by trehalose-6-phosphate.
Repressor for the trePA operon. It is able to bind trehalose-6-phosphate.
A double cshB-cspD mutant grows slowly at 15 degrees Celsius.
Belongs to the CPA3 antiporters (TC 2.A.63) subunit C family.
Expressed shortly after the beginning of sporulation.
Unknown. Affects both sporulation and germination.
Interacts with both DnaA and DnaN, acting as a bridge between these two proteins.
Involved in initiation control of chromosome replication.
Belongs to the bacterial flagellin family.
Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.
Flagellin is the subunit which polymerizes to form the filaments of bacterial flagella. Assembly into flagella requires FliW (PubMed:16936039). Acts as a homeostatic autoinhibitory regulator to control its own cytoplasmic levels. Partner switching by flagellin between FliW and CsrA provides a flagellar assembly checkpoint to tightly control the timing of flagellin synthesis. Flagellin binds to assembly factor FliW, freeing translation regulator CsrA to repress translation of the flagellin mRNA. When the flagellar hook is assembled flagellin is secreted, depleting intracellular flagellin, which frees FliW to interact with CsrA. This derepresses flagellin translation and provides protein for flagellar assembly. Once the flagellar filament is completed cytoplasmic flagellin levels rise and CsrA translation repression of flagellin reinitiates (PubMed:21895793).
Interacts with FliW in a 1:1 complex (PubMed:16936039, PubMed:21895793). Forms a 3-way complex of Hag, FliS and FliW, in which Flis and FliW do not directly interact (PubMed:23144244).
Under positive control of SigD (PubMed:11987133). Repressed by CsrA; repression is greater in the 1A96 than 168 genetic background and higher in minimal than rich medium (PubMed:17555441).
Belongs to the universal ribosomal protein uL1 family.
Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release.
Part of the 50S ribosomal subunit (PubMed:30126986). Interacts with RNA helicase CshA (PubMed:23175651). Interacts with VmlR (PubMed:30126986).
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.
Heterodimer of an alpha and a beta chain.
The B.subtilis PDH complex possesses also branched-chain 2-oxoacid dehydrogenase (BCDH) activity.
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
Belongs to the myoviridae tail sheath protein family.
Involved in the polymerization and cross-linking of spore peptidoglycan. May be required for synthesis of the spore germ cell wall, the first layer of peptidoglycan synthesized on the surface of the inner forespore membrane.
No visible phenotype; due to the redundancy with PbpF. Spores have normal heat-resistance, cortex structure, and germination and outgrowth properties.
Sporulation specific. Expressed predominantly, if not exclusively, in the forespore.
Belongs to the tRNA(Ile)-lysidine synthase family.
Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Belongs to the glycosyl hydrolase 42 family.
Inhibited by zinc, cobalt and copper ions.
Involved in galactan degradation (PubMed:27501980). Hydrolyzes galactooligosaccharides released by the endo-beta-1,4-galactanase GanB from galactan (PubMed:17056685, PubMed:27501980). Degrades galactotetraose, galactotriose and galactobiose, generating galactose as the end product (PubMed:27501980). It is unable to use lactose (PubMed:17056685). In vitro, shows maximal activity with o-nitrophenyl-beta-D-galactopyranoside (ONPG) and p-nitrophenyl-beta-D-galactopyranoside (PNPG) as substrates, trace activity with p-nitrophenyl-alpha-L-arabinopyranoside and o-nitrophenyl-beta-D-fucopyranoside as substrates, but no activity with p-nitrophenyl-alpha-D-galactopyranoside, p-nitrophenyl-beta-D-glucopyranoside, o-nitrophenyl-beta-D-xylopyranoside, p-nitrophenyl-beta-D-mannopyranoside or p-nitrophenyl-alpha-L-arabinofuranoside as substrates (PubMed:17056685).
No chromogen 5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside (X-Gal) hydrolyzation. Reduces beta-galactosidase activity observed with polygalacturonic acid, citrus and apple pectins, galactan and soy flour.
According to PubMed:14761999, can complement an E.coli mutT mutant. According to PubMed:15576788, cannot complement an E.coli mutT mutant.
Expressed during both vegetative growth and early stage of sporulation.
Growing cells lacking this gene have a 4-fold increased spontaneous mutation frequency (a mild mutator phenotype), as well as an increased sensitivity to DNA-damaging agents such as H(2)O(2) or t-BHP. These phenotypes are increased in a double ytkD/mutT disruption (PubMed:16513759). They are also seen in stationary phase cells. Triple ytkD/mutM/mutY disrupted strains show increased mutation rates during exponential and stationary phase (PubMed:19011023).
Involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine, 8-oxo-dGTP) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions (By similarity). Functions, in conjunction with MutT, to protect vegetatively growing cells from DNA-damaging agents such as H(2)O(2) or t-BHP (t-butylhydroperoxide). The 2 proteins do not however protect spores. According to PubMed:15576788, phosphohydrolase that catalyzes the hydrolysis of all common nucleoside triphosphates as well as of the mutagenic analog 8-oxo-dGTP. The high catalytic efficiency on dGTP is in contrast to results from PubMed:14761999. According to PubMed:14761999, catalyzes the hydrolysis of 8-oxo-dGTP with a specific activity 413 times higher than that exhibited against dGTP. Preferentially catalyzes the hydrolysis of 8-oxo-dGTP and 8-oxo-GTP. According to PubMed:15576788, hydrolyzes nucleoside triphosphates in a stepwise fashion through the diphosphate to the monophosphate, releasing two molecules of inorganic orthophosphate.
Not induced by oxidative damage (following treatment with paraquat or hydrogen peroxide). Not induced by mitomycin C. Not induced by sigma-B general stress inducers such as sodium chloride, ethanol or heat.
Important for the use of proline as a sole carbon and energy source or a sole nitrogen source.
Deletion mutant shows no detectable conjugative transfer of ICEBs1.
Exhibits both muramidase and DL-endopeptidase activities (PubMed:18305117, PubMed:24532767). The N-terminal region acts as a N-acetylmuramidase, which cleaves the bond between N-acetylmuramic acid and N-acetyl-D-glucosamine (MurNAc-GlcNAc) in peptidoglycan (PubMed:18305117). The C-terminal region acts as a DL-endopeptidase that cleaves the bond between D-gamma-glutamate and meso-diaminopimelic acid (PubMed:18305117). Cannot degrade purified B.anthracis peptidoglycan, which differ from those of B.subtilis (PubMed:24532767). CwlT is required for ICEBs1 conjugation: the muramidase activity is essential, whereas the peptidase activity is partially dispensable for transfer of ICEBs1 (PubMed:24532767).
Exogenous CwlT causes lysis of B.subtilis and B.anthracis, most likely by causing at least minimal degradation of the cell wall.
The cwlT gene is located in the region of the mobile genetic element ICEBs1, an integrative and conjugative element (ICE) found in B.subtilis.
Belongs to the helicase family. DinG subfamily.
Belongs to the amino acid-polyamine-organocation (APC) superfamily. Spore germination protein (SGP) (TC 2.A.3.9) family.
Involved in the germinative response to L-alanine. Could be an amino acid transporter (By similarity).
Alters assembly of FloT membrane rafts; more diffuse rafts are seen. Double floA-nfeD2 deletion mutants are wild-type (PubMed:22753055). No visible effect on FloT membrane assemblies (PubMed:27362352).
Expression is sigma W-dependent. Up-regulated by alkali shock and by infection with phage SPP1.
Plays a role in assembly of FloT membrane rafts, probably recruited to rafts by FloT.
Member of the two-component regulatory system NatK/NatR that positively regulates the expression of the natAB operon. Acts by binding directly to the promoter of natAB.
Expressed during growth and early stationary phase.
Phosphorylates the sporulation-regulatory protein spo0A under biofilm growth conditions. Also able to weakly phosphorylate spo0F.
Homodimer (PubMed:10864496, PubMed:25691471). Under conditions of nitrogen excess, TnrA forms a stable complex with feedback-inhibited GlnA. Interacts with GlnK-AmtB complex.
The amino acid sequences of the N-terminal DNA binding domains of TnrA and GlnR are highly similar, and both proteins bind to DNA sequences with a common consensus sequence. In contrast, the C-terminal signal transduction domains of TnrA and GlnR have no homology.
TnrA mutant is impaired in its ability to utilize allantoin, gamma-aminobutyrate, isoleucine, nitrate, urea and valine as nitrogen sources. During nitrogen-limited growth, transcription of the nrgAB, nasB, gabP, and ure genes is significantly reduced in the tnrA mutant. In contrast, the level of glnRA expression is 4-fold higher in the tnrA mutant than in wild-type cells during nitrogen restriction.
Transcription regulator that actives the transcription of genes required for nitrogen assimilation such as nrgAB (ammonium transport), nasABCDEF (nitrate/nitrite assimilation), ureABC (urea degradation) and gabP (GABA transport), during nitrogen limitation (PubMed:8799114, PubMed:9603886, PubMed:10231480, PubMed:10864496, PubMed:11719184, PubMed:12823818). Also represses glnRA and gltAB in the absence of ammonium (PubMed:8799114, PubMed:9603886, PubMed:10231480, PubMed:10864496, PubMed:11719184, PubMed:12823818). On the contrary of the MerR members, which require longer DNA sites for high-affinity binding, TnrA requires a DNA sequence of 17 nucleotides as minimal binding site (PubMed:10231480, PubMed:25691471).
Under conditions of nitrogen excess, repressed by GlnR. Under conditions of nitrogen-limited growth, it positively regulates its own expression.
Under conditions of nitrogen excess, the DNA-binding activity is inhibited by the formation of a stable complex with feedback-inhibited GlnA (PubMed:11719184, PubMed:25691471). The presence of glutamine and AMP increases the inhibitory activity of glutamine synthetase by more than 1000-fold (PubMed:11719184).
Low-potential electron donor to a number of redox enzymes.
Binding to DNA is allosterically inhibited by an effector molecule (PubMed:20047956, PubMed:21602348, PubMed:24673833, PubMed:25564531). Binding of the effector to the C-terminal domain leads to a conformational change that modulates binding to DNA and thereby regulates transcription of the target genes (PubMed:20047956, PubMed:25564531). Glucosamine-6-phosphate (GlcN6P) and/or N-acetylglucosamine-6-phosphate (GlcNAc6P) are putative effectors of NagR (PubMed:20047956, PubMed:21602348, PubMed:24673833, PubMed:25564531). Binding of GlcNAc6P may prevent the protein-protein interactions responsible for polymerization along the DNA, but not the specific DNA binding (PubMed:24673833).
Deletion of the gene results in the modulation of the expression of many important genes, probably indirectly due to an excess of the crucial molecules acetate, ammonia, and fructose-6-phosphate, resulting from complete hydrolysis of GlcNAc (PubMed:21602348). Disruption of the gene induces a slight but consistent increase in MapB activity (PubMed:16207374).
Homodimer (PubMed:19342794, PubMed:20047956, PubMed:25564531). Forms dimers via the C-terminal effector-binding domain (PubMed:20047956). At high concentrations, probably forms polymers along the DNA (PubMed:24673833).
Main transcriptional repressor of genes involved in N-acetylglucosamine (GlcNAc) transport and utilization (PubMed:21602348, PubMed:20047956, PubMed:24673833). Represses the expression of the nagAB and nagP operons by binding directly within their upstream regions (PubMed:21602348, PubMed:24673833). Binds to the DNA consensus sequence 5'-ATTGGTATAGACAACT-3' (PubMed:21602348). Also acts as a weak repressor of mapB expression (PubMed:16207374).
The N-terminal region contains a canonical wHTH DNA-binding domain. It is linked via a 21 residue-long linker to the C-terminal domain, which binds the effector molecule.
In the C-terminal section; belongs to the PRA-PH family.
In the N-terminal section; belongs to the PRA-CH family.
Member of the two-component regulatory system CitT/CitS. Regulates the expression of the citM-yflN operon. Phosphorylated CitT binds to the citM promoter to activate the transcription of the citM-yflN operon.
Cells lacking this gene show reduced bacilysin biosynthetic activity.
Belongs to the CbiX family. SirB subfamily.
Chelates iron to the siroheme precursor.
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit (By similarity).
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.
Probably part of the binding-protein-dependent transport system YurMNO.
Allosterically activated by GTP, when glutamine is the substrate; GTP has no effect on the reaction when ammonia is the substrate. The allosteric effector GTP functions by stabilizing the protein conformation that binds the tetrahedral intermediate(s) formed during glutamine hydrolysis. Inhibited by the product CTP, via allosteric rather than competitive inhibition.
CTPSs have evolved a hybrid strategy for distinguishing between UTP and CTP. The overlapping regions of the product feedback inhibitory and substrate sites recognize a common feature in both compounds, the triphosphate moiety. To differentiate isosteric substrate and product pyrimidine rings, an additional pocket far from the expected kinase/ligase catalytic site, specifically recognizes the cytosine and ribose portions of the product inhibitor.
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
Homotetramer (By similarity). Interacts with BrxC (PubMed:33722570).
Catalyzes the release of inorganic phosphate from 2',3'-cyclic nucleotides through consecutive 2',3'-phosphodiesterase and 3'- (or 2') nucleotidase activities. Also possesses a 5'-nucleotidase activity. Does not catalyze the release of inorganic phosphate from 3',5'-cyclic nucleotides. Probably plays a role in the cellular reprocessing of nucleotides present in the medium, under conditions of phosphate shortage.
The N-terminal region (amino acids 35-623) is able to catalyze the release of phosphate from 2',3'-cyclic nucleotides, but not from 5'-nucleotides.
Belongs to the HAD-like hydrolase superfamily.
Catalyzes the dephosphorylation of C5 and C6 carbon sugars in vitro (PubMed:21575135, PubMed:25848029). Catalyzes the dephosphorylation of 3'-AMP and phosphoserine in vitro (PubMed:25848029).
Belongs to the gamma-glutamyltransferase family.
Cleaved by autocatalysis into a large and a small subunit.
Grows normally with glutathione as a sulfur source.
Is not involved in the utilization of extracellular glutathione as a sulfur source.
Overexpressed protein with an N-terminal His tag has been reported not to hydrolyze glutathione; it is not clear if the construct is processed to 2 subunits (PubMed:14762019).
This enzyme consists of two polypeptide chains, which are synthesized from a single polypeptide.
This enzyme consists of two polypeptide chains, which are synthesized in precursor form from a single polypeptide.
Hydrolyzes various disaccharides such as sucrose, maltose, and isomaltose with different efficiencies. Also hydrolyzes longer maltodextrins from maltotriose up to maltohexaose, but not maltoheptaose, palatinose, isomaltotriose, or isomaltotetraose.
Belongs to the MurCDEF family. MurE subfamily.
Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP.
Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
Belongs to the mannose-6-phosphate isomerase type 1 family.
Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella - in particular of its basal body - and sporulation. CwlC is able to hydrolyze type A cell walls such as B.subtilis. Its main function is to lyze the mother cell wall peptidoglycan, playing a role during sporulation.
Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
Contains an N-terminal catalytic domain and two C-terminal tandem repeat sequences that play an important role in peptidoglycan binding.
Induced at 6 to 7 hours after sporulation.
Expressed under control of sigma-A RNA polymerase.
Is the major glucosaminidase responsible for peptidoglycan structural determination during vegetative growth. Catalyzes the hydrolysis of 1,4-beta-linkages between N-acetyl-D-glucosamine and N-acetylmuramic acid residues in peptidoglycan. Acts processively from the ends of the glycan strands. Also plays a role in motility, chemotaxis and cell division.
Belongs to the bacterial diacylglycerol kinase family.
Catalyzes the phosphorylation of undecaprenol in vitro, which is probably the physiological substrate. Exhibits no detectable activity against other substrates such as monoacylglycerol, ceramide, or diacylglycerol (DAG). Appears indispensable for the maintenance of spore stability and viability in B.subtilis.
Cells lacking this gene exhibit an abnormal cortex structure in mutant endospores 6 hours after the onset of sporulation, an indication of cortex degeneration. In addition, they display a significant decrease in the dipicolinic acid content of mutant spores.
Mainly expressed during the vegetative phase of growth.
Mn(2+), Zn(2+), Cd(2+) and Co(2+) support activity to lesser extents.
Was originally thought to be a diacylglycerol kinase.
Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Transcriptional repressor for the ribose rbsDACBK operon.
Essential, it cannot be deleted. Upon depletion cells grow very slowly while aconitase and succinate dehydrogenase, both of which contain Fe-S clusters, have decreased activity. Upon depletion no change in reactive oxygen species is observed, while a modified bacillibactin (BB), an endogenous siderophore, is produced.
Interacts with SufS; this interaction enhances SufS cysteine desulfurase activity. Interacts with frataxin/Fra (PubMed:27382962).
Part of the SUF-like system that mediates the biosynthesis of iron-sulfur (Fe-S) clusters. Acts as a sulfurtransferase and thus transfers sulfur from SufS to SufB (PubMed:29292548). Mechanistically, the transfer from SufS to SufU is triggered by zinc-ligand swapping that provides a free thiol from SufU to accept sulfur from SufS (PubMed:29235855).
The inhibition of SufS activity by the Cys-41 mutation in this protein has been described as competitive and non-competitive inhibition (PubMed:21236255, PubMed:24321018).
Was originally thought to be an iron-sulfur cluster assembly scaffold protein (PubMed:20097860, PubMed:21236255). It is now thought to be a zinc-dependent sulfur transfer protein (PubMed:24321018).
Induced during development under sigma-K control and negatively regulated by GerE.
Involved in spore outer coat assembly. May be part of a cross-linked insoluble skeleton that surrounds the spore, serves as a matrix for the assembly of additional outer coat material, and confers structural stability to the final structure.
Activated by alpha-ketoglutarate and inhibited by glutamate and by RocG.
Induced by glucose, repressed by arginine, less protein accumulates when grown in the presence of glucose and arginine (at protein level).
Interacts with gutamate dehydrogenase RocG.
Positive regulator of glutamate biosynthesis (gltAB genes). Negatively regulates its own expression.
Member of the two-component regulatory system YvrG/YvrH that positively regulates 7 transcriptional units (wprA, wapA-yxxG, dltABCDE, sunA, sunT-bdbA-yolJ-bdbB, sigO-rsoA, and sigX-rsiX), and negatively regulates the lytABC operon. Probably activates YvrH by phosphorylation.
ATPase that binds to both the 70S ribosome and the 50S ribosomal subunit in a nucleotide-independent manner.
Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. YchF/OLA1 subfamily.
Weakly expressed during exponential growth in rich medium, stops at onset of stationary phase. In minimal medium is more strongly expressed and continues into stationary phase, part of the ychF-rpsF-ssbA-rpsR operon (PubMed:14762004).
Autoregulated. Transcriptionally regulated by sigma-K. Expressed during exponential growth.
Cells lacking this gene display increased rates of transcription of mutY, fabL, sspE and yfhP.
May act as a negative regulator for the transcription of mutY, fabL, sspE and yfhP.
Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. MalY/PatB cystathionine beta-lyase subfamily.
Catalyzes the transformation of cystathionine to homocysteine. Also exhibits cysteine desulfhydrase activity in vitro, producing sulfide from cysteine.
Constitutively expressed at a low level.
Involved in the D-alanylation of lipoteichoic acid (LTA). Could be responsible for the transfer of DltC-carried D-alanyl groups to cell membrane phosphatidylglycerol (PG), or alternatively of D-alanine residues from D-Ala-undecaprenol phosphate to the poly(glycerophosphate) chains of LTA. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall.
Activated by divalent metal cations; Mn(2+) is the most efficient, followed by Ca(2+) and Mg(2+). In contrast to PgdA from S.pneumoniae, these ions are not absolutely required for deacetylase activity.
Catalyzes the deacetylation of N-acetylmuramic acid (MurNAc) residues in peptidoglycan, a modification that confers resistance to lysosyme. Is not able to deacetylate N-acetylglucosamine (GlcNAc) residues in peptidoglycan, but can deacylate chitin oligomers such as GlcNAc4 and GlcNAc5. Is essentially not active toward chitosan (partially deacetylated GlcNAc polymer) and has very low activity toward chitin (GlcNAc polymer). Does not deacetylate GlcNAc.
Cells lacking this gene show sensitivity to lysosyme, in contrast to wild-type.
Derepression of pdaC in cells depleted for yycFG leads to increased resistance of the cell walls to lysozyme digestion.
In the C-terminal section; belongs to the polysaccharide deacetylase family.
In the N-terminal section; belongs to the RsiV family.
The product of deacetylated GlcNAc4 by PdaC is GlcNAc-GlcNAc-GlcN-GlcNAc.
Was originally described as a deoxyribonuclease (PubMed:17878218), but it was later shown that PdaC has no DNase activity at all (PubMed:22277649).
Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family.
Requires glycerol 3-phosphate and the GlpP product; repressed by glucose.
Belongs to the dienelactone hydrolase family.
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family.
Catalyzes the transamination between an unstable intermediate ((S)-ureidoglycine) and the end product of purine catabolism (glyoxylate) to yield oxalurate and glycine. Glyoxylate is the preferred substrate, but other amino-group acceptors can be used.
Expression is very low in excess nitrogen (glutamate plus ammonia) and is induced during limiting-nitrogen conditions (glutamate). Expression is further induced when allantoin is added during limiting-nitrogen conditions.
By mitomycin C and UV irradiation which requires RecA.
Cells lacking this gene display a derepression of rapG and rapH expression, which leads to a down-regulation of sfrA that in turn leads to the expression abolition of both comK and the late com operon comG.
Represses the expression of yvaM and both rapG and rapH. Binds directly to the promoter regions of yvaM, rapG and rapH.
Binds 2 manganese ions per subunit. Can also use other divalent cation, with lower efficiency (PubMed:4990470).
Catalyzes the conversion of N-formimidoyl-L-glutamate to L-glutamate and formamide.
Has a minor role in biofilm architecture. May contribute to the surface hydrophobicity.
Involved in forespore engulfment. Forms a channel with SpoIIIAH that is open on the forespore end and closed (or gated) on the mother cell end. This allows sigma-E-directed gene expression in the mother-cell compartment of the sporangium to trigger the activation of sigma-G forespore-specific gene expression by a pathway of intercellular signaling.
Specifically expressed in the mother cell during sporulation under the control of the sigma-E factor.
Induced by sulfate, part of the yoaDCB operon.
Induced in the presence of D-glucarate or D-galactarate.
Probably involved in the uptake of galactarate and/or D-glucarate.
A benzaldehyde dehydrogenase able to act on substrates with 3- and 4-hydroxy and methoxy substitutions; converts vanillin (4-hydroxy-3-methoxybenzaldehyde) to vanillic acid in vitro (PubMed:26658822). The physiological substrate is unknown (PubMed:26658822).
Loss of conversion of vanillin to vanillic acid (PubMed:26658822).
Transcriptionally regulated by SigD; part of the yfmT/yfmS operon.
Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids threonine, isoleucine and methionine.
Lysine-sensitive. Regulated by degradation in response to starvation of cells for various nutrients. Ammonium starvation induced the fastest aspartokinase II decline, followed by amino acid starvation and glucose limitation.
Tetramer consisting of 2 isoforms Alpha (catalytic and regulation) and of a homodimer of 2 isoforms Beta (regulation).
Morphogenic protein required for the assembly of the outer coat of the endospore. Is also a regulatory protein for the expression of cotA, cotB, cotC, cotH and other genes encoding spore outer coat proteins.
Negatively regulates the expression of the ganSPQAB operon (PubMed:2104611, PubMed:9287030, PubMed:27501980). Inhibits transcription of the operon by binding to an operator in the promoter region (PubMed:27501980). In the presence of galactobiose, GanR dissociates from the promoter, resulting in the expression of the gan operon (PubMed:27501980).
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Belongs to the GatB/GatE family. GatB subfamily.
The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. This system is involved in fructose transport.
Belongs to the CMP-NeuNAc synthase family.
Belongs to the ABC-3 integral membrane protein family.
Probably part of the ABC transporter complex MntABCD involved in manganese import. Probably responsible for the translocation of the substrate across the membrane.
Belongs to the glycosyltransferase 28 family.
Cells lacking this gene express the exu locus genes (required for hexuronate utilization) constitutively. Its absence additionally confers the ability to grow on minimal medium plus glucuronate, which cells cannot do in the presence of ExuR.
Transcriptional repressor for the exu locus which is required for galacturonate utilization.
F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains (Probable). The F(1)F(0) complex interacts with SpoIIIJ and YqjG; YqgA is found in the same complex.
F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains.
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
Deletion mutant grows less well than wild type on minimal medium with ammonium as nitrogen source and cannot grow on 5-oxoproline. Mutant lacks 5-oxoprolinase activity and accumulates 5-oxo-L-proline.
Forms a complex composed of PxpA, PxpB and PxpC.
Expression is sigma Y-dependent. Induced upon nitrogen starvation.
Cells lacking this gene show no maltose uptake.
Maltose uptake in B.subtilis occurs only via the malP-encoded specific PTS-dependent EIICB(Mal) and not via another transport mechanism.
The EIIC domain type-1 forms the PTS system translocation channel and contains the specific substrate-binding site.
The PTS EIIB type-1 domain is phosphorylated by phospho-EIIA on a cysteinyl residue. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the PTS EIIC type-1 domain.
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in maltose transport.
Belongs to the KtrA potassium transport family.
Catalytic subunit of the KtrCD potassium uptake transporter. The 2 major potassium transporter complexes KtrAB and KtrCD confer resistance to both suddenly imposed and prolonged osmotic stress.
Homodimer, tetramer (dimer of homodimer) and octamer (tetramer of homodimer). Part of the KtrCD complex formed by an octameric catalytic ring of KtrC and a membrane associated dimer of KtrD forming a potassium channel (By similarity).
Belongs to the FKBP-type PPIase family. Tig subfamily.
Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity).
Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Expressed at very low levels throughout growth.
To B.subtilis XtmB and phage SPP1 terminase large subunit.
Required for vegetative and sporulation septum formation. Required for the activation of genes expressed under the control of the sporulation transcription factors sigma F and sigma E.
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Expressed during both vegetative growth phase and sporulation.
Mutants show poor germination in the presence of L-alanine and reduced biofilm formation.
Stimulates biofilm formation via transcriptional activation of extracellular matrix genes. Acts by repressing SinR activity, independently of the SinI, SlrA and SlrR pathways. Could also be involved in the regulation of other genes during biofilm and spore formation.
Belongs to the SorC transcriptional regulatory family.
Deoxyribose-5-phosphate is most likely the effector that modulates binding of DeoR to DNA.
Negative regulator of the dra-nupC-pdp operon. DeoR binds cooperatively to the operator DNA, which consists of a palindrome and a direct repeat sequence located 3' to the palindrome.
Forms a 24-polypeptide structural core with octahedral symmetry.
Belongs to the glycosyl hydrolase 65 family.
Catalyzes the phosphorolysis of maltose, leading to the formation of glucose and glucose 1-P.
Belongs to the glycosyl hydrolase 1 family.
Expressed at a low and constant level during growth, sporulation, and spore germination.
Is able to catalyze the hydrolysis of aryl-phospho-beta-D-glucosides such as 4-methylumbelliferyl-phospho-beta-D-glucopyranoside (MUG-P), phosphoarbutin and phosphosalicin. Is not essential for growth on arbutin and salicin as the sole carbon source.
Is not induced by aryl-beta-D-glucosides such as arbutin, salicin or 4-methylumbelliferyl-beta-D-glucopyranoside (MUG). Is not repressed by glucose.
Belongs to the CPA3 antiporters (TC 2.A.63) subunit A family.
Belongs to the inorganic carbon transporter (TC 9.A.2) DabB family.
Homodimer (PubMed:14517982, PubMed:24120662). Forms a complex with antitoxin EndoAI in which the toxin activity is inhibited (PubMed:15882409). One dimer binds a ssRNA substrate, forms a heterohexamer composed of alternating toxin and antitoxin homodimers which inhibits the endoribonuclease activity. Antitoxin prevents RNA binding to the endoribonuclease (PubMed:24120662).
Replacing all Arg residues by canavanine yields an enzyme that recognizes a longer consensus sequence UACAUA, thus altering its substrate specificity. Still cleaves between the first and second nucleotides.
Toxic component of a type II toxin-antitoxin (TA) system.
Toxic component of a type II toxin-antitoxin (TA) system. Specific for 5'-UACAU-3' sequences, cleaving after the first U (PubMed:21763692). Yields cleavage products with 3' phosphate and 5' hydroxyl groups (PubMed:15882409). Cannot digest substrate with a UUdUACAUAA cleavage site (PubMed:24120662). Overexpression is toxic for cell growth (shown in E.coli), probably by inhibiting protein synthesis through the cleavage of single-stranded RNA. The toxicity is reversed by the antitoxin EndoAI. Toxin activity cannot be inhibited by MazE from E.coli. The EndoA-EndoAI complex does not seem to bind its own promoter (PubMed:24120662).
Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
Cell wall hydrolase that cleaves gamma-D-glutamate-meso-diaminopimelate bonds in peptidoglycan (By similarity). Seems to play a role in cell separation during vegetative growth.
Cells lacking this gene are about twice as long as those of the wild-type strain.
Expressed during the exponential growth phase, under the control of SigA (major) and SigH (minor). Is also positively regulated by the two-component system YycFG.
Belongs to the glycosyl hydrolase 26 family.
Involved in the degradation of glucomannan. Catalyzes the endo hydrolysis of beta-1,4-linked mannan, galactomannan and glucomannan.
Member of the two-component regulatory system YvrG/YvrH that positively regulates 7 transcriptional units (wprA, wapA-yxxG, dltABCDE, sunA, sunT-bdbA-yolJ-bdbB, sigO-rsoA, and sigX-rsiX), and negatively regulates the lytABC operon.
Belongs to the alpha-acetolactate decarboxylase family.
Converts acetolactate into acetoin, which can be excreted by the cells. This may be a mechanism for controlling the internal pH of cells in the stationary stage.
Strongly induced under anaerobic conditions. Activated by ResDE, Fnr and ArfM.
Catalyzes quinol oxidation with the concomitant reduction of oxygen to water.
Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Major component for energy conversion during vegetative growth (By similarity).
Catalyzes the reduction of 2,5-diketo-3-deoxygluconate (DKII or 4,6-dihydroxy-2,5-dioxohexanoate) into 2-keto-3-deoxygluconate (KDG or 2-dehydro-3-deoxygluconate) with a concomitant oxidation of NADH.
May play a role in the degradation of type I rhamnogalacturonan derived from plant cell walls.
Involved in the catabolism of L-rhamnose (6-deoxy-L-mannose). Catalyzes the transfer of the gamma-phosphate group from ATP to the 1-hydroxyl group of L-rhamnulose to yield L-rhamnulose 1-phosphate.
Belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.
Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Homodimer (By similarity). Interacts with BrxC(PubMed:33722570).
Belongs to the vitamin uptake transporter (VUT/ECF) (TC 2.A.88) family. TrpP subfamily.
Cells lacking this gene grow on 40-fold higher concentrations of the tryptophan analog 5-fluorotryptophan than the level that inhibits the wild-type strain.
Its translation is regulated by tryptophan-activated RNA-binding regulatory protein (TRAP).
Expressed at only a very low level in exponential-phase cells and germinating spores, but is expressed at a higher levels upon entry into the stationary phase of growth.
Phospho-beta-D-glucosidase that seems to be involved in the degradation of glucomannan. Is also capable of hydrolyzing aryl-phospho-beta-D-glucosides, although very weakly, and plays only a minor role, if any, in the degradation of these substrates in vivo.
Up-regulated by konjac glucomannan and by cellobiose and mannobiose, the possible degradation products of glucomannan. Repressed by glucose via the carbon catabolite repression system. Also repressed by GmuR. Is not induced by aryl-beta-D-glucosides such as arbutin or salicin.
Belongs to the thiolase-like superfamily. HMG-CoA synthase family.
Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. It catalyzes the aldol condensation between the acetyl group attached to the acyl-carrier-protein AcpK (Ac-AcpK) and a beta-ketothioester polyketide intermediate linked to one of the consecutive thiolation domains of PksL.
Part of a binding-protein-dependent transport system for aliphatic sulfonates. Putative binding protein.
Belongs to the radical SAM superfamily. 7-carboxy-7-deazaguanine synthase family.
Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7-deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds.
By mitomycin C and UV irradiation which requires RecA; probably a member of the yhaONM operon.
Member of the two-component regulatory system YbdK/YbdJ.
Belongs to the 4-oxalocrotonate tautomerase family.
Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
Under oxidizing conditions two disulfide bonds are formed involving the reactive cysteines. Under reducing conditions zinc is bound to the reactive cysteines and the protein is inactive.
Belongs to the thioester dehydratase family. FabZ subfamily.
Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH.
Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH. Is the predominant 6-P-gluconate dehydrogenase isoenzyme in B.subtilis during growth on glucose and gluconate.
Cells lacking this gene exhibit a reduced growth on glucose as the sole carbon source, and they do not use the pentose phosphate (PP) pathway at all.
Uptake of L-lactate across the membrane. Can also transport D-lactate and glycolate.
Catalyzes the transformation of cystathionine into homocysteine. Also exhibits cysteine desulfhydrase activity in vitro, producing sulfide from cysteine.
Cells lacking this gene grow as well as the wild-type in the presence of sulfate, cysteine, homocysteine or methionine as sole sulfur source, but do not grow in the presence of cystathionine.
Belongs to the adenylate cyclase family. DacA/CdaA subfamily.
Catalyzes the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP), a second messenger used to regulate differing processes in different bacteria.
DAC activity is stimulated about 20-fold in E.coli by coexpression with CdaR (PubMed:23192352).
Increased sensitivity to the beta-lactam antibiotic cefuroxime (CEF), upon overexpression of the c-di-AMP phosphodiesterase GdpP greatly increased sensitivity to CEF (PubMed:22211522). Double disA-cdaA mutants cannot be made, suggesting they are lethal, while double disA-cdaS and cdaA-cdaS mutants are viable (PubMed:22211522, PubMed:23192352). Depletion of cdaA in double disA-cdaA deletion cells leads to cell lysis (PubMed:22211522). Exponentially growing cells are extremely sensitive to H(2)O(2), no change in response to methyl methanesulfonate (PubMed:25616256).
One of 3 paralogous diadenylate cyclases (DAC) in this bacteria, catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP) (Probable). Upon expression in E.coli leads to c-di-AMP synthesis (PubMed:23192352). Probably the main producer of c-di-AMP for the cell; is probably implicated in control of peptidogylcan synthesis (PubMed:22211522, PubMed:23192352, PubMed:26240071). In B.subtilis c-di-AMP is a second messenger that mediates growth, DNA repair and cell wall homeostasis; it is toxic when present in excess (PubMed:26240071).
Probably a homodimer (By similarity). Interacts with CdaR (PubMed:23192352, PubMed:26240071). May interact with GlmM (PubMed:26240071).
Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Belongs to the amidase family. GatA subfamily.
Heterotrimer of A, B and C subunits (PubMed:9342321). Interacts with BrxC (PubMed:33722570).
Could be the product of a pseudogene. The N-terminus is about 750 residues shorter than orthologs, and it contains a truncated response regulatory domain.
The phosphoserine observed at Ser-1006 in PubMed:17218307 undoubtedly results from the secondary neutral loss of pantetheine from the phosphodiester linked cofactor.
This protein is a multifunctional enzyme able to activate and polymerize the amino acids Leu, Glu, Asp and Val. Activation sites for these AA consist of individual domains.
Belongs to the transthyretin family. 5-hydroxyisourate hydrolase subfamily.
Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
Expression is very low in excess nitrogen (glutamate plus ammonia) and is induced by TnrA during limiting-nitrogen conditions (glutamate). Expression is further induced when allantoin or uric acid are added during limiting-nitrogen conditions.
HIU hydrolysis also occurs spontaneously, but more slowly.
Belongs to the binding-protein-dependent transport system permease family. FecCD subfamily.
Part of the ABC transporter complex YfmCDEF involved in citrate-dependent Fe(3+) import. Involved in the translocation of the substrate across the membrane (Probable).
The complex is composed of one ATP-binding protein (YfmF), two transmembrane proteins (YfmD and YfmE) and a solute-binding protein (YfmC).
Processing of ComGD in competent cells requires ComC.
Belongs to the bacteriophage holin family. Cp-1 holin subfamily.
By aldehyde stress, positively regulates its own expression.
Loss of expression of the adhA-yraA operon in response to formaldehyde and methylgloxal.
Transcriptional regulator involved in the response to aldehyde stress. Binds to the promoter region of the adhA-yraA operon, the yraC and its own promoter region; binding is unchanged in the presence of aldehydes.
Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Could be an interacting mediator in the complex formation among RNA sulfuration components, RNA processing components, and aminoacyl-tRNA synthetases.
Belongs to the UDP-glycosyltransferase family.
Belongs to the methyltransferase superfamily. RsmI family.
Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA.
By heat shock, salt stress, ethanol stress, oxidative stress, glucose limitation and oxygen limitation.
Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX (PubMed:20305655). Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcriptional activation of genes under the control of the sigma-W factor (PubMed:16899079). Probably the major protease that degrades proteins tagged by trans-translation (PubMed:11395451, PubMed:31155236).
Fourteen ClpP subunits assemble into 2 heptameric rings which stack back to back to give a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes (PubMed:20305655, PubMed:22080375). Forms large heterooligomeric complexes consisting of an ATPase component (ClpX, ClpC or ClpE) and a proteolytic component (ClpP)(PubMed:20305655).
Fourteen ClpP subunits assemble into 2 heptameric rings which stack back to back to give a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes.
Low intrinsic peptidase activity is stimulated by ATP-binding subunits ClpC, ClpE and ClpX. Activity is disregulated by acyldepsipeptides (ADEP) antibiotics, which negate the need for ATP-binding subunits for activation and which makes it into an unregulated protease. Each ClpP subunit binds 1 ADEP molecule, which prevents binding of ClpX. ADEP binding causes conformational shifts that open the gated pore of the ring (PubMed:20305655). Protease activity is inhibited by diisopropylfluoro-phosphate (PubMed:22080375). Protease activity is inhibited by bortezomib, an oncology drug originally designed to work on the human proteasome (PubMed:31155236).
No degradation of trans-translationally tagged-peptides (PubMed:11395451, PubMed:31155236). Triple rqcH clpP ssrA mutants cannot be generated (ssrA, or tmRNA, encodes the SsrA tag added to nascent proteins in stalled ribosomes by trans-translation, targeting the nascent protein for degradation) (PubMed:31155236).
Peptide exit pores open in the compressed state; in this conformation the active site residues move apart and the protease cannot be active.
Belongs to the isocitrate and isopropylmalate dehydrogenases family.
The enzyme can be phosphorylated in vitro by the E.coli isocitrate dehydrogenase kinase/phosphatase, but B.subtilis lacks such an enzyme.
Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases.
Expressed at the end of vegetative growth.
Loss of ability to grow with glutathione as a sulfur source.
Belongs to the AB hydrolase superfamily. MenH family.
Catalyzes a proton abstraction reaction that results in 2,5-elimination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC) and the formation of 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC).
Belongs to the LDH2/MDH2 oxidoreductase family.
Belongs to the type-B carboxylesterase/lipase family.
Catalyzes hydrolysis of several beta-lactam antibiotic PNB esters to the corresponding free acid and PNB alcohol.
Induced by Btr in iron-limited conditions.
Repressed by AbrB during growth and activated at the onset of sporulation in a Spo0A-dependent manner.
Required for proper spore morphogenesis. Important for spore germination.
In the C-terminal section; belongs to the 5'-nucleotidase family.
Requires a minimum of 0.1 mM of calcium for a significant activity. Maximal activity was observed with concentrations of calcium between 1 to 5 mM. Is 10-fold less active with the corresponding concentrations of manganese. Inhibited by NaCl at concentrations of 100 mM and higher.
Sugar-nonspecific endonuclease that yields nucleotide 3'-monophosphate products. No 5'-nucleotidase activity was detected, using 5'-AMP as the substrate, in the presence of diverse divalent metals and with various pH values.
Belongs to the terpene cyclase/mutase family.
Catalyzes the cyclization of tetraprenyl beta-curcumene into sporulenol.
Belongs to the YohK (E.coli)/YwbG (IPA-22R) (B.subtilis) family.
Belongs to the DEAD box helicase family. CshA subfamily.
DEAD-box RNA helicase possibly involved in RNA degradation. Unwinds dsRNA in both 5'- and 3'-directions, has RNA-dependent ATPase activity.
Homodimer or oligomer. May interact with RNA helicases CshB and DbpA (DeaD). Probably a component of the RNA degradosome complex composed of rny, rnjA, rnjB, pnp, pfkA and eno, and possibly also rnpA (although rnjA and rnjB's presence is unclear). Interacts with ribosomal proteins L1 and L3 (rplA and rplC) and the protein component of RNase RnpA. Interacts with the RNA polymerase core (PubMed:21710567).
Induced by cold shock (PubMed:12399512). Constitutively expressed at 37 and 16 degrees Celsius in rich and minimal medium and in exponential, transition and stationary phase (at protein level) (PubMed:20572937, PubMed:23175651). Protein level not increased at 16 degrees Celsius (at protein level) (PubMed:20572937).
Oligomerizes, may be a member of the RNA degradosome.
RNA helicase activity is inhibited by EDTA.
Slow vegetative growth at 37 degrees Celsius, impaired growth at 22 degrees Celsius (PubMed:16861794) and 16 degrees Celsius (PubMed:23175651). Another report shows no growth difference at 15 degrees Celsius (PubMed:16352840). The presence of CshA or CshB is essential for viability; in a cshA disruption mutant further depletion of cshB stops growth after 1 cell duplication (PubMed:16352840). Others show a quadruple disruption of all RNA helicases (cshA, cshB, deaD, yfmL) was not lethal at 37 degrees Celsius, although both 50S and 70S ribosomes are decreased, growth stops at 16 degrees (PubMed:23175651). At 20 degrees Celsius cells are elongated and wrinkled, with smaller cell diameter and thickened walls, and decreased amounts of 70S and 50S ribosomes; levels of over 200 transcripts are altered (PubMed:23175651).
The C-terminal half of the protein (residues 225-494) is required for interaction with most RNA degradosome partners, whereas dimerization or oligomerization only requires the extreme C-terminus (residues 413-494). Addition of the latter domain to CshB confers on it the ability to interact with Rny.
The most abundant DEAD-box RNA helicase. An ATP-dependent RNA helicase with RNA-dependent ATPase activity. May work in conjunction with the cold shock proteins to ensure proper initiation of transcription at low and optimal temperatures. In vitro, unwinds dsRNA in both 5'- and 3'- directions. Plays a role in ribosomal 50S subunit assembly. Its deletion leads to changes in mRNA levels for over 200 transcripts.
Belongs to the imidazoleglycerol-phosphate dehydratase family.
Endonucleolytically cleaves ssRNA generating a 3'-OH and (presumably) a 5'-phosphate group. Cleaves preferentially at U residues, has no activity on dsRNA or dsDNA. Upon expression in E.coli contributes to the degradation of small RNA (sRNA) RhyB.
Mn(2+) gives highest endonuclease activity in vitro, followed by Mg(2+) and to a lesser extent by Co(2+).
No visible phenotype, no effect on sporulation. A quintuple ribonuclease deletion mutant (pnp, rph, rnr, yhaM, yloC) is viable.
Oligomerizes, perhaps as a hexamer (PubMed:34815358). Might interact with PNPase (pnp) in E.coli (PubMed:34815358) (Probable).
Catalyzes the reversible NAD(+)-dependent oxidation of scyllo-inositol (SI) to 2,4,6/3,5-pentahydroxycyclohexanone (scyllo-inosose or SIS). Is required for SI catabolism that allows B.subtilis to utilize SI as the sole carbon source for growth. Cannot use NADP(+) instead of NAD(+).
Inactivation of this gene abolishes growth on SI as the sole carbon source, but does not affect growth on MI or glucose.
Induced by either myo-inositol (MI) or SI; SI is approximately three times more efficient than MI.
Belongs to the phosphoglycerate kinase family.
Expressed under the control of the late mother cell-specific sigma factor sigma-K.
L-Ala--D-Glu endopeptidase involved in production of single L-alanine side chains from tetrapeptides in the spore cortex peptidoglycan. Therefore, is required for the endospore cortex maturation.
The presence of single L-alanine residues in the spore cortex increases the spores ability to be resistant to heat.
Belongs to the sigma-70 factor family. SigB subfamily.
By heat shock, salt stress, oxidative stress, glucose limitation, oxygen limitation and entry into stationary phase. Association with RNAP core increases during alcohol, NaOH, NaCl stress and during sporulation (at protein level) (PubMed:21710567).
Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released. Sigma B is not essential for sporulation; rather it is required for maximal expression of ctc and csbA which are transcribed in the early stationary phase under conditions inimical to sporulation. May play a role in the ability of the bacterium to adapt to various stresses but is not essential for its survival under these conditions. Positively regulates expression of its own operon. The second most abundant sigma factor, it associates with RNAP core under all growth phases (PubMed:21710567).
Part of the ABC transporter complex BceAB (TC 3.A.1.123.5) involved in bacitracin export.
Probably functions as a sodium/glutamine symporter for glutamine uptake.
A late competence gene, expression is enhanced in the presence of ComK.
Belongs to the thioredoxin family. DsbA subfamily.
Cells partially restore cytochrome c oxidase activity in a CcdA-deficient mutant, possibly because the bacteria can no longer oxidize the 2 heme-binding thiol groups in apocytochrome c.
Required for the stabilization, possibly via formation of a disulfide bond, of the obligatory competence protein ComGC. May be required for the stability of secreted proteins with disulfide bonds. Not required for sporulation.
Involved in formation and maintenance of cell shape.
Involved in formation and maintenance of cell shape. Required for the formation of proper helical filaments of MreB and for cell wall synthesis in the cylindrical part of the cell leading to cell elongation.
Loss of viability. Cells lacking sufficient quantities of this protein undergo morphological changes, namely, swelling and twisting of the cells followed by cell lysis. A polymeric material accumulates at one side of the division septum of the cells and the presence of this material correlates with the bending of the cell. After prolonged depletion in the presence of MgCl(2), the cells become very short and fat and eventually spheroidal, but no significant lysis is observed. Addition of sucrose results in rounded cells. Cells are still capable of making division septa. Null mutants show little or no sign of a defined long axis and have a severe shape defect.
Self-associates. Interacts with MreD and proteins that belong to class A and class B high-molecular-weight penicillin-binding proteins (PBP2b, PBP1, PBP2a, PBP3, PBP4, PBP2c, PBP2d, PBPH and PBP4b).
Belongs to the glutamyl-tRNA reductase family.
Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
During catalysis, the active site Cys acts as a nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate with the formation of a thioester intermediate between enzyme and glutamate, and the concomitant release of tRNA(Glu). The thioester intermediate is finally reduced by direct hydride transfer from NADPH, to form the product GSA.
Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
Constitutively expressed during exponential growth. Encoded in an operon with ydiR and ydiS.
Not essential; its disruption results in increased transformation by plasmid DNA carrying multiple BsuMI target sequences (PubMed:11751814). Triple deletion ydiO-ydiP-ydjA leads to loss of susceptibility to MspJI, which only digests C-methylated DNA (PubMed:32324221).
Involved in a high affinity multicomponent binding-protein-dependent transport system for glycine betaine, carnitine and choline; probably responsible for the translocation of the substrate across the membrane.
Part of the binding-protein-dependent transport system for oligopeptides; probably responsible for the translocation of the substrate across the membrane. Also required for sporulation and competence.
Positive regulatory protein that acts at the late promoter PL.
Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
Activity is stimulated by high salt concentrations with different efficiencies depending on the kind of salt. In vitro, inhibited by glucose.
Hydrolyzes trehalose-6-phosphate to glucose and glucose 6-phosphate. Can also very effectively hydrolyze p-nitrophenyl-alpha-D-glucopyranoside, but not lactose, maltose, sucrose or sucrose-6-phosphate. Trehalose is also hydrolyzed, but to a much smaller extent than trehalose-6-phosphate.
Induced by trehalose and repressed by glucose, fructose or mannitol.
Belongs to the DNA mismatch repair MutS family.
Cells lacking this gene have a 225-fold increased spontaneous mutation frequency. Double or triple disruptions with mutL/nth do not change the frequency.
This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity (By similarity). Overexpression of mutSL partially suppresses the high spontaneous mutation frequency of a ytkD/mutM/mutY triple disruption which lacks the system required to prevent damage by oxidized guanine (8-oxo-dGTP). This suggests that MutSL also functions to repair mismatches due to oxidative stress in both growing and stationary phase cells.
This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity.
Negatively regulates the transcription of the comG operon.
Belongs to the free Met sulfoxide reductase family.
Anti-sigma factor for SigV. Negatively regulates SigV activity through direct interaction.
Interacts (via N-terminal region) with SigV.
Active toward triacylglycerides with a preference for esters with C8:0 acyl groups; barely active on C18:1 or C18:4 substrates. Active against p-nitrophenylesters with fatty acid chain lengths from C6 to C18.
Maximally expressed in late exponential growth phase. Expression decreases rapidly in the stationary phase. Expressed in both rich and minimal media with glucose as carbon source (at protein level).
Strongly inhibited when incubated with the serine reagent phenylmethylsulfonyl fluoride. Activated by the addition of calcium to the reaction mixture. When calcium was incubated with the lipase but not added to the reaction mixture, its effect is lower but still observable. Magnesium, manganese and strontium are not able to replace calcium with full retention of activity.
Belongs to the pseudouridine synthase RluA family.
Responsible for synthesis of pseudouridine from uracil.
Catalyzes the N-acetylation of S-(2-succino)cysteine. Is involved in a S-(2-succino)cysteine (2SC) degradation pathway that allows B.subtilis to grow on 2SC as a sole sulfur source, via its metabolization to cysteine. Moreover, 2SC is a toxic compound in B.subtilis at high exogenous concentrations, and this enzyme relieves 2SC toxicity via N-acetylation.
Cells lacking this gene almost lose the ability to grow on 2SC as the sulfur source but are still able to grow on sulfate. Moreover, in contrast to wild type, they highly accumulate 2SC when grown on fumarate as the sulfur source. Addition of 2SC causes growth inhibition of the deletion mutant but not the wild type grown on sulfate as the sulfur source.
Fumarate mediated succination of thiols increases in certain tumors and in response to glucotoxicity associated with diabetes. Therefore, S-(2-succino)-adducts such as S-(2-succino)cysteine (2SC) are considered oncometabolites and biomarkers for human disease. The demonstration of a metabolic disposal route for a S-(2-succino)-compound paves the way toward the identification of corresponding pathways in other species.
May catalyze the ATP-dependent phosphorylation of lipids other than diacylglycerol (DAG). In fact, is not able to exhibit diacylglycerol kinase activity in vitro.
Essential, it cannot be deleted (PubMed:8244929, PubMed:8636036). Depletion leads to an arrest of cell division after 80 minutes at 37 degrees Celsius and 40 minutes at 48 degrees Celsius with a concomitant reduction in FtsL and to a lesser extent DivIC levels; cells lengthen after arrest and eventually lyse (PubMed:16936019, PubMed:28792086).
Penicillin-binding proteins (PBPs) function in the late steps of murein biosynthesis. PBP-2B is required for vegetative cell division and sporulation septation. Beta-lactams inactivate the PBPs by acylating an essential serine residue in the active site of these proteins, thereby interrupting normal cell wall synthesis (Probable). This protein itself, but not its transpeptidase activity, is required for cell division (PubMed:28792086).
Synthesized throughout vegetative growth. Synthesis is enhanced during stage II of sporulation and in stage IV mother cells. Undetectable in stage IV forespores. Present in the inner forespore membrane of the dormant spore.
Transcribed at a low constant level in all growth phases. Part of the mraZ-rsmH-ftsL-pbpB operon.
Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.
Carbon 2 of the heme B porphyrin ring is defined according to the Fischer nomenclature.
Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Belongs to the aldo/keto reductase family. Aldo/keto reductase 11 subfamily.
Disruption of this gene affects neither growth on inositol nor the inducibility and catabolite repression of Idh synthesis.
In vitro, is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose and methylglyoxal in the presence of NADPH, albeit with poor efficiency. Shows only trace activity with benzaldehyde and butyraldehyde. Is unable to oxidize myo-inositol with either NADP(+) or NAD(+) as a cosubstrate and also does not use glucose, 2-pyridine carboxyaldehyde, fructose, xylose and succinyl semialdehyde as a substrate (PubMed:12554958, PubMed:15019785). The physiological function of this enzyme is not clear (PubMed:15019785). Does not seem to be necessary for inositol catabolism (PubMed:9226270).
Induced by inositol (PubMed:9226270). Repressed by glucose (PubMed:11160890). Is cotranscribed with iolR, the repressor of the iol operon (PubMed:9226270).
The 3D-structure shows a unique architecture for an AKR active site, which may explain the low catalytic power.
Phosphorylates the sporulation-regulatory proteins spo0A and spo0F. Spo0F is required for the KinB activity.
During sporulation, is negatively regulated by MciZ, which binds to FtsZ and inhibits its polymerization and the formation of the Z ring.
Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.
Homodimer. Polymerizes to form a dynamic ring structure in a strictly GTP-dependent manner (By similarity). Interacts directly with several other division proteins (By similarity). Interacts with FtsA (PubMed:16159787). Interacts with Phi29 DNA replication protein 1 (PubMed:23836667). Interacts with the cell division inhibitor MciZ (PubMed:23836667, PubMed:25848052).
Homodimer. Polymerizes to form a dynamic ring structure in a strictly GTP-dependent manner. Interacts directly with several other division proteins.
Belongs to the helicase family. DnaB subfamily.
Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity.
Cells lacking this gene have a 5-fold increased spontaneous mutation frequency. A double mutM/mutY mutant has a 1000-fold increased spontaneous mutation frequency (PubMed:12483591). Triple ytkD/mutM/mutY disrupted strains show increased mutation rates during both exponential and stationary phase (PubMed:19011023).
Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
Involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine, 8-oxo-dGTP) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions (By similarity). Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 8-oxo-dGTP. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base.
Reduces glyoxal and methylglyoxal (2-oxopropanal). Is not involved in the vitamin B6 biosynthesis.
Belongs to the methylglyoxal synthase family.
Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate.
Produced during the exponential death phase of growth, just before sporulation.
Produces unsaturated products from polygalacturonate.
Belongs to the glutathione peroxidase family.
Cleaves the peptide side chain from the N-acetylmuramic acid residues in peptidoglycan. This is a step in the formation of muramic delta-lactam residues in spore cortex.
CwlD and PdaA are necessary and sufficient for muramic delta-lactam production in B.subtilis spore peptidoglycan.
Expression of cwlD takes place in both the mother cell and forespore compartments of sporulating cells.
Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family.
A conformational change of sigma-A occurs during its association with the core enzyme.
Association with RNAP core remains approximately constant during all stresses tested and during sporulation (at protein level).
Belongs to the sigma-70 factor family. RpoD/SigA subfamily.
Interacts transiently with the RNA polymerase catalytic core.
Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released. This sigma factor is the primary sigma factor during all growth phases, stress and during sporulation. It associates with the RNAP core at all growth stages with a slight increase in stationary phase.
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth.
Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. Probably catalyzes the dehydration of the (S)-3-hydroxy-3-methylglutaryl group attached to PksL.
The growth-defect caused by the iolF inactivation was only observed in the iolT-null background.
Belongs to the 2H phosphoesterase superfamily. ThpR family.
Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
Belongs to the gamma-glutamyl phosphate reductase family.
Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
Could be the product of a pseudogene. This sequence is shorter than orthologs and lacks the conserved active site Tyr residue.
Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family.
Catalyzes phosphorolysis of the pyrimidine nucleosides uridine, thymidine and 2'-deoxyuridine with the formation of the corresponding pyrimidine base and ribose-1-phosphate.
Bacillus subtilis contains 2 species of O-6-methylguanine-DNA alkyltransferases. Ogt and adaB are regulated in different ways, constitutively and inducibly on adaptive treatment, respectively.
May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO.
Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity.
May be involved in polyketide synthesis.
Part of the ABC transporter complex YfiYZ/YfhA/YusV involved in import of the iron-hydroxamate siderophores schizokinen, arthrobactin and corprogen.
The complex is composed of one ATP-binding protein (YusV), two transmembrane proteins (YfiZ and YfhA) and a solute-binding protein (YfiY).
Induced by maltose and repressed by glucose.
Maltodextrin can also be transported inside the cell after degradation to maltose by extracellular amylase AmyE, transported as maltose by MalP.
Part of the ABC transporter complex involved in maltodextrin import. Binds maltodextrin. Can also bind maltose with low affinity, but is not involved in its uptake.
The complex is composed of two ATP-binding proteins (MsmX), two transmembrane proteins (MdxF and MdxG) and a solute-binding protein (MdxE).
An ATP-dependent kinase that phosphorylates glucose to make glucose-6-phosphate, not active on fructose, galactose or mannose. Restores glucose kinase activity in E.coli glk mutants.
Constitutively expressed, activity is maximal at the end of vegetative growth and declines during stationary phase when grown in rich broth (LB) (at protein level). Expressed in a similar fashion in minimal medium containing glucose, fructose, trehalose, maltose or sucrose.
Loss of glucokinase activity, no growth phenotype on glucose, fructose, maltose, sucrose or trehalose-containing minimal media.
Activates the phosphorylation activity of the protein-arginine kinase McsB. Is required for the delocalization of competence proteins from the cell poles.
Cells lacking this gene show a defect in the delocalization of competence proteins.
Is repressed by the transcriptional regulator CtsR. Forms part of an operon with ctsR, mcsB and clpC.
Essential for growth and viability in the presence of catechol and probably involved in the detoxification of catechol.
Increases the processivity of the PcrA helicase, but does not bind to DNA.
Interacts with PcrA, Pdp, YclM, YkvL, YhcQ and YomL. The interaction with PcrA is not essential for cell viability or repair of UV-induced lesions.
Belongs to the acyl coenzyme A hydrolase family.
Belongs to the peroxiredoxin family. Tpx subfamily.
ATPase. Has a role at an early stage in the morphogenesis of the spore coat outer layers. Its ATP hydrolysis is required for proper assembly of the spore coat. Forms a basement layer around the outside surface of the forespore and self-assembles irreversibly into higher order structures by binding and hydrolyzing ATP thus creating a durable and stable platform upon which thereafter morphogenesis of the coat can take place. Required for proper localization of spore coat protein CotE and sporulation-specific proteins including SpoVM.
ATPase. Has a role at an early stage in the morphogenesis of the spore coat.
Expressed soon after the formation of the asymmetric septum during sporulation. Expression commences about 2 hours after the onset of sporulation. Assembly around the developing forespore commences at the time of polar division and seems to continue after engulfment of the forespore is complete. Remains present throughout the late stages of morphogenesis and during this accumulation process preferentially collects on the mother cell side of the engulfed forespore, but eventually is deposited equally all around the forespore.
Extreme C-terminal region (AA 487-492) is required for its proper localization into a spherical shell around the developing forespore. N-terminus (AA 1-64) is functionally important although largely dispensable for proper localization.
Forespores lack a well-defined cortex, and the coat is present as swirls in the mother cell compartment of the sporangia rather than having been deposited around the forespore protoplasts. According to PubMed:18691972, unable to sporulate.
Polymerizes to self-assemble into static filaments. ATP hydrolysis is required by every subunit for incorporation into the growing polymer by inducing a conformational change that drives polymerization of a nucleotide-free filament. Polymerization requires a critical concentration of the protein and only occurs after it is localized to the surface of the developing spore. Interacts (via extreme C-terminus Gly-486) with SpoVM (via Ile-6). Interacts (via full-length) with SpoVID (via C-terminus 499-575 AA). Interacts with SafA.
Seems to be cleaved by the YabG protease.
Belongs to the ATP phosphoribosyltransferase family. Short subfamily.
Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity (By similarity).
Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
Heteromultimer composed of HisG and HisZ subunits.
Lacks the C-terminal regulatory region which is replaced by HisZ.
Processing of ComGC in competent cells requires ComC, while stabilization, possibly by formation of a disulfide bond, requires BdbC and BdbD.
Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. MtnE subfamily.
Disruption mutant grows more slowly than the wild type strain on methylthioribose (MTR) as the sulfur source.
Involved in the methylthioribose (MTR) recycling pathway (PubMed:12022921, PubMed:24837359). Catalyzes the formation of methionine from 2-keto-4-methylthiobutyrate (KMTB) (PubMed:12670965, PubMed:24837359).
Belongs to the helicase family. RecQ subfamily.
Cells lacking this gene have an increased sensitivity to DNA damaging agents, 100-fold decreased plasmid transformation and 4-fold reduced chromosomal DNA transformation. Sensitivity increases in the presence of mutated AddAB nuclease.
Probable DNA helicase. Required in synaptic and/or post-synaptic stages of recombination. Probably has overlapping function with RecQ (AC O34748). It probably acts to help generate ss-DNA from ds-DNA breaks.
Belongs to the bacterial solute-binding protein 9 family.
Cells lacking this gene grow slowly in zinc-deficient medium; this effect is suppressed upon addition of exogenous Zn(2+). Growth is slower yet in a double knockout with YciC. Disruption results in low transformability.
Part of the ATP-binding cassette (ABC) transport system ZnuABC involved in zinc import (By similarity). Binds zinc with high affinity and specificity and delivers it to the membrane permease for translocation into the cytoplasm (By similarity). ZnuABC-mediated zinc transport is required for comF expression and competence development (PubMed:21813502, PubMed:9811636).
The complex is composed of two ATP-binding proteins (ZnuC), two transmembrane proteins (ZnuB) and a solute-binding protein (ZnuA).
Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a repressor.
Belongs to the biotin--protein ligase family.
Involved in the control of degradation of B.subtilis amidophosphoribosyltransferase (purF). Probably activates the gene for a degradative protease.
May act as an export chaperone for the filament capping protein FliD.
Component of the 30S ribosomal translation pre-initiation complex which assembles on the 30S ribosome in the order IF-2 and IF-3, IF-1 and N-formylmethionyl-tRNA(fMet); mRNA recruitment can occur at any time during PIC assembly.
One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex.
Putative nitroreductase that may contribute to the degradation of aromatic compounds.
Repressed by YodB. Strongly induced by stress due to exposure to catechol and less strongly induced after diamide or 2-methylhydroquinone (2-MHQ) stress. Not induced by oxidative stress due to hydrogen peroxide or methylglyoxal.
This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (By similarity).
Belongs to the alpha/beta-type SASP family.
SASP are bound to spore DNA. They are double-stranded DNA-binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light.
SASP are degraded in the first minutes of spore germination and provide amino acids for both new protein synthesis and metabolism.
Deletion of the gene does not affect growth on glucose and arabinose, but it has a negative effect on the ability of the mutant to grow on the alpha-1,5-arabinose oligomers alpha-1,5-arabinobiose, alpha-1,5-arabinotriose and alpha-1,5-arabinotetraose. AraE/araN double mutant is unable to grow in the presence of alpha-1,5-arabinobiose.
Part of the ABC transporter complex AraNPQ involved in the uptake of arabinooligosaccharides. Transports alpha-1,5-arabinooligosaccharides, at least up to four L-arabinosyl units (PubMed:20693325). AraN captures the substrate and delivers it to the two transmembrane components (Probable).
Branched-chain amino acid transport system which is involved in the uptake of isoleucine, valine and probably leucine (PubMed:25645558). Together with BcaP and BrnQ, plays an important role in the activation of CodY, a branched-chain amino acid-responsive transcriptional regulator that controls the expression of several dozen transcription units in B.subtilis (PubMed:25645558).
Expression is under both negative and positive control by the transcriptional regulator CodY (PubMed:26473603). The negative control is direct and the positive control is indirect and mediated by another transcriptional regulator, ScoC (or Hpr), which, in turn, is repressed by CodY (PubMed:26473603). Thus, CodY and ScoC form a feed-forward regulatory loop in which CodY acts an indirect positive regulator of braB (PubMed:26473603). This feed-forward regulatory loop at the braB promoter is an arrangement in which two regulatory proteins repress the same target gene and one of the regulators represses expression of the other (PubMed:26473603).
Mutant is still able to take up isoleucine, leucine and valine.
Found in a complex with F(1)F(0) ATP synthase and SpoIIIJ and YqjG.
Probable signaling protein whose physiological role is not yet known.
Belongs to the glycerol-1-phosphate dehydrogenase family.
Binds 1 nickel ion per subunit. Is not active with other divalent metal cations such as Zn(2+), Cu(2+), Ca(2+), Mg(2+), Mn(2+) or Fe(2+).
Catalyzes the NAD(P)H-dependent reduction of dihydroxyacetonephosphate (DHAP or glycerone phosphate) to glycerol 1-phosphate (G1P). The G1P thus generated is probably used for the synthesis of phosphoglycerolipids in Gram-positive bacterial species.
Catalyzes the NAD(P)H-dependent reduction of dihydroxyacetonephosphate (DHAP or glycerone phosphate) to glycerol 1-phosphate (G1P). The G1P thus generated is probably used for the synthesis of phosphoglycerolipids in Gram-positive bacterial species. Prefers NADH over NADPH as coenzyme. Is also able to catalyze the reverse reaction, i.e. the NAD(+)-dependent oxidation of G1P but not of G3P. Does not possess glycerol dehydrogenase activity.
Acts to efflux copper or a copper complex. It is possible that YfmO could contribute to copper resistance.
Active only in the forespore (PubMed:18208527).
Activity repressed by anti-sigma-G factor Gin (csfB) and Lon protease during the early stages of forespore development (PubMed:17921305). When both Gin and sigma-G are expressed in E.coli Gin inhibits sigma-G activity, strongly suggesting Gin inhibits by direct physical interaction (PubMed:19497328).
Expressed and active 2 hours after sporulation starts (at protein level); stimulates its own transcription (PubMed:18208527).
Interacts with anti-sigma-G factor Gin (csfB) (PubMed:18208527, PubMed:19497328).
Recognition of anti-sigma-G factor Gin (csfB) occurs via the first 71 residues (PubMed:18208527).
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released (PubMed:18208527). This sigma factor is responsible for the expression of sporulation specific genes in the forespore (PubMed:18208527).
Involved in the catabolism of quinolinic acid (QA).
It is uncertain whether Met-1, Leu-59 or Met-74 is the initiator.
Belongs to the RecD family. RecD-like subfamily.
DNA-dependent ATPase and ATP-dependent 5'-3' DNA helicase. Has no activity on blunt DNA or DNA with 3'-overhangs, requires at least 10 bases of 5'-ssDNA for helicase activity.
Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.
Involved in the biosynthesis of p-aminobenzoate (PABA), a precursor of tetrahydrofolate. Converts 4-amino-4-deoxychorismate into 4-aminobenzoate (PABA) and pyruvate (By similarity).
Requires p-aminobenzoic acid for growth.
Acts as a negative controlling element, employing Zn(2+) as a cofactor to bind the operator of the repressed genes. Required for the zinc-specific repression of two operons implicated in zinc uptake, yciC and ycdHIyceA. Also represses the expression of rpmE2, the gene for ribosomal protein L31B, which is expressed only after the end of exponential growth.
Contains 3 zinc-binding sites. Site 1 has a structural role and site 2 is the Zn(2+) sensing site. Site 3 residues do not bind metal ions with a physiologically relevant affinity, but contribute to dimer stability.
Sequentially activated from an inactive dimer (Zur(2):Zn(2)) to a partially active asymmetric dimer (Zur(2):Zn(3)), and finally to the fully zinc-loaded active form (Zur(2):Zn(4)). Binds a maximum of 4 Zn(2+) ions per dimer.
Belongs to the HPS/KGPDC family. HPS subfamily.
Catalyzes the condensation of ribulose 5-phosphate with formaldehyde to form 3-hexulose 6-phosphate. Together with HxlB, may act as a formaldehyde detoxification system.
Aldo-keto reductase (AKR) that displays broad substrate specificity in vitro. Is able to reduce the standard AKR substrates DL-glyceraldehyde, D-erythrose, methylglyoxal, p-nitrobenzaldehyde, benzaldehyde and butyraldehyde, in the presence of NADPH. Cannot use NADH as a cosubstrate. Does not act on glucose, 2-pyridine carboxyaldehyde, fructose and xylose. The physiological function of this enzyme is not clear. May play a role in bacterial stress response and/or in detoxification of reactive aldehydes.
Is under the control of the sigma-B transcription factor. Is induced by heat shock, salt stress, oxidative stress, glucose limitation and oxygen limitation.
Arrested in competence development and sporulation.
By heat-shock, ethanol stress, zinc, cobalt and cadmium.
Couples the hydrolysis of ATP with the transport of cadmium, zinc and cobalt out of the cell. Does not seem to transport copper.
Expression increases rapidly at 5 hours and peaks at 7 hours after onset of sporulation.
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains (Probable). The F(1)F(0) complex interacts with SpoIIIJ and YqjG; YqgA is found in the same complex.
F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains.
Belongs to the methyltransferase superfamily. RsmH family.
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Transcribed at a low level in exponential phase, it may be further induced in stationary phase. Part of the mraZ-rsmH-ftsL-pbpB operon.
Required for YukE secretion. Probable component or regulator of the ESX/ESAT-6-like secretion system (BsEss) (PubMed:23861817, PubMed:24798022). Bacteriophage SPP1 receptor. Essential for the irreversible adsorption of the bacteriophage (PubMed:15576783).
Negative regulator of sigma-B activity. Dephosphorylates RsbS. Plays a role both in maintaining low sigma-B activity during growth and in reestablishing prestress sigma-B activity after induction. Could have a negative feedback role by indirectly communicating sigma-B protein levels.
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily.
Catalyzes the transfer of the alpha-amino group from L-lysine to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). B.subtilis is the only bacterium known to utilize L-lysine as an amino donor in the biosynthesis of DAPA.
Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only aminotransferase known to utilize SAM as an amino donor.
Inhibited by 7-keto-8-aminopelargonic acid at concentrations above 80 uM.
Acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate cofactor to form pyridoxamine and an alpha-keto acid in the first half-reaction.
Acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate cofactor to form pyridoxamine and an alpha-keto acid in the first half-reaction. The second half-reaction is the reverse of the first, transferring the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essential bacterial cell wall components (By similarity).
Activated by the two-component regulatory system MalK/MalR in response to malate. The regulator MalR binds to the promoter region of yflS.
Belongs to the SLC13A/DASS transporter (TC 2.A.47) family. DIT1 subfamily.
Expressed in the mother cell compartment at the second hour of sporulation.
Expression is sigma E-dependent and negatively regulated by spo0A.
Belongs to the cytidylate kinase family. Type 1 subfamily.
Transcribed during sporulation. May not be transcribed with the downstream gene (a ribosomal protein bS1 homolog), there is a probable transcription terminator between the 2 genes.
Together with YxlE, is important for negative regulation of sigma Y activity, being the major negative regulator.
Belongs to the universal stress protein A family.
Belongs to the bacterial/plant glucose-1-phosphate adenylyltransferase family.
Expressed exclusively on media containing carbon sources that allow efficient sporulation.
Delay in chromosome segregation and an increase in the sensitivity to agents that induce DNA damage. They divide over unsegregated chromosomes with increased frequencies. A cell filamentation phenotype can also be seen, when associated with a noc deletion.
Required for the accurate completion of chromosome partitioning, in part by promoting efficient resolution of chromosome dimers, before the formation of the division septum. Binds to DNA in a non-specific manner. Shows ATPase activity. Not required for cytokinesis.
StfA and SpoIIIE are not functionally redundant. They probably play distinct roles during growth and sporulation.
Expression is regulated by the XptR regulon. Negatively regulated by hypoxanthine and guanine.
Involved in the uptake of the purine ribonucleosides inosine and guanosine.
Belongs to the 2H phosphoesterase superfamily. YjcG family.
Essential for filament assembly (PubMed:23144244). May act as a facilitator of flagellin (hag) secretion. Antagonizes translational repressor CsrA indirectly (PubMed:23144244).
Homodimer (PubMed:23144244, PubMed:16021622). Interacts directly with flagellin (hag), forms a 3-way complex of Hag, FliS and FliW in which Flis and FliW do not directly interact (PubMed:23144244).
Severe defect in motility on agar plates, forms multiple short filament stubs on the cell surface, decreased expression of flagellin (hag), 30-fold decrease in Hag secretion. All phenotypes are partially suppressed by deletion of csrA, which increases translation of Hag (PubMed:23144244).
Member of the two-component regulatory system YesM/YesN. Probably activates YesN by phosphorylation.
ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
Belongs to the ABC transporter superfamily. Energy-coupling factor EcfA family.
Expressed only in the forespore compartment of sporulating cells. Disappears after 45 minutes of spore germination. Expression is sigma G-dependent.
An esterase which preferentially hydrolyzes triacylglyceride substrates with short chain fatty acids (C3-C10) with the maximum activity towards tricaprylin (C8:0); essentially inactive on C18:1 or C18:4 substrates. Active against p-nitrophenylesters with fatty acid chain lengths from C6 to C18.
Induced in rich but not minimal media with glucose as carbon source (at protein level). Induced by growth on n-hexadecane and tributyrin.
Disulfide cross-linked either to itself or to CotY.
Belongs to the ABC transporter superfamily. Iron (Fe3+)-hydroxamate importer (TC 3.A.1.14.7) family.
Part of the ABC transporter complex FhuBGCD involved in iron(3+)-hydroxamate import. Responsible for energy coupling to the transport system (By similarity).
The complex is composed of an ATP-binding protein (FhuC), two transmembrane proteins (FhuB and FhuG) and a solute-binding protein (FhuD or YxeB).
Belongs to the major facilitator superfamily. Drug:H(+) antiporter-3 (DHA3) (TC 2.A.1.21) family.
Involved, directly or indirectly, in spore cortex biosynthesis. Affects only indirectly the expression of late sporulation genes.
SpoVB transcription takes place during the second hour of sporulation. It may be transcribed mainly, if not only, in the mother cell. Indeed, it is required only in the mother cell.
Positively regulates the ntdABC operon and negatively regulates its own transcription. Binds to NTD to induce ntdABC transcription.
Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. HflX GTPase family.
GTPase that associates with the 50S ribosomal subunit and may have a role during protein synthesis or ribosome biogenesis.
Monomer. Associates with the 50S ribosomal subunit.
Belongs to the universal ribosomal protein uL5 family.
Part of the 50S ribosomal subunit (PubMed:30126986). Part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA and the P site tRNA. Forms a bridge to the 30S subunit in the 70S ribosome (By similarity). Interacts with VmlR (PubMed:30126986).
Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA and the P site tRNA. Forms a bridge to the 30S subunit in the 70S ribosome.
This is 1 of the proteins that bind and probably mediate the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.
This is one of the proteins that bind and probably mediate the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.
Involved in spore core dehydration; might be involved in the transport of something into or out of the forespore or could be required for some modification of the cortex peptidoglycan structure.
Belongs to the prephenate/arogenate dehydrogenase family.
Belongs to the phosphopentomutase family.
Phosphotransfer between the C1 and C5 carbon atoms of pentose.
Involved in forespore engulfment and required for anchoring membrane proteins on the forespore side of the septal membrane. Forms a channel with SpoIIIAH that is open on the forespore end and closed (or gated) on the mother cell end. This allows sigma-E-directed gene expression in the mother-cell compartment of the sporangium to trigger the activation of sigma-G forespore-specific gene expression by a pathway of intercellular signaling.
Specifically expressed in the forespore under the control of the sigma-K factor.
Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits) (Probable). Has a partially redundant function with PBP-2A (pbpA) during spore outgrowth (PubMed:9851991).
Expression increases during vegetative growth and decreases soon after entry into sporulation.
It is uncertain whether Met-1 or Met-3 is the initiator.
No visible phenotype (PubMed:7961491). Double pbpA-pbpD deletions spores have greatly decreased spore outgrowth and peptidoglycan synthesis (PubMed:9851991).
Acts as an anti-CsrA protein, binds CsrA and prevents it from repressing translation of its target genes, one of which is flagellin. Binds to flagellin (hag), which is implicated in polymerization, and participates in the assembly of the flagellum (PubMed:16936039). An antagonist to translational regulator CsrA, it binds CsrA at an allosteric site and non-competitively inhibits CsrA binding to hag RNA (PubMed:27516547). Partner switching by flagellin between FliW and CsrA provides a flagellar assembly checkpoint to tightly control the timing of flagellin synthesis. Flagellin binds to assembly factor FliW, freeing translation regulator CsrA to repress translation of the flagellin mRNA. When the flagellar hook is assembled flagellin is secreted, depleting intracellular flagellin, which frees FliW to interact with CsrA and inhibits CsrA binding to mRNA. This derepresses flagellin translation and provides protein for flagellar assembly. Once the flagellar filament is completed cytoplasmic flagellin levels rise and CsrA translation repression of flagellin reinitiates (PubMed:21895793). Binds to CsrA and displaces it from hag mRNA (PubMed:21895793, PubMed:27516547). Binds to hag mRNA itself, but only at much higher concentrations than those required to displace CsrA (PubMed:21895793, PubMed:27516547).
Acts as an anti-CsrA protein, binds CsrA and prevents it from repressing translation of its target genes, one of which is flagellin. Binds to flagellin and participates in the assembly of the flagellum.
Greatly reduced swarming motility, less flagellin (PubMed:16936039, PubMed:21895793). Fewer, shorter flagella assemble (PubMed:21895793). Loss of motility and flagellar assembly are suppressed by deletion of csrA (PubMed:21895793). Decreased expression of flagellin (Hag) which is suppressed by deletion of csrA (PubMed:23144244).
Interacts with flagellin in a 1:1 complex (PubMed:16936039, PubMed:21895793). Two molecules interact with each CsrA dimer; cannot interact with both flagellin and CsrA simultaneously (PubMed:21895793, PubMed:27516547). Has a higher affinity for CsrA than for flagellin (PubMed:21895793). Interacts directly with flagellin (hag), forms a 3-way complex of Hag, FliS and FliW in which Flis and FliW do not directly interact (PubMed:23144244). Interaction with Hag may occur via the C-terminus of Hag (PubMed:16936039).
Interacts with translational regulator CsrA and flagellin(s).
Part of the SigD-controlled yvyF-csrA operon and the SigA-controlled fliW-csrA operon (PubMed:17555441).
Belongs to the monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family.
Belongs to the monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family. Nhak (TC 2.A.36.3.2) subfamily.
Constitutively expressed, with higher levels at stationary phase.
Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
Transporter involved in the efflux of sodium, potassium, lithium and rubidium.
Belongs to the RecA family. RadA subfamily.
DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function.
General sensitivity to DNA damaging agents. Increased sensitivity to methyl methanesulfonate (MMS), decreased survival after UV irradiation in transition and stationary phase, decrease in transformation with chromosomal DNA requiring homologous recombination (PubMed:9141693, PubMed:11810266). Increased sensitivity to mitomycin C, H(2)O(2), and nalidixic acid; a further disA deletion suppresses H(2)O(2) sensitivity but has no effect on MMS sensitivity, suggesting radA and disA might work in the same DNA repair pathway (PubMed:25616256). Partially suppresses DNA damaging agent sensitivity of recU deletions (PubMed:11810266). Suppresses a chromosome segregation defect in ruvA and recD mutants cells, but not in recU mutant cells (PubMed:15317759).
Has a putative N-terminal zinc-finger, a middle region with homology to RecA with ATPase motifs including the RadA KNRFG motif, while the C-terminus is homologous to Lon protease.
Plays a role in DNA repair (PubMed:9141693, PubMed:11810266). Might stabilize or process Holliday junction intermediates (PubMed:15317759). May work with DisA following methyl methanesulfonate (MMS) but not H(2)O(2) damage; DisA is a DNA integrity scanning protein with c-di-AMP synthase activity.
Plays a role in repairing double-strand DNA breaks, probably involving stabilizing or processing branched DNA or blocked replication forks.
The middle region has homology to RecA with ATPase motifs including the RadA KNRFG motif, while the C-terminus is homologous to Lon protease.
Deletion of the gene has no detectable effect on expression of the srfA operon.
Inhibited by PhrK, which prevents RapK-ComA interaction.
Involved in the regulation of genetic competence development (PubMed:16816200). Inhibits the activity of ComA, a transcriptional factor that regulates the development of genetic competence (PubMed:16816200). Likely affects the activity of additional regulators, in particular Spo0A (PubMed:16816200).
3-fold induction by growth at 15 degrees Celsius.
A 50S ribosomal subunit assembly protein with GTPase activity, required for 50S subunit assembly at low temperatures, may also play a role in translation. Binds GTP and analogs. Binds the 70S ribosome between the 30S and 50S subunits, in a similar position as ribosome-bound EF-G; it contacts a number of ribosomal proteins, both rRNAs and the A-site tRNA.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. BipA subfamily.
No visible growth phenotype at 15 degrees Celsius.
Belongs to the truncated hemoglobin family. Group II subfamily.
Hemoglobin-like protein that exhibits a low peroxidase activity. Its very high oxygen affinity may rule out the possibility that it is involved in oxygen transport.
Methylated by PrmC. Methylation increases the termination efficiency of RF2 (By similarity).
Methylated by PrmC. Methylation increases the termination efficiency of RF2.
Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA.
The gene for this protein contains a UGA in-frame termination codon after Leu-24; a naturally occurring frameshift enables complete translation of RF-2. This provides a mechanism for the protein to regulate its own production.
Induced in response to leucine limitation. Regulated via the T box transcriptional antitermination system.
May participate in leucine metabolism. May transport leucine or a compound related to leucine metabolism.
No growth phenotype is observed for the knockout strain.
Involved in the germinative response to L-alanine. Could be an amino acid transporter. Forms a complex at the inner spore membrane which acts as a receptor for L-alanine, thus is involved in the stimulation of germination in response to alanine. Can stimulate germination in the absence of gerD and gerK gene products (fructose and glucose receptors, respectively), but the response is improved in their presence.
In wild-type cells, during the early stages of sporulation, a product of 43 kDa (the predicted size of SafA) was detected. However, in later stages, a 30-kDa species was the major form of SafA detected. The N-terminus sequence of the 30-kDa product starts at Met-164. It is not known if the smaller form results from proteolysis or from translation initiated at Met-164.
Probably involved in the assembly of some coat protein components implicated in both lysozyme resistance and germination. Could be required for the assembly of CotG. Associates with SpoIVD during the early stage of coat assembly.
Several coat proteins are extracted in reduced amounts from SafA mutant spores, one of which is CotG. SafA mutant spores have abnormal coat layers and have lost their resistance to lysozyme. Their response to L-alanine suggest that they have a defect at a late stage of spore germination. Their response to AGFK also suggests that they have an additional defect at a early stage of spore germination. The mutation of SafA has no effect on vegetative growth and spore resistance to heat and chloroform.
Transcribed by SigE at time T2 of sporulation.
In stationary phase of anaerobic cultures.
Catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate.
A transposon insertion in this gene eliminates the uptake of GABA and severely inhibits the utilization of GABA as a nitrogen source (PubMed:8951816). Triple deletion of gabP, putP and opuE confers resistance to the proline analog 3,4-dehydro-DL-proline (DHP), abolishes GABA utilization and prevents use of proline as a nitrogen source (PubMed:24142252).
Belongs to the amino acid-polyamine-organocation (APC) superfamily. Amino acid transporter (AAT) (TC 2.A.3.1) family.
Positively regulated by TnrA under conditions of nitrogen limitation (PubMed:8951816). Expression is not significantly induced by GABA (PubMed:8951816).
The ligand-recognition profile of the B.subtilis GabP was found to differ substantially from that of the highly homologous E.coli GabP. B.subtilis GabP exhibits more stringent requirements than E.coli GabP for substrate recognition and translocation.
Transporter for gamma-aminobutyrate (GABA) (PubMed:8951816, PubMed:9677314, PubMed:24142252). Can also transport beta-alanine (PubMed:9677314). Can translocate several open-chain GABA analogs (3-aminobutyrate, 3-aminopropanoate, cis-4-aminobutenoate) across the membrane via counterflow against GABA, but cannot transport muscimol (PubMed:9677314). Functions also as a low-affinity proline importer (PubMed:24142252).
Probable member of the two-component regulatory system YxdK/YxdJ. May activate YxdJ in response to the antibacterial protein LL-37.
Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
Cells lacking this gene are unable to grow in medium containing asparagine as a sole carbon source but presents the same growth rate as the wild-type in glucose-containing medium.
In response to oxidative stress, the active site Cys likely reacts with bacillithiol (BSH) to form mixed disulfides to protect the Cys residue against overoxidation. S-bacillithiolation presumably leads to loss of catalytic activity. Debacillithiolation by monothiol bacilliredoxin BrxC restores the activity.
Involved in the gluconeogenesis. Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NADP. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NADP to NADPH. The reduced NADPH is then exchanged with the second NADP, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG.
Belongs to the universal ribosomal protein uS8 family.
One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.
Part of the 30S ribosomal subunit (PubMed:30126986). Contacts proteins S5 and S12 (By similarity).
Part of the 30S ribosomal subunit. Contacts proteins S5 and S12.
Negatively regulates the transcription of the fatR-cypB operon. Is displaced from its operator by a range of fatty acids such as oleate, linoleate and phytanate, thereby allowing transcription of the fatR-cypB operon.
Catalyzes the synthesis of GMP from XMP.
Transcription is activated at hour 4 of sporulation, requires sigma-K and is repressed by GerE. Maximal expression depends on SpoIIID.
Belongs to the DyP-type peroxidase family.
Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently per subunit.
Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently.
Catalyzes the peroxide-dependent oxidation of various industrial dyes contributing to their detoxification and thus can be used for the bioremediation of dye-contaminated wastewater.
Component of the iron transporter efeUOB/M complex composed of EfeU, EfeM and EfeB; EfeU is essential for the complex formation.
Exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Involved in the recovery of exogenous heme iron (By similarity). Extracts iron from heme while preserving the protoporphyrin ring intact (By similarity). Part of the iron transporter system efeUOB/M involved in iron import (PubMed:16672620, PubMed:23764491). Catalyzes the peroxide-mediated oxidation of Fe(2+) into Fe(3+); EfeM binds Fe(3+) and delivers it to the cell membrane permease EfeU (PubMed:23764491).
Involved in the recovery of exogenous heme iron. Extracts iron from heme while preserving the protoporphyrin ring intact.
Severe reduction in Fe(2+) uptake and in cell growth under anaerobic conditions but not in aerobic and microaerobic conditions.
Belongs to the P-Pant transferase superfamily. AcpS family.
Belongs to the P-Pant transferase superfamily. Gsp/Sfp/HetI/AcpT family.
Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of fatty acid acyl-carrier-protein ACP. Also modifies the D-alanyl carrier protein but fails to recognize PCP and AcpK, an acyl carrier protein of secondary metabolism.
Catalyzes the deacetylation of N-acetylmuramic acid (MurNAc) residues in glycan strands of peptidoglycan, leading to the formation of muramic delta-lactam residues in spore cortex, after transpeptidation of deacetylated muramic acid residues. PdaA probably carries out both deacetylation and lactam ring formation and requires the product of CwlD activity on peptidoglycan as a substrate. Is required for germination. Cannot use chitin oligomer (hexa-N-acetylchitohexaose) as a substrate.
Expressed in the forespore, then exported into the developing cortex.
Spores have no muramic delta-lactam structure in the cortex and cannot germinate. Mutant spore peptidoglycan possesses many MurNAc residues lacking peptide side chains.
Belongs to the GTP cyclohydrolase I family.
K(+) ions moderately increases the Vmax, whereas UTP and Ca(2+) and Mg(2+) ions drastically increase the Km for GTP.
Toroid-shaped homodecamer, composed of two pentamers of five dimers.
Catalyzes the specific dephosphorylation of phosphoarginine residues in a large number of proteins. Counteracts the protein arginine kinase McsB in vivo. Can dephosphorylate CtsR-P; thus, can restore the DNA-binding ability of the CtsR repressor by reversing the McsB-mediated phosphorylation. Is the only active pArg phosphatase present in B.subtilis. Exhibits almost no activity against pSer, pThr, or pTyr peptides. Appears to play a role in B.subtilis stress resistance. Protein arginine phosphorylation has a physiologically important role and is involved in the regulation of many critical cellular processes, such as protein homeostasis, motility, competence, and stringent and stress responses, by regulating gene expression and protein activity.
Cellular protein arginine phosphorylation is only detectable in a ywlE mutant and not in the wild-type strain, and global gene expression is significantly impacted in the mutant strain (PubMed:22517742, PubMed:24263382). Cells lacking this gene are impaired in dephosphorylating McsB-P (PubMed:23770242). They also show a reduced resistance to ethanol stress (PubMed:15995210).
Efficiently inhibited by Cu(2+) ion, Zn(2+) ion, sodium pyrophosphate and N-ethylmaleimide, while the addition of Mg(2+), Ca(2+) or Fe(3+) ions has minimal effect. Inhibited in a competitive manner by vanadate.
Expression is up-regulated in the exponential phase of growth, followed by a significant and gradual reduction in the stationary/sporulation phase. Is not up-regulated during ethanol stress.
Was originally thought to be a protein-tyrosine-phosphatase (PubMed:15995210). Was later shown to function as an arginine phosphatase in vivo and in vitro (PubMed:22517742, PubMed:23770242).
The EIID domain, with its homologous EIIC domain, forms the PTS system translocation channel and contains part of its specific substrate-binding site.
By heat shock, salt stress, oxidative stress, glucose limitation and oxygen limitation. Expressed under control of the sigma-B transcription factor.
Catalyzes the formation of UDP-glucose from glucose-1-phosphate and UTP. This is an intermediate step in the biosynthesis of diglucosyl-diacylglycerol (Glc2-DAG), i.e. the predominant glycolipid found in B.subtilis membrane, which is also used as a membrane anchor for lipoteichoic acid (LTA). Has a role in the biosynthesis of all phosphate-containing envelope polymers, since UDP-glucose serves as a glucosyl donor not only for the biosynthesis of LTA but also for wall teichoic acids (WTAs). Is required for biofilm formation. This is likely due to another role of UDP-glucose, which might also act as a metabolic signal regulating biofilm formation or may be involved in some unknown biosynthetic pathway essential for biofilm formation, e.g. the synthesis of an exopolysaccharide.
GtaB is the main UGPase enzyme producing UDP-glucose under both aerobic and anaerobic fermentative growth conditions (PubMed:33556370). YngB augments UDP-glucose production under anaerobic growth conditions (PubMed:33556370).
Under aerobic growth condition, deletion mutants display morphological defects and the cells are curled and show some bulges (PubMed:33556370). No aberrant morphology is observed for the deletion mutants under anaerobic growth conditions (PubMed:33556370).
Catalyzes the dephosphorylation of phosphorylated 5-6 carbon sugars and monophosphate nucleotides (NMP) in vitro (By similarity). To a lesser extent, dephosphorylates flavin mononucleotide (FMN) in vitro (PubMed:26316208).
May play a role in the degradation of rhamnogalacturonan derived from plant cell walls. Probably has broad substrate specificity and may degrade several types of acetylated substrates.
In the presence of sucrose, SacY is activated and prevents premature termination of transcription by binding to a RNA-antiterminator (RAT) sequence (partially overlapping with the terminator sequence) located upstream of the sacB gene. Formation of the SacY-RAT complex prevents alternative formation of the terminator, allowing transcription of the sacB gene. In the absence of sucrose, inhibition of SacY activity by SacX leads to termination of transcription.
Phosphorylated by HPr (PtsH). Also phosphorylated by SacX on His-99, leading to its inactivation.
Belongs to the quinolinate synthase family. Type 3 subfamily.
Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. All amino acids serve as attractants in B.subtilis, they appear to cause an increase in the turnover methyl groups, leading to methylation of an unidentified acceptor, while repellents have been shown to cause a decrease in methyl group turnover. The methyl groups are added by a methyltransferase and removed by a methylesterase.
Belongs to the asparagine synthetase family.
Catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to formate and tetrahydrofolate (FH4).
Part of the ABC transporter complex YfmCDEF involved in citrate-dependent Fe(3+) import. Responsible for energy coupling to the transport system (Probable).
Belongs to the NmrA-type oxidoreductase family.
Belongs to the bile acid:sodium symporter (BASS) (TC 2.A.28) family.
Tetramer consisting of 2 isoforms Alpha (catalytic) and 2 isoforms Beta (function not known).
Although it shares some weak sequence similarity with the UPF0398 family, it is distinct form other members of the family.
Cells lacking this gene are unable to grow on minimal medium with L-lactate as the sole carbon source. Cells lacking the lutABC operon exhibit little or no defect in biofilm formation on MSgg medium, but form small colonies that almost completely lacked surface architecture when glycerol is replaced with L-lactate in the MSgg medium.
Is essential for L-lactate degradation and allows cells to grow with lactate as the sole carbon source. Has probably a role as an electron transporter during oxidation of L-lactate. May also allow cells to utilize an alternative carbon source during biofilm formation, since it contributes to the formation of architecturally complex communities when lactate is present.
Is involved in L-lactate degradation and allows cells to grow with lactate as the sole carbon source. Has probably a role as an electron transporter during oxidation of L-lactate.
Is under the dual control of the transcriptional repressors LutR and SinR, which allows the lutABC operon to be induced during both growth in liquid culture and biofilm formation. Is induced by L-lactate, which relieves LutR repression.
Could be member of the two-component regulatory system YclK/YclJ. Potentially phosphorylates YclJ.
Deletion of the ywqH-ywqI-ywqJ-ywqK-nfi operon has no visible growth phenotype, however it is out-competed by wild-type cells.
Essential for recycling GMP and indirectly, cGMP.
Component of the oligopeptide permease, a binding protein-dependent transport system. Necessary for genetic competence but not sporulation. Probably responsible for energy coupling to the transport system.
Belongs to the peptidase M28 family. M28B subfamily.
Catalyzes the hydrolysis of a range of N-terminal amino acids.
Belongs to the cation diffusion facilitator (CDF) transporter (TC 2.A.4) family.
Deletion of the gene has no significant effet. However, a mneP-mneS double mutant is manganese sensitive and accumulates high levels of intracellular manganese.
Secondary manganese efflux system. May prevent manganese intoxication.
Transcriptionally activated by MntR in response to manganese excess. Expressed at a basal level in the absence of MntR.
Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity).
Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen.
Belongs to the dethiobiotin synthetase family.
Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
Belongs to the succinate/malate CoA ligase alpha subunit family.
Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.
Probably part of the ABC transporter complex YxeMNO that could be involved in amino-acid import. May transport S-methylcysteine. Responsible for energy coupling to the transport system (Probable).
The complex is composed of two ATP-binding proteins (YxeO), two transmembrane proteins (YxeN) and a solute-binding protein (YxeM).
Belongs to the thioesterase PaaI family.
Belongs to the metallo-dependent hydrolases superfamily. Uronate isomerase family.
Involved in the biosynthesis of kanosamine (3-amino-3-deoxy-D-glucose), which is known to have antibiotic and antifungal properties, and to be a precursor of the antibiotic neotrehalosadiamine (3,3'-diamino-3,3'-dideoxy-alpha,beta-trehalose (NTD)). Catalyzes the reversible pyridoxal phosphate-dependent transamination of 3-dehydro-alpha-D-glucose 6-phosphate to form alpha-D-kanosamine-6-phosphate. It can only use alpha-anomer and glutamate is the only amino donor.
Belongs to the site-specific recombinase resolvase family.
A hairpin loop (about residues 4-24) tethers the protein in the inner membrane. The isolated PHB domain (also called SPFH) oligomerizes, but does not bind lipids (PubMed:25635948). The C-terminal 24 residues are not required for correct localization, but the last 300 residues are required (PubMed:22753055). The C-terminus determines the oligomerization state of the protein; there are few large foci for FloT. Swapping with the C-terminus of FloA leads to many smaller foci (PubMed:25909364).
Belongs to the band 7/mec-2 family. Flotillin subfamily.
Delay in sporulation onset, 65% reduction in sporulation efficiency (PubMed:19383680, PubMed:22882210). No effect on KinC activity, a double floT-floA deletion decreases the number of proteins in the DRM, blocks the ability of KinC to stimulate biofilm formation (PubMed:20713508). Single floT deletion has defective motility, loss of NfeD2 localization, no change in FloA localization. Double floA-floT mutants have marked defects in cell morphology, motility, and transformation efficiency (PubMed:22753055). Double floA-floT deletion makes no biofilm, has greatly reduced FtsH, sporulates less than either single mutant (PubMed:22882210). Double dynA-floT deletions are highly elongated, filamentous and have strong defects in cell shape; cells grow very slowly with an extended lag phase (PubMed:23249255). Single mutation has a decrease in membrane fluidity and 35% decrease in protein secretion, a double floT-floA deletion has a stronger decrease in membrane fluidity and the same decrease in protein secretion (PubMed:23651456). Double dynA-floT deletion strains are less motile than single floT deletions (PubMed:26842743). Double floA-floT deletion has reduced oligomerization of KinC (PubMed:26297017). Double floA-floT deletion cells are somewhat elongated, the site of cell wall synthesis is affected, increasing at division septa. The speed of MreB movement around the cell is significantly decreased in rich medium in the floA-floT mutant (PubMed:32662773).
Found in functional membrane microdomains (FMM) that may be equivalent to eukaryotic membrane rafts. FMMs are highly dynamic and increase in number as cells age. FloA and FloT function is partially redundant; double deletions have marked synthetic phenotypes (PubMed:20713508, PubMed:22753055, PubMed:25909364, PubMed:27362352). Flotillins are thought to be important factors in membrane fluidity, especially during periods of rapid growth in rich media (Probable). Whether specific proteins are associated with FMMs is controversial; in one study FloT rafts have been shown to include proteins involved in adaptation to stationary phase, while FloA-FloT rafts include proteins involved in differentiation including sporulation, biofilm formation and DNA uptake competence. Another (more finely resolved) study only showed association of NfeD2 with FloT rafts of all the proteins examined (PubMed:25909364, PubMed:27362352). Aids homooligomerization of KinC and KinD but not KinB, may prevent incorrect hetero-association of the above kinases (PubMed:26297017). Simultaneous overexpression of both FloA and FloT leads to defects in cell division and differentiation, in part caused by stabilization of FtsH and its subsequent increased ability to degrade proteins. Cells make more biofilm, are about half as long, have less EzrA and more frequent Z-rings (PubMed:24222488). Involved in spatial organization of membranes, perhaps recruiting proteins (e.g. NfeD2) to specific membrane regions (Probable) (PubMed:23651456). Plays a role in phosphorylation of master regulator Spo0A, an early sporulation event (PubMed:19383680). Plays a non-redundant role with dynamin-like protein A (dynA) in membrane dynamics and cell shape (PubMed:23249255).
Homooligomerizes (PubMed:25909364). Oligomerizes in very large complexes in vitro. Interacts with FloA, FtsH, FtsX, OppA, SdhA and SecY in detergent-resistant membrane (DRM) fractions (PubMed:23651456). Interacts with FtsH at midcell (Probable). Interacts with FloA (PubMed:25909364). Interacts in vivo with KinC, FloA, FtsH and ResE (PubMed:26297017). Interacts with ResE, colocalizes with ResE in FloT-only membrane rafts (PubMed:25909364). Another study shows nearly complete colocalization with NfeD2, but only minor colocalization with FtsH or KinC (PubMed:27362352).
Transcription starts during stationary phase. Few foci are seen in exponential phase cells; the number of foci increases as cells enter stationary phase (at protein level) (PubMed:19383680, PubMed:23651456, PubMed:22753055). Few foci are seen on rich media, when cells are grown in minimal medium more foci are seen (at protein level) (PubMed:22753055). Expressed at low levels in rich media during exponential growth, more highly expressed in stationary phase on sporulation/biofilm-inducing media, activated by spo0A probably via AbrB (at protein level). Surfactin induces expression via spo0A (PubMed:25909364).
Allows enhanced growth with L-aspartate as a sole source nitrogen source.
Belongs to the amino acid-polyamine-organocation (APC) superfamily. AGT (TC 2.A.3.11) family.
Inhibited by carbonyl cyanide m-chlorophenylhydrazone and carbonyl cyanide 4-trifluoro-methoxyphenylhydrazone.
Uptake of L-aspartate with the concomitant import of a proton. Can also transport aspartate hydroxamate and L-glutamate with lower affinity and efficiency.
To E.coli YfcC and H.influenzae HI_0594.
Belongs to the bacterial sortase family. Class D subfamily.
Mutant releases elevated levels of the sortase substrate YfkN into the culture medium upon phosphate starvation (PubMed:21800427). Inactivation of the gene abolishes the cell wall anchoring of a fusion protein composed of a beta-lactamase reporter and the C-terminal region of the sortase substrate YhcR (PubMed:22020651).
Transpeptidase that anchors surface proteins to the cell wall (PubMed:21906378, PubMed:21800427, PubMed:22020651). Recognizes and modifies its substrate by proteolytic cleavage of a C-terminal sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the sortase and its substrate, which is then transferred and covalently attached to the cell wall (Probable). This sortase recognizes a Leu-Pro-Asp-Thr-Ser/Ala (LPDTS/A) motif (PubMed:21906378, PubMed:22020651). It has two substrates, YhcR and YfkN (PubMed:21906378, PubMed:21800427, PubMed:22020651).
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.
Belongs to the CPA3 antiporters (TC 2.A.63) subunit G family.
May enhance MrpA stability, assembly, or function. May play chaperone or assembly roles for MrpA and perhaps for other mrp proteins.
Induced by several classes of structurally unrelated antibiotics, such as erythromycin, fusidic acid or linezolid.
Involved in the transport of four structurally unrelated drugs, including doxorubicin and mitoxantrone. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Overexpression reduces the sporulation efficiency possibly by modulating the function of KinA.
Cells lacking this gene have no visible phenotype in response to salt, ethanol or energy stress. However cells with multiple disruptions (RsbRA, RsbRB, RsbRC and RsbRD) have an increased basal level of sigma-B, indicating this protein is a negative regulator of sigma-B.
Probably present in the stressosome with RsbRA, RsbRB, RsbRD and RsbS.
Belongs to the universal ribosomal protein uS4 family.
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit.
Part of the 30S ribosomal subunit (PubMed:30126986). Contacts protein S5. The interaction surface between S4 and S5 is involved in control of translational fidelity.
Part of the 30S ribosomal subunit. Contacts protein S5. The interaction surface between S4 and S5 is involved in control of translational fidelity.
S4 represses its own expression; it is not know if this is at the level of translation or of mRNA stability.
With S5 and S12 plays an important role in translational accuracy.
With S5 and S12 plays an important role in translational accuracy; many suppressors of streptomycin-dependent mutants of protein S12 are found in this protein, some but not all of which decrease translational accuracy (ram, ribosomal ambiguity mutations).
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.
Homodimer (By similarity). Interacts with WalK and YycI.
No cellular levels increase of either WalK or WalR. Induction of WalR-dependent gene expression. Cell wall defect.
The transmembrane region is required for the regulation of WalK activity.
Together with YycI, regulates the activity of the two-component system WalR/WalK.
Part of a binding-protein-dependent transport system for aliphatic sulfonates. Probably responsible for the translocation of the substrate across the membrane.
Catalyzes the NAD(P)(+)-dependent oxidation of alpha-ketoglutaric semialdehyde (alphaKGSA) to alpha-ketoglutarate. Prefers NADP(+) to NAD(+) as a cosubstrate. In vitro, can also use various aldehydes.
Binds 2 divalent metal cations per subunit (By similarity). Is most efficient with Zn(2+) and Co(2+), has only a small activity with Ni(2+) and Mn(2+) and no activity with Mg(2+), Fe(3+), and Fe(2+) (PubMed:35584544).
Involved in a cysteine salvage pathway from S-alkylcysteine. Catalyzes the last step in this pathway, i.e. the deacetylation of N-acetyl-L-cysteine. This pathway is likely important in the catabolism of alkylated cysteine generated by proteolysis of alkylated glutathione formed in the detoxification of a wide range of electrophiles.
Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits) (Probable). Required for vegetative growth (Probable). Has a partially redundant function with PBP-2A (pbpA) during spore outgrowth (PubMed:9851991).
Cells require increased levels of Mg(2+) or Ca(2+) for growth and germination. Approximately 50% of cells without the gene contain abnormal FtsZ rings, suggesting it is involved in septum synthesis; increased levels of Mg(2+) or Ca(2+) only partially eliminate the septation defects (PubMed:9721295). Double ponA-pbpA deletions spores have greatly decreased viability, peptidoglycan synthesis and elongate poorly; increased levels of Mg(2+) increase spore viability (PubMed:9851991).
Expression is constant during growth, decreases during sporulation and is induced approximately 15 min into spore germination. Present in the inner forespore membrane of the dormant spore (PubMed:3080407).
The product expressed from the translation of the ponA gene appears as two bands on a gel (1A and 1B), but the specific amino acid sequence of each protein is unknown.
A double cshB-cspB disruption mutant cannot be made.
Binds to the pentamer sequences ATTGG and CCAAT with highest affinity in single-stranded DNA, and also to other sequences. Has greater affinity for ATTGG than CCAAT. Can act as transcriptional activator of cold shock genes by recognizing putative ATTGG-box elements present in promoter regions of genes induced under cold shock conditions.
Homodimer. Interacts with RNA helicase CshB when cells are transcriptionally active.
Catalyzes the conversion of urocanate to 4-imidazolone-5-propionate.
Dispensable for transformability. Not known if it can act as a pyrroline-5-carboxylate reductase.
Belongs to the cytidylyltransferase family.
Catalyzes the transfer of the cytidylyl group of CTP to sn-glycerol 3-phosphate so the activated glycerol 3-phosphate can be used for teichoic acid synthesis, via incorporation into both the linkage unit and the teichoic acid polymer by TagB and TagF.
Inhibited by the divalent cations cadmium, mercury, tin, copper and zinc.
Proceeds via a random order reaction mechanism where there is negative cooperativity in the binding of substrates but not in catalysis.
Belongs to the glycosyl hydrolase 5 (cellulase A) family.
An RNase that has 5'-3' exonuclease and possibly endonuclease activity. Involved in maturation of rRNA and in some organisms also mRNA maturation and/or decay.
Belongs to the metallo-beta-lactamase superfamily. RNA-metabolizing metallo-beta-lactamase-like family. Bacterial RNase J subfamily.
Binds 1 zinc ion per subunit. The inability to bind a second zinc ion may explain its very poor exonuclease activity (PubMed:21893285).
Binds 2 Zn(2+) ions per subunit. It is not clear if Zn(2+) or Mg(2+) is physiologically important.
Endonucleolytically cleaves the 5'-leader sequence of certain mRNAs. Endonuclease digestion by the RNase J1/J2 complex occurs at a different site and in some cases more efficiently than J1 or J2 alone. The exonuclease activity of the J1/J2 complex is highly processive on substrates longer than 5 nucleotides, on shorter substrates is distributive. Plays a role in mRNA maturation and stability. Appears to have a limited effect on 16S rRNA maturation, despite its similarity to RNase J1. This subunit alone has very poor 5'-3' exonuclease activity.
Homodimer, may be a subunit of the RNA degradosome.
Not essential. While depletion/deletion of RNase J1 or J2 has no large impact on global gene expression, a double mutant alters the expression of hundreds of genes (PubMed:18713320).
Present in about 3000 monomers per cell in mid-log phase.
Unclear whether it forms homodimers or belongs to a larger complex. According to (PubMed:20025672) probably does not form homodimers, while (PubMed:21893285) shows homodimer formation. Both reports show RNase J1 and J2 interaction, probably as a heterotetramer (PubMed:19193632) shows it is a component of a possible RNA degradosome complex composed of rny, rnjA, rnjB, pnp, pfkA and eno, while (PubMed:20025672) finds no evidence of an RNA degradosome complex.
Putative N-acetyltransferase. May act on ribosomal proteins (Potential).
Part of the ABC transporter complex FhuCBGD involved in iron(3+)-hydroxamate import. Binds the iron(3+)-hydroxamate complex and transfers it to the membrane-bound permease. Required for the transport of ferrichrome and coprogen.
Belongs to the vitamin-B12 independent methionine synthase family.
Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
In response to oxidative stress, Cys-719 can react with bacillithiol (BSH) to form mixed disulfides. S-bacillithiolation leads to loss of catalytic activity and methionine auxotrophy.
Member of the two-component regulatory system PhoP/PhoR involved in the alkaline phosphatase genes regulation. PhoR may function as a membrane-associated protein kinase that phosphorylates PhoP in response to environmental signals.
Oligomerizes, probably forms homodimers. Interacts with FloA, colocalizes with FloA-only membrane rafts. Oligomerization is assisted by FloA (PubMed:25909364). Another study shows only minor colocalization with FloA or FloT (PubMed:27362352).
Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Belongs to the Cu-Zn superoxide dismutase family.
Binds 1 zinc ion per homodimer. The zinc ion is bound between 2 subunits and mediates dimerization.
Monomer, and homodimer. Largely unstructured monomer in solution. Well-ordered homodimer in the crystal.
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
YlmH and DivIVA are functionally unrelated.
Belongs to the glycosyl hydrolase 51 family.
Cells lacking this gene retain 38% of arabinofuranosidase activity, and the double mutant abfA/abf2 is inactive.
Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the cleavage of terminal alpha-(1->5)-arabinofuranosyl bonds in different hemicellulosic homopolysaccharides (branched and debranched arabinans). It acts preferentially on arabinotriose, arabinobiose and linear alpha-(1->5)-L-arabinan, and is much less effective on branched sugar beet arabinan.
Transcription is repressed by glucose and by the binding of AraR to the operon promoter. L-arabinose acts as an inducer by inhibiting the binding of AraR to the DNA, thus allowing expression of the gene (Probable).
When combined with a yraA disruption shows significantly reduced growth in the presence of formaldehye and methylglyoxal.
Might be involved in the translocation of teichuronic acid repeating units from the inner to the outer surface of the membrane.
Involved in the regulation of spore formation. Directs the transcription of several genes that encode structural components of the protein coat that encases the mature spore (CotB, CotC, CotG, CotS, CotV, CotW, CotX, CotY and CotZ). Controls also the cgeAB and cgeCDE operons.
Belongs to the radical SAM superfamily. RlmN family.
Reaction proceeds by a ping-pong mechanism involving intermediate methylation of a conserved cysteine residue.
Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
Cells lacking this gene sporulate normally in spo0F mutants.
Oligomerizes, probably forms homodimers; oligomerization is assisted by FloT. Interacts with FloT.
Phosphorylates the sporulation-regulatory protein spo0F and, to a minor extent, is responsible for heterogeneous expression of spo0A during logarithmical growth. Also phosphorylates spo0A under biofilm growth conditions.
Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine, 3-methylguanine, 7-methylguanine, O2-methylthymine, and O2-methylcytosine from the damaged DNA polymer formed by alkylation lesions.
Belongs to the HPF/YfiA ribosome-associated protein family. Long HPF subfamily.
Expressed under the dual control of sigma-B (PubMed:9296790) and sigma-H factors (PubMed:9296790, PubMed:9852014). The sigma-B-dependent promoter drives expression of yvyD under stress conditions and after glucose starvation, whereas a sigma-H-dependent promoter is responsible for yvyD transcription following amino acid depletion (PubMed:9852014). Also claimed to be under sole control of sigma-H (PubMed:22950019).
Interacts with 100S ribosomes. Not associated with 70S ribosome monomers, about 1 monomer per ribosome (PubMed:22950019).
Required for dimerization of active 70S ribosomes into 100S ribosomes in stationary phase; 100S ribosomes are translationally inactive and sometimes present during exponential growth.
Required for dimerization of active 70S ribosomes into 100S ribosomes in stationary phase; 100S ribosomes are translationally inactive and sometimes present during exponential growth. May not be the only factor implicated (PubMed:22950019). Might negatively regulate the activity of the sigma-54 factor (SigL) (PubMed:9852014).
The expression of a sigL-dependent gene (levD) is up-regulated two-fold in cells lacking yvyD, but the relative amount of the sigL transcript is not increased (PubMed:9852014). In cells overexpressing ppGpp synthase YwaC, deletion of this gene causes loss of 100S ribosome formation by dimerizing 70S ribosomes (PubMed:22950019).
Expressed during sporulation, and this requires the RNA polymerase sigma factor SigK.
Cells lacking this gene display release of repression of protease synthesis and sporulation in glucose-enriched medium.
Involved in the protection against polyamine toxicity by regulating their concentration. Could also be involved in the negative control of sporulation as well as production of degradative enzymes such as alpha-amylase, levansucrase and alkaline phosphatase. Catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to an acceptor substrate and releases both CoA and the acetylated product. It possesses N1-acetyltransferase activity toward polyamine substrates including spermidine, spermine, aminopropylcadaverine, norspermidine, homospermidine, N(8)-acetylspermidine, diaminopropane and agmatine.
Belongs to the transaldolase family. Type 3B subfamily.
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. Does not show fructose-6-P aldolase activity.
Impaired growth on arginine as the nitrogen source.
Part of a binding-protein-dependent transport system for arginine. Probably responsible for energy coupling to the transport system.
Expressed only in the forespore compartment of sporulating cells. Disappears after 45 minutes of spore germination. Expression is sigma F and sigma G-dependent.
Cells lacking this gene exhibit a lack of cytochromes c but normal contents of cytochrome a and b. Can sporulate.
Required for the biogenesis of c-type cytochromes.
Cells exhibit poorly methylated receptors, are tumbly and have a decreased sensitivity to attractants.
Deamidates 'Gln-593' and 'Gln-594' of the chemoreceptor McpA. In addition, deamidates other chemoreceptors, including McpB and McpC. CheD-mediated MCP (methyl-accepting chemotaxis proteins) deamidation is required for productive communication of the conformational signals of the chemoreceptors to the CheA kinase. CheD is absolutely required for a behavioral response mediated by McpC but is not required for the response to asparagine mediated by McpB. CheD is necessary for the generation of wild-type prestimulus CheA autophosphorylation levels. Also required for methylation of MCPs by CheR. In addition, enhances the activity of CheC 5-fold in vitro.
Deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs). CheD-mediated MCP deamidation is required for productive communication of the conformational signals of the chemoreceptors to the cheA kinase.
Catalyzes the dehydration of D-altronate.
Last gene in the exu locus which is required for galacturonate utilization.
Belongs to the phosphate acetyltransferase and butyryltransferase family.
Binds cyclic di-AMP (c-di-AMP), which may regulate the transporter activity.
Involved in a high affinity multicomponent binding-protein-dependent transport system for glycine betaine, carnitine and choline; probably responsible for energy coupling to the transport system.
Catalysis proceeds by a classical ping-pong bi-bi reaction mechanism.
Inhibited by deoxyguanosine at concentrations above 30 uM only with UTP as phosphate donor. dGTP is a potent competitive inhibitor.
Plays an essential role in generating the deoxyribonucleotide precursors dGTP for DNA metabolism. Highly specific toward deoxyguanosine (dGuo) and deoxyinosine (dIno). Only marginal activity is observed with guanosine. UTP is slightly more efficient as phosphate donor than CTP, ATP and GTP.
Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.
Digests double-stranded RNA. Involved in the processing of ribosomal RNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Also processes pre-scRNA (the precursor of the signal recognition particle RNA). Probably also processes some mRNAs, and tRNAs when they are encoded in the rRNA operon (PubMed:22229825, PubMed:26940229, PubMed:11123676, PubMed:17576666, PubMed:18363798, PubMed:22412379). Probably processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism (Probable). Involved in degradation of type I toxin-antitoxin system duplex RNAs (PubMed:22229825, PubMed:26940229).
Essential. Depletion leads to the accumulation of 30S precursor rRNA (PubMed:11123676), and alteration of levels of about 11% of total transcripts (PubMed:22412379, PubMed:11123676, PubMed:18363798). Increased half-life of type I toxin-antitoxin system RNAs of BsrG/SR4 and toxin BsrE mRNA (note these strains must have an essential second-site suppressor to survive) (PubMed:22229825, PubMed:26940229).
According to PubMed:12779331, the mutation G152A reduces the kinase activity about twofold and has little effect on phosphorylase activity, whereas according to PubMed:12055300, it completely prevents both functions. This conflicting result may be explained by limiting amounts substrates conditions used in PubMed:12779331 assays.
Both phosphorylation and phosphorolysis are carried out by the same active site and suggest a common mechanism for both reactions.
Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of 'Ser-45' in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr). The two antagonistic activities of HprK/P are regulated by several intracellular metabolites, which change their concentration in response to the absence or presence of rapidly metabolisable carbon sources (glucose, fructose, etc.) in the growth medium. Also phosphorylates/dephosphorylates the HPr-like catabolite repression protein crh on 'Ser-46'. Therefore, by controlling the phosphorylation state of HPr and crh, HPrK/P is a sensor enzyme that plays a major role in the regulation of carbon metabolism and sugar transport: it mediates carbon catabolite repression (CCR), and regulates PTS-catalyzed carbohydrate uptake and inducer exclusion.
Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr). The two antagonistic activities of HprK/P are regulated by several intracellular metabolites, which change their concentration in response to the absence or presence of rapidly metabolisable carbon sources (glucose, fructose, etc.) in the growth medium. Also phosphorylates/dephosphorylates the HPr-like catabolite repression protein crh on a specific serine residue. Therefore, by controlling the phosphorylation state of HPr and crh, HPrK/P is a sensor enzyme that plays a major role in the regulation of carbon metabolism and sugar transport: it mediates carbon catabolite repression (CCR), and regulates PTS-catalyzed carbohydrate uptake and inducer exclusion.
Constitutively expressed, with or without glucose in the growth medium.
Is active as a kinase only at high ATP concentrations or at low ATP concentrations in the presence of the allosteric activator fructose 1,6-bisphosphate (FBP). The pyrophosphate-dependent HPr phosphorylation is not stimulated by FBP. Kinase activity is inhibited by inorganic phosphate (Pi). Dephosphorylation of HPr(Ser-P) by B.subtilis HPrK/P becomes prevalent when the concentration of Pi increases. Thus, the kinase activity may prevail under conditions of good nutrient supply, whereas the phosphorylase activity is dominant if carbon and energy sources become limiting.
The Walker A ATP-binding motif also binds Pi and PPi.
The enzyme may harbor two different cation-binding sites, one that interacts specifically with the nucleotide, and the other that is involved in the binding of the protein substrate.
Was originally called HPr kinase/phosphatase, but P-Ser-HPr dephosphorylation was found to follow a quite unique mechanism (PubMed:12359880), in which Pi instead of H(2)O is used for the nucleophilic attack on the phosphoryl group. P-Ser-HPr dephosphorylation is therefore not a phosphohydrolysis but a phospho-phosphorolysis reaction, and the bifunctional enzyme was dubbed HPr kinase/phosphorylase.
Endoribonuclease that initiates mRNA decay.
Endoribonuclease that initiates mRNA decay. Initiates the decay of all SAM-dependent riboswitches, such as yitJ riboswitch. Involved in processing of the gapA operon mRNA, it cleaves between cggR and gapA (PubMed:19193632). Is also the decay-initiating endonuclease for rpsO mRNA. Involved in degradation of type I toxin-antitoxin system bsrG/SR4 RNAs and a minor role in degradation of type I toxin-antitoxin system bsrE/SR5 degradation (PubMed:22229825, PubMed:26940229).
Essential; depletion mutants show a significant increase in global mRNA half-life (PubMed:19779461) a decrease in at least 1 specific mRNA processing event (PubMed:19193632); in a more severe depletion experiment alteration of about 26% of transcripts was seen (PubMed:22412379). Later shown not to be essential in 4 strains, with a doubled doubling time, cells are translucent, suggesting a possible cell surface defect. 168 trpC2 cells able to grow on minimal medium. Loss of competence for plasmid transformation, 1000-fold less sporulation. Increased sensitivity to a wide range of antibiotics. Thinner cells form long curved structures of 2-3 cell lengths, cell walls are altered with looser, considerably less dense peptidoglycan. Double pnp-rny mutants grow very slowly, while rnjA-rny mutants could not be isolated (PubMed:23504012). Increased half-life of type I toxin-antitoxin system RNAs of BsrG/SR4 (PubMed:22229825).
Has 5 domains: N-terminal transmembrane, coiled-coil, KH, HD and an unnamed conserved C-terminal domain (residues 430-520). Both the N-terminal transmembrane helix and C-terminal domain are required for protein function in vivo.
Homodimer (Probable). Component of a possible RNA degradosome complex composed of rny, rnjA, rnjB, pnp, pfkA and eno (PubMed:19193632) (although rnjA and rnjB's presence is unclear). Interacts with RNA helicase CshA which may also be a member of the RNA degradosome complex (PubMed:20572937). Interacts with full-length dynamin-like protein DynA (PubMed:23060960).
Magnesium. Can also use manganese or zinc.
Shows preference for transcripts carrying a monophosphate group at the 5' end.
Component of the flagellar switch. Binds CheY-P and increases its hydrolysis rate in vitro. May function constitutively to remove CheY-P around the flagellar switch to maintain an optimal level of CheY-P whereas CheC may function after addition of an attractant to cope with increased levels of CheY-P.
FliN is one of three proteins (FliG, FliN, FliM) that form the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation.
Induced by ethanol and the protonophore carbonylcyanide p-chlorophenylhydrazone (CCCP) and, more modestly, by sodium and potassium. Positively regulated by the two-component regulatory system NatK/NatR.
Part of an ABC transporter that catalyzes ATP-dependent electrogenic sodium extrusion.
The complex is composed of NatA and NatB.
Could not restore staphylococcal growth after ltaS depletion.
Proteolytically cleaved by the type I signal peptidases SipT and SipV.
The cotJ operon proteins affect spore coat composition. They are either required for the normal formation of the inner layers of the coat or are themselves structural components of the coat.
Belongs to the DNA glycosylase MPG family.
Belongs to the 4-hydroxybenzoyl-CoA thioesterase family.
Belongs to the glycosyl hydrolase 68 family.
Belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family.
Catalyzes the dehydrogenation of precorrin-2 to form sirohydrochlorin which is used as a precursor in both siroheme biosynthesis and in the anaerobic branch of adenosylcobalamin biosynthesis.
Cells lacking this gene are unable to grow on minimal medium with nitrate as nitrogen source. Growth is restored only after addition of both cysteine and ammonia to the medium.
By Spo0A during nutrient starvation (PubMed:12817086). Repressed by AbrB during regular growth when nutrients are plentiful, in association with the transcriptional repressor Abh.
Required for the maturation of SdpC to SDP (PubMed:12817086). Not required for SdpC signal peptide cleavage, secretion from the cell or disulfide bond formation (PubMed:23687264).
When the sdpA-sdpB-sdpC operon is deleted, increased rate of spore formation; a double operon deletion (sdpA-sdpC plus skfA-skfH) makes spores even faster (PubMed:12817086). A single deletion mutant does not have SDP activity (active peptide of sdpC) (PubMed:23687264).
Functions as a (p)ppGpp synthase; GDP can be used instead of GTP, resulting in an increase of (p)ppGpp synthesis (PubMed:18067544). Overexpression in relA mutants (triple relA-yjbM-ywaC deletions and single relA deletions) leads to growth arrest; GTP levels fall drastically, various guanine-related nucleotides are synthesized (ppGp or pGpp), the cellular transcriptional profile changes dramatically and 70S ribosome dimerization occurs (PubMed:22950019). Overexpression in the presence of a wild-type relA gene does not have these effects (PubMed:22950019). In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. activities in response to changes in nutritional abundance. YwaC has probably a minor role in stringent response (PubMed:18067544).
No visible phenotype, double yjbM-ywaC and triple relA-yjbM-ywaC mutants are also viable (PubMed:18067544).
The synthase activity of YwaC is weaker than that of YjbM (PubMed:18067544).
Weakly expressed during exponential growth with a marked and transient increase at the onset of the stationary phase (PubMed:18067544). Protein expression is very low during the first 3.5 hours after inoculation (at protein level) (PubMed:22950019). Induced by alkaline shock (PubMed:18067544).
Involved in a multicomponent binding-protein-dependent transport system for glycine betaine; probably responsible for the translocation of the substrate across the membrane.
Homodecamer. A 20 Angstroms wide channel runs through the complex, giving access to a central chamber holding the active sites.
Hydrolyzes N-terminal residues in D-amino acid containing peptides. Among the tested substrates, the highest activities are with D-Ala-D-Ala and D-Ala-Gly-Gly. The physiological role is not clear.
A non-essential component of RNA polymerase (RNAP) (PubMed:6802805, PubMed:18289874, PubMed:21710567, PubMed:25092033). Has a similar structure to bacteriophage T7 protein Gp2 (AC P03704), which is known to bind to RNAP in the DNA binding-cleft. Unlike Gp2 however, this protein does not inhibit transcription initiation (PubMed:25092033). In vitro reconstitution experiments show this subunit is dispensible (PubMed:18289874).
A non-essential component of RNA polymerase (RNAP).
Belongs to the RNA polymerase subunit epsilon family.
Monomer (By similarity). RNAP is composed of a core of 2 alpha, a beta and a beta' subunit. The core is associated with a delta subunit, and at least one of epsilon or omega (PubMed:6802805, PubMed:18289874, PubMed:21710567, PubMed:25092033). When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription (PubMed:18289874).
No visible phenotype; growth, bacterial fitness in competition experiments, RNAP distribution, global transcript levels and transcription initiation in vitro are all unaffected.
Part of the rpoY-rnjA operon, transcribed constitutively.
RNAP is composed of a core of 2 alpha, a beta and a beta' subunit. The core is associated with a delta subunit, and at least one of epsilon or omega. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription.
Belongs to the major facilitator superfamily. Cyanate porter (TC 2.A.1.17) family.
Belongs to the cytochrome c oxidase subunit 3 family.
Belongs to the DNA repair enzymes AP/ExoA family.
Probably binds two magnesium or manganese ions per subunit.
Might take part in the signal recognition particle (SRP) pathway. This is inferred from the conservation of its genetic proximity to ftsY/ffh. May be a regulatory protein.
Seems to be involved in the degradation of glucomannan.
Belongs to the heat shock protein 70 family.
Member of the two-component regulatory system YdfH/YdfI. Regulates the transcription of ydfJ by binding to its promoter region.
Belongs to the NAD(P)H dehydrogenase (quinone) family.
Belongs to the glycosyl hydrolase 11 (cellulase G) family.
Belongs to the CPA3 antiporters (TC 2.A.63) subunit E family.
An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
The PRC barrel domain binds ribosomal protein uS19.
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane.
Belongs to the FPP/GGPP synthase family.
Cells lacking this gene show an accumulation of dihydroanticapsin and dihydrobacilysin.
Part of the bacABCDEFG operon responsible for the biosynthesis of bacilysin, an irreversible inactivator of the glutaminase domain of glucosamine synthetase. Catalyzes the dehydrogenation of the C7-hydroxyl group in the 4S-tetrahydrotyrosine (4S-H4Tyr) to yield anticapsin (epoxycyclohexanonyl-Ala). It is not able to oxidize the 4R-H4Tyr diastereomer and the dihydrobacilysin dipeptide (L-Ala-4S-H4Tyr dipeptide).
Belongs to the NADH:flavin oxidoreductase/NADH oxidase family.
Belongs to the sodium:citrate (SCF) symporter family.
Proton motive force-driven secondary transporter that catalyzes the uptake of both citrate and malate. Appears to be an electroneutral proton-solute symporter; the number of protons transported is equal to the valence of the transported anions. Is strictly stereoselective, translocating only the (S)-enantiomer of malate.
The uptake activity is inhibited by divalent metal ions such as Ca(2+), Mg(2+) and Ni(2+).
Cleaved by RasP. Cleavage is important for turnover and function of FtsL.
Essential cell division protein that may play a structural role. Probably involved in the regulation of the timing of cell division. Also required for sporulation.
Is thermodynamically highly unstable and is likely to be rapidly degraded unless stabilized by interaction with other septasomal proteins.
Monomer. Interacts with DivIB and DivIC. Interaction with DivIC stabilizes FtsL against RasP cleavage.
The cytoplasmic region is involved in protein stability.
The question of whether FtsL and DivIC interact directly (PubMed:16936019) or indirectly (PubMed:11994149) remains controversial.
Specifically inhibits the KinA pathway to sporulation.
Member of the two-component regulatory system YbdK/YbdJ. Probably activates YbdJ by phosphorylation.
Generates the two 5 and 8 kDa components of the spore coat, after proteolytic processing.
Catalyzes the proton-dependent uptake of 2-keto-3-deoxygluconate (KDG) into the cell.
Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Probably responsible for the translocation of the substrate across the membrane.
Part of the ABC transporter complex involved in maltodextrin import. Probably responsible for the translocation of the substrate across the membrane (Probable).
Belongs to the glycosyltransferase 4 family. MraY subfamily.
Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-dependent O-methyltransferase family.
Binds magnesium, but the ion is dispensable for mo5U forming activity.
Catalyzes the methylation of 5-hydroxyuridine (ho5U) to form 5-methoxyuridine (mo5U) at position 34 in tRNAs.
Destabilization of ComGA (PubMed:17630974).
Involved in transformation (competence for DNA uptake). Required for DNA uptake but not for binding. May provide the driving force for transport of DNA through an aqueous channel.
Catalyzes an amino-pyrimidine hydrolysis reaction at the C5' of the pyrimidine moiety of thiamine compounds, a reaction that is part of a thiamine salvage pathway.
Catalyzes an amino-pyrimidine hydrolysis reaction at the C5' of the pyrimidine moiety of thiamine compounds, a reaction that is part of a thiamine salvage pathway. Thus, catalyzes the conversion of 4-amino-5-aminomethyl-2-methylpyrimidine to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP). To a lesser extent, is also able to catalyze the hydrolytic cleavage of thiamine; however, this thiaminase activity is unlikely to be physiologically relevant. Therefore, is involved in the regeneration of the thiamine pyrimidine from thiamine degraded products present in the environment, rather than in thiamine degradation.
Inactivation of this gene causes a delay in sporulation, but does not affect cell growth and the production of extracellular enzymes (PubMed:1898926). The deletion mutant does not require a hydroxypyrimidine source as it is able to biosynthesize it using ThiA; the tenA/thiA double mutant, however, is hydroxypyrimidine-requiring and is unable to salvage the pyrimidine from formylaminopyrimidine, aminopyrimidine, or base-degraded thiamine (PubMed:17618314).
Was originally described as a regulatory protein involved in the regulation of the production of extracellular enzymes.
In the C-terminal section; belongs to the prokaryotic molybdopterin-containing oxidoreductase family.
Cells lacking this gene are viable, have no defect in growth, but produce fewer spores, slightly longer cells and show an increase in cell chain formation. Also exhibits some resistance to moenomycin (PubMed:19648239, PubMed:19666716). Mutants lacking both murJ and amj have a lethal defect in cell wall synthesis (PubMed:25918422).
Expressed at low levels during vegetative growth. Expression decreases significantly during sporulation.
Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane (PubMed:25918422). Not essential for growth (PubMed:19648239, PubMed:19666716).
All three domains (PPIase domain and the flanking N- and C-terminal domains) are essential for activity.
Essential protein that plays a major role in protein secretion by helping the post-translocational extracellular folding of several secreted proteins. Has PPIase activity but it is not essential for its function in vivo.
Plays a major role in protein secretion by helping the post-translocational extracellular folding of several secreted proteins.
Sequencing errors. The N-terminus of this sequence is probably the N-terminus of phrI.
Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
Deletion of the yobL-yobK operon has no visible growth phenotype, however it is out-competed by wild-type cells.
Immunity component of one of 6 LXG toxin-immunity modules in this strain. They promote kin selection, mediate competition in biofilms, and drive spatial segregation of different strains, indicating that LXG toxins may help avoid warfare between strains in biofilms. Mediates intercellular competition during biofilm formation; disruption of the operon disadvantages the bacteria, but overexpression of the cognate immunity protein restores growth in competition with wild-type. In situ neutralizes the toxic effect of cognate toxin YobL (PubMed:34280190). Neutralizes the toxic activity of cognate toxin YobL upon expression in E.coli. Does not have immunity protein activity on other LXG toxins (PubMed:22200572).
Interacts with cognate toxin YobL but not with non-cognate putative toxin YeeF. The interaction inhibits the toxic activity of YobL.
Member of the two-component regulatory system CssS/CssR required to control the cellular response to secretion stress. Required for the transcription of htrA. Could detect misfolded proteins at the membrane-cell wall interface and then activate CssR by phosphorylation.
Essential for the localization of CwlJ in the spore coat and for spore germination triggered by calcium and dipicolinic acid (DPA). Its assembly into the spore coat is dependent on the coat morphogenetic proteins CotE and SpoIVA.
Expressed during sporulation in mother cell compartment.
Multimer. Is cross-linked by Tgl and YabG into an insoluble high-molecular-mass complex that appears very late in sporulation.
Three N-terminal lysines form epsilon-(gamma-glutamyl)lysine isopeptide bonds with glutamines of other spore coat proteins.
Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Heterooligomer composed of large and small subunits.
Alpha-galacturonidase able to catalyze the hydrolysis of the chromogenic substrate p-nitrophenyl-alpha-D-galacturonic acid (pNPalphaGalUA), and of the probable natural substrate alpha-1,4-di-galacturonate (GalUA(2)). Can neither hydrolyze pNPbetaGalUA, nor the stereoisomeric pNPalphaGlcUA. Does not display alpha- or beta-glucosidase activity as it fails to hydrolyze melibiose, raffinose, lactose and the chromogenic analogs, pNPalphaGal and pNPbetaGal. Cannot use the following compounds as substrates: pNP-N-acetyl-alpha- and beta-D-galactosaminide, pNP-N-acetyl-alpha- and beta-D-glucosaminide, pNP-alpha-L- and beta-L-arabinopyranoside, pNP-alpha- and beta-D-glucuronide, pNP-alpha- and beta-D-glucopyranoside, pNP-alpha- and beta-D-glucopyranoside 6-phosphate, pNP-alpha-D-galactopyranoside 6-phosphate and oNP-beta-D-galactopyranoside 6-phosphate.
Binds 1 Mn(2+) ion per subunit. Although a Mg(2+) ion is seen in the structure, galacturonidase activity was shown using manganese (PubMed:23416295).
Belongs to the binding-protein-dependent transport system permease family. HisMQ subfamily.
Part of a binding-protein-dependent transport system for arginine. Probably responsible for the translocation of the substrate across the membrane.
Activity is inhibited by phenylmethylsulfonyl fluoride (PMSF), but not by EDTA.
Expression is negatively controlled by CodY, which binds to the regulatory regions of vpr, in the vicinity of its transcription start point (PubMed:25666135). Expression is sigma H-dependent (PubMed:25666135).
Mutant lacking this gene does not show significant decrease in CSF production, but the triple deletion mutant aprE-epr-vpr is defective in the cleavage event to release mature CSF.
Probably undergoes C-terminal processing or proteolysis (PubMed:1938892). Auto-processed to form active enzymes of several different molecular weights (PubMed:15596354).
Serine protease (PubMed:1938892, PubMed:17666034). Involved in the production of the competence and sporulation stimulating factor CSF (PubMed:17666034). Is directly involved in the processing of pro-CSF to CSF (PubMed:17666034). Can also cleave pro-PhrA to PhrA, but cannot cleave pro-PhrE (PubMed:17666034). Shows fibrinolytic activity in vitro (PubMed:15596354). Not essential for growth or sporulation (PubMed:1938892).
By glycerol 3-phosphate. Repressed by glucose, glucose 6-phosphate and fructose 6-phosphate.
Defective in glycerol 3-phosphate uptake. Noninducible for glpK and glpD. Is able to grow at concentrations of the antibiotic fosfomycin that is not tolerated by the wild-type.
Regulates expression of the glpD operon. In the presence of glycerol 3-phosphate (G3P) causes antitermination of transcription of glpD at the inverted repeat of the leader region to enhance its transcription. Binds and stabilizes glpD leader mRNA.
Regulates expression of the glpD operon. In the presence of glycerol 3-phosphate (G3P) causes antitermination of transcription of glpD at the inverted repeat of the leader region to enhance its transcription. Binds and stabilizes glpD leader mRNA. May also regulate expression of the glpFK operon.
Disruption of the gene prevents the development of competence as well as the transcription of comG, a late competence operon (PubMed:1715859). Disruption also decreases the expression of srfA, a regulatory operon needed for the expression of competence (PubMed:1715859).
Expression is maximal early in growth and declines as the cells approach the stationary phase.
Part of a major quorum-sensing system that regulates the development of genetic competence (PubMed:1715859, PubMed:11751817). Involved in the maturation of the competence pheromone ComX (PubMed:11751817, PubMed:31670609). Acts by catalyzing the transfer of a farnesyl group on the ComX pheromone (PubMed:31670609). Shows weak geranylation activity with geranyl diphosphate (GPP) (PubMed:31670609).
The DNA sequences encoding comQ, comX and the N-terminal two-thirds of comP show a striking polymorphism, which determines the specificity of the quorum-sensing system in the different pherotypes of Bacillus.
The EIIC type-3 domain forms the PTS system translocation channel and contains the specific substrate-binding site.
Cells lacking this gene are unable to grow in minimal medium with mannose as the sole carbon source. They show impaired growth in rich medium, and impairment increases in the presence of greater than 1.4 mM mannose.
Up-regulated by mannose. Is under the control of ManR. Is subject to carbon catabolite repression (CCR) by glucose. Forms part of an operon with manP and yjdF.
Part of the iron transporter system efeUOB/M involved in iron import (PubMed:16672620, PubMed:23764491). Specifically binds Fe(3+), which is produced by EfeB-mediated oxidation of Fe(2+), and delivers it to the cell membrane permease EfeU (PubMed:23764491).
Severe reduction in Fe(2+) and Fe(3+) uptake and in cell growth.
The peptidase M75 domain contains 2 metal binding sites, site III and site IV (By similarity). Lacks the N-terminal Cup-like domain present in EfeO proteins that contains metal binding sites I and II (By similarity).
This protein does not seem to be able to bind zinc, which all carbonic anhydrases are thought to require.
Belongs to the FHIPEP (flagella/HR/invasion proteins export pore) family.
Involved in the export of flagellum proteins.
Required for formation of the rod structure of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin.
Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P. Shows no activity with pyridoxal, pyridoxamine or pyridoxine.
Belongs to the IspD/TarI cytidylyltransferase family. IspD subfamily.
Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Activity is stimulated by high osmolarity.
Belongs to the BCCT transporter (TC 2.A.15) family.
High-affinity uptake of glycine betaine. Does not mediate either carnitine or choline uptake.
Expressed under the control of the sigma-W factor SigW.
Induced by galacturonate and negatively regulated by itself. Is subject to catabolite repression by glucose involving the ccpA gene.
Transcriptional repressor of the kdgRKAT and kduID operons for pectin utilization.
Contains an extended N-terminal domain, which probably binds RNA, connected by an interdomain linker to a C-terminal catalytic domain, which adopts a typical SPOUT fold.
Mutant strain lacks G2553 methylation in 23S rRNA (PubMed:35710145). Loss of the gene does not affect growth nor lead to ribosome assembly intermediates accumulation (PubMed:35710145).
Specifically methylates the ribose of guanosine 2553 (G2553) in 23S rRNA (PubMed:35710145). When the target G2553 is mutated, is able to methylate the ribose of adenosine, but it cannot methylate cytidine nor uridine (PubMed:35710145). Modifies free 23S rRNA but not the fully assembled ribosome nor the 50S subunit, suggesting that the modification occurs early during ribosome biogenesis (PubMed:35710145).
Catalyzes the conversion of L-asparagine to L-aspartate and ammonium.
Expression is induced during limiting-nitrogen conditions by the nitrogen regulatory factor TnrA.
Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Part of the ABC transporter complex MelEDC-MsmX involved in melibiose, raffinose and stachyose import. Probably responsible for the translocation of the substrate across the membrane.
Deletion of the yqcF-yqcG operon has no visible growth phenotype, however it is out-competed by wild-type cells.
Immunity component of one of 6 LXG toxin-immunity modules in this strain. They promote kin selection, mediate competition in biofilms, and drive spatial segregation of different strains, indicating that LXG toxins may help avoid warfare between strains in biofilms. Mediates intercellular competition during biofilm formation; disruption of the operon disadvantages the bacteria, but overexpression of the cognate immunity protein restores growth in competition with wild-type. In situ neutralizes the toxic effect of cognate toxin YqcG (PubMed:34280190). Neutralizes the toxic activity of cognate toxin YqcG upon expression in E.coli. Does not have immunity protein activity on other LXG toxins (PubMed:22200572).
Probably interacts with cognate toxin YqcG but not with other non-cognate toxins. The interaction inhibits the toxic activity of YqcG (Probable).
Belongs to the RNA polymerase beta' chain family.
ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Probably the major protease that degrades proteins tagged by trans-translation (PubMed:11395451).
ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.
Component of the ClpX-ClpP complex. Forms a hexameric ring that, in the presence of ATP, binds to fourteen ClpP subunits assembled into a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes.
No degradation of trans-translationally tagged-peptides.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIA subfamily.
Expressed from 4 hours and peaks at 9 hours after onset of sporulation.
Expressed under control of sigma-F (sigF).
Phosphorylated in a Ca(2+)-dependent manner starting 4 hours after shifting to sporulation medium.
Spores are less resistant to heat and germinate at a slower rate, Ca(2+)-dependent phosphorylation is no longer seen.
This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium.
A single subunit DNA-dependent RNA polymerase (RNAP) that catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates (rNTPs) as substrates. The enzyme is more highly processive than the multisubunit RNAP from E.coli but is considerably more error-prone. It has no detectable proof-reading function but can perform pyrophosphorolysis. Transcribes the late genes of the SPbeta prophage starting from yonK (approximately 35 genes are encoded in the prophage downstream from yonK).
Belongs to the YRH RNA polymerase family.
No expression under phage non-inducing conditions; induced by mitomycin C (at protein level).
Catalyzes the decarboxylation of malate to pyruvate (PubMed:12949160, PubMed:16788182). Can use NAD and NADP, but with a strong preference for NAD (PubMed:12949160, PubMed:16788182). Can also catalyze the decarboxylation of oxaloacetate (PubMed:16788182). Involved in keeping the ATP levels high (PubMed:23136871).
Induced in the presence of malate via the two-component system MalK/MalR. The regulator MalR binds to the promoter region of maeA. Is not subject to carbon catabolite repression.
Mutant can use malate, succinate plus glutamate or glucose as efficiently as the wild-type strain (PubMed:12949160, PubMed:16788182). The ATP concentrations in the mutant grown in minimal medium with glucose are similar to the wild-type level. ATP concentrations decrease by about 10% in malate minimal medium. The mleA-maeA-malS triple mutant shows a decrease in ATP concentrations by about 20% and a moderate growth defect (PubMed:23136871). NADPH overproduction is roughly halved in the deletion mutant (PubMed:33824210).
A translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability. Usually binds in the 5'-UTR at or near the Shine-Dalgarno sequence preventing ribosome-binding, thus repressing translation. Its main target seems to be the major flagellin gene, while its function is anatagonized by FliW.
A translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability. Usually binds in the 5'-UTR at or near the Shine-Dalgarno sequence preventing ribosome-binding, thus repressing translation. Represses expression of flagellin (hag) in a post-transcriptional fashion. Specifically binds to 2 sites in the 5'-UTR of hag mRNA in a cooperative fashion; the second site overlaps the Shine-Dalgarno sequence and prevents 30S ribosomal subunit binding (PubMed:17555441). Mutation of either binding site abolishes CsrA regulation of hag expression (PubMed:17555441, PubMed:21895793). Repression is greater in the 1A96 than 168 genetic background and higher in minimal than rich medium (PubMed:17555441). Translation repression is antagonized by FliW (PubMed:21895793). Partner switching by flagellin between FliW and CsrA provides a flagellar assembly checkpoint to tightly control the timing of flagellin synthesis. Flagellin binds to assembly factor FliW, freeing CsrA to repress translation of the flagellin mRNA. When the flagellar hook is assembled flagellin is secreted, depleting intracellular flagellin, which frees FliW to interact with CsrA and inhibits CsrA binding to mRNA. This derepresses flagellin translation and provides protein for flagellar assembly. Once the flagellar filament is completed cytoplasmic flagellin levels rise and CsrA translation repression of flagellin reinitiates (PubMed:21895793, PubMed:27516547). Overexpression leads to a dramatic reduction in motility, a significant reduction in flagellin synthesis and reduced flagella assembly (PubMed:21895793).
Contacts FliW via its C-terminus (residues 49-58).
Homodimer (PubMed:17555441). The beta-strands of each monomer intercalate to form a hydrophobic core while the alpha-helices form wings that extend away from the core (By similarity). Two molecules of FliW interact with 1 homodimer (PubMed:21895793, PubMed:27516547). mRNA and FliW bind to different sites on CsrA (PubMed:27516547).
Homodimer; the beta-strands of each monomer intercalate to form a hydrophobic core, while the alpha-helices form wings that extend away from the core.
Increased expression of flagellin (hag), 30% decrease in motility halo (PubMed:17555441). Suppresses the motility loss and flagellar assembly defect of an fliW deletion (PubMed:21895793). Suppresses the phenotypes associated with deletion of the intracellular flagella chaperone fliS (PubMed:23144244).
Part of the SigD-controlled yvyF-csrA operon and the SigA-controlled fliW-csrA operon (PubMed:17555441). Expressed from the SigA operon at low levels during log phase, with a 5-fold increase as the culture transitions to stationary phase, peaking 1 hour later.
Belongs to the bacterial ribosomal protein bL17 family.
Part of the 50S ribosomal subunit (PubMed:30126986). Contacts protein L32 (By similarity).
Part of the 50S ribosomal subunit. Contacts protein L32.
Belongs to the MsrB Met sulfoxide reductase family.
Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides (By similarity).
Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
Negative regulator of protease production and sporulation.
Negative regulator of protease production and sporulation. Acts by binding directly to the promoter of protease genes (aprE and nprE), and by repressing oligopeptide permease operons (appABCDF and oppABCDF), thereby preventing uptake of oligopeptides required for initiation of sporulation. Acts with SinR as a corepressor of epr expression. Binds to non-m6A-5-methylated 5'-GACGAG-3' sites, tested with scpA; when the target is methylated by DnmA, this repressor no longer binds and transcription is up-regulated (PubMed:32324221).
Negatively regulated by the Mrp homolog protein SalA and by SenS.
Essential for sporulation. Interferes with or is a negative regulator of the pathway leading to asymmetric septation.
Cells lacking this gene do not grow in presence of arginine as sole nitrogen source.
Not induced by arginine, repressed by RocR itself.
Positive regulator of arginine catabolism. Controls the transcription of the two operons rocABC and rocDEF and probably acts by binding to the corresponding upstream activating sequences.
An essential component of the DNA double-stranded break repair machinery, the heterodimer acts as both an ATP-dependent DNA helicase and an ATP-dependent, dual-direction single-stranded exonuclease. Recognizes the B.subtilis chi site (5'-AGCGG-3') which transforms the enzyme from a helicase which degrades both DNA strands to one with only 5' -> 3' exonuclease activity. This generates a double-stranded DNA with a protruding 3'-terminated single-stranded tail suitable for the initiation of homologous recombination (chi fragment). The AddA nuclease domain in particular is required for chi fragment generation; this subunit has 3' -> 5' nuclease and helicase activity. RecA thread formation during DNA double-strand break repair requires RecJ or AddAB.
At low magnesium concentrations there is no nuclease activity, but helicase activity is unaffected.
Belongs to the helicase family. AddA subfamily.
This enzyme is a functional homolog of the E.coli RecBCD enzyme; unlike the RecBCD enzyme it degrades both duplex strands symmetrically.
Part of the ABC transporter complex YclNOPQ involved in uptake of ferric-petrobactin. Petrobactin is a photoreactive 3,4-catecholate siderophore produced by many members of the B.cereus group, including B.anthracis. Probably responsible for the translocation of the substrate across the membrane.
The complex is composed of two ATP-binding proteins (YclP), two transmembrane proteins (YclN and YclO) and a solute-binding protein (YclQ).
Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family.
Cells lacking this gene cease to produce phospholipid and accumulate fatty acids arising from the dephosphorylation of 1-acylglycerol-3-P.
Converts lysophosphatidic acid (LPA) into phosphatidic acid (PA) by incorporating an acyl moiety at the 2 position. This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Uptake of allantoin into the cell (PubMed:11344136, PubMed:26967546). Allantoin uptake is not dependent on sodium, and PucI is likely to be a proton-coupled symporter (PubMed:26967546). Shows highest recognition for binding of allantoin, good recognition for binding of hydantoin, L-5-benzylhydantoin and 5-hydroxyhydantoin, and to a lesser extent for a range of nucleobases and nucleosides (PubMed:26967546).
Expressed in the mother cell compartment from T4 of sporulation.
Inactivation of the ykuD gene does not affect vegetative growth, spore resistance to heat, chloroform and lysozyme, or spore germination in the presence of L-alanine.
LysM domains are thought to be involved in peptidoglycan binding.
Probable enzyme that may play an important role in cell wall biology.
Regulated by SigK. Could also be negatively regulated by GerE. Transcribed by SigK RNA polymerase.
Disruption mutants are unable to use petrobactin for iron delivery and growth.
Part of the ABC transporter complex YclNOPQ involved in uptake of ferric-petrobactin. Petrobactin is a photoreactive 3,4-catecholate siderophore produced by many members of the B.cereus group, including B.anthracis. Probably responsible for energy coupling to the transport system.
Binds 1 Mg(2+) per subunit, coordinated entirely by the nucleotide and ordered water molecules.
Involved in nucleotide metabolism: produces dUMP, the immediate precursor of thymidine nucleotides and decreases the intracellular concentration of dUTP, so that uracil cannot be incorporated into DNA (Probable). The Ser-64 side chain changes its position upon ligand-binding to make contacts with the nucleotide phosphates (PubMed:20823546).
No visible phenotype; double yncF-yosS deletions (both encode dUTPases) are also viable.
The uracil deoxyribose moiety interacts with the protein through Ile-81 and Tyr-85, which discriminate against the ribose form of the nucleotide.
Mutant has normal levels of bacillithiol, but bshB1/bshB2 double mutant does not produce bacillithiol.
Catalyzes the last step of the phosphorylated serine biosynthetic pathway, i.e. dephosphorylation of O-phospho-L-serine to form L-serine. To a lesser extent, is also able to dephosphorylate phosphothreonine, phosphoethanolamine, and histidinol phosphate in vitro.
Cells lacking this gene cannot grow in minimal medium, in contrast to wild type. ysaA, serA, and serC deletion mutants have virtually identical profiles when observed across all the conditions studied, likely placing YsaA in the serine biosynthesis pathway. The defect is complemented by glycine, or a combination of serine and other amino acids such as glutamine or glutamate. The inability of serine alone to rescue the growth defect of the deletion mutant is due to serine toxicity.
ysaA complements E.coli serB and vice versa.
Belongs to the argininosuccinate synthase family. Type 1 subfamily.
The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
30S ribosomal subunit binding to Shine-Dalgarno sequences blocks exonuclease activity.
An RNase that has endonuclease and 5'-3' exonuclease activity, playing a role in both rRNA and mRNA stability and degradation. Endonuclease activity can cleave within 4 nucleotides of the 5'-end of a triphosphorylated RNA. Endonuclease digestion by the RNase J1/J2 complex occurs at a different site and in some cases more efficiently than J1 or J2 alone. The exonuclease activity of the J1/J2 complex is highly processive on substrates longer than 5 nucleotides, on shorter substrates is distributive. Preferentially cleaves ssRNA, possibly in AU-rich regions. The 5'-exonuclease activity acts on 5'-hydroxyl and 5'-monophosphate but not 5'-triphosphate ends; it can digest through stem-loop structures if they are not too stable. Required for maturation of 16S rRNA. Acts preferentially on 16S rRNA precursors after association of the 30S and 50S ribosomal subunits. Plays a role in the secondary pathway of 23S rRNA 5' end maturation. Probably also participates in processing of pre-scRNA (the precursor of the signal recognition particle RNA). Major RNase that degrades both RNAs of the type I toxin-antitoxin system BsrE/SR5 (PubMed:26940229).
Binds 1 Ca(2+) cation per subunit. Seen in 1 crystal structure, it is not clear if it is physiologically important.
Essential. In depletion experiments there is decreased 5'-exonuclease processing of 16S rRNA (PubMed:17512403), decreased accumulation of correctly-sized scRNA (PubMed:17576666), decreased decay of trp mRNA leader (PubMed:18445592), while correct processing of the 5' end of 23S rRNA no longer occurs in the absence of mrnC (PubMed:19880604). While depletion/deletion of RNase J1 or J2 has no large impact on global gene expression, a double mutant alters the expression of hundreds of genes (PubMed:18713320). In a more severe depletion experiment alteration of about 30% of transcripts was seen (PubMed:22412379). Later shown not to be essential in 4 strains, with a tripled doubling time. 168 trpC2 cells able to grow on minimal medium. Loss of competence for plasmid transformation, nearly complete loss of sporulation, poor growth at 30 degrees Celsius and no growth under 25 degrees Celsius. Increased sensitivity to a wide range of antibiotics. Irregularly shaped cells form clumps of spiral cells connected by long chains, with few visible septa, cell walls are altered with looser, less dense peptidoglycan. Double pnp-rnjA or rnjA-rny mutants could not be isolated (PubMed:23504012). Increased half-life of both RNAs of the type I toxin-antitoxin system BsrE/SR5 (PubMed:26940229).
Present in about 2500 monomers per cell in mid-log phase.
The C-terminal domain (residues 450-555) are required for nuclease activity and dimerization.
Belongs to the ABC transporter superfamily. ABCF family. YdiF subfamily.
Deletion mutant displays a 2-fold increase in the doubling time when galactan is the sole carbon and energy source.
Involved in galactan degradation (PubMed:27501980, PubMed:29240795). Part of the ABC transporter complex GanPQS involved in the uptake of galactooligosaccharides (PubMed:27501980, PubMed:29240795). Binds mainly galactotetraose and galactotriose (PubMed:27501980).
Was originally described as a cyclodextrin-binding protein, but it was shown later that it has no affinity for cyclodextrin.
Belongs to the aldehyde dehydrogenase family. IolA subfamily.
Catalyzes the oxidation of malonate semialdehyde (MSA) and methylmalonate semialdehyde (MMSA) into acetyl-CoA and propanoyl-CoA, respectively (PubMed:16332250, PubMed:18310071, PubMed:21515690). Is involved in a myo-inositol catabolic pathway (PubMed:18310071). Bicarbonate, and not CO2, is the end-product of the enzymatic reaction (PubMed:16332250).
Catalyzes the oxidation of malonate semialdehyde (MSA) and methylmalonate semialdehyde (MMSA) into acetyl-CoA and propanoyl-CoA, respectively.
Represses the synthesis of biosynthetic enzymes and activates the arginine catabolism. Controls the transcription of the two operons rocABC and rocDEF.
The EIIA type-4 domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the EIIB type-4 domain.
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II LevDE PTS system is involved in fructose transport.
Up-regulated by xylose. Subject to carbon catabolite repression (CCR).
Belongs to the precorrin methyltransferase family.
Probable component of primosome involved in the initiation of DNA replication.
Belongs to the uracil-DNA glycosylase (UDG) superfamily. UNG family.
Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Interacts with bacillus phage phi29 protein p56; this interaction inhibits the uracil-DNA glycosylase.
Expressed during sporulation (at protein level).
Decreases c-di-AMP levels in mid-exponential phase from about 3.8 uM to about 2.8 uM in strain BG214 (PubMed:25616256). No change in sensitivity to methyl methanesulfonate (MMS), decreased survival after UV irradiation in transition and stationary phase, strong decrease in competence (PubMed:9141693). Cells lacking this gene show a reduced c-di-AMP level compared to wild-type and cannot properly trigger the DNA damage response (PubMed:21566650). No effect on antibiotic sensitivity to the beta-lactam antibiotic cefuroxime (CEF), upon overexpression of the c-di-AMP phosphodiesterase GdpP increased sensitivity to CEF (PubMed:22211522). Double disA-cdaA mutants cannot be made, suggesting they are lethal, while double disA-cdaS and cdaA-cdaS mutants are viable (PubMed:22211522, PubMed:23192352). Depletion of cdaA in double disA-cdaA deletion cells leads to cell lysis (PubMed:22211522). Exponentially growing cells are 100-fold more sensitive to MMS, no change in response to H(2)O(2) or nalidixic acid; a double disA-radA deletion suppresses H(2)O(2) sensitivity of the radA mutant, but has no effect on MMS sensitivity, suggesting radA and disA might work in the same DNA repair pathway (PubMed:25616256).
Diadenylate cyclase activity is inhibited by the interaction with RadA (By similarity). Diadenylate cyclase activity is not affected by ssDNA or dsDNA, but three- and four-way junctions strongly inhibit the activity of DisA, suggesting the enzyme is regulated by branched nucleic acids.
Expression increases during late exponential phase and at the onset of sporulation (PubMed:16713562). Transcribed under partial control of SigM ECF sigma factor (PubMed:17434969).
Has also diadenylate cyclase activity, catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP). c-di-AMP acts as a signaling molecule that couples DNA integrity with progression of sporulation. The rise in c-di-AMP level generated by DisA while scanning the chromosome, operates as a positive signal that advances sporulation; upon encountering a lesion, the DisA focus arrests at the damaged site and halts c-di-AMP synthesis.
Homooligomer (PubMed:18439896). Interacts with RadA (PubMed:23760274).
One of 3 paralogous diadenylate cyclases (DAC) in this bacteria (PubMed:23192352). Has diadenylate cyclase activity, catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP) (PubMed:18439896, PubMed:25616256). c-di-AMP acts as a signaling molecule that couples DNA integrity with progression of sporulation. The rise in c-di-AMP level generated by DisA while scanning the chromosome operates as a positive signal that advances sporulation; upon encountering a lesion, the DisA focus arrests at the damaged site and halts c-di-AMP synthesis. Does not convert GTP to c-di-GMP (PubMed:18439896).
Participates in a DNA-damage check-point that is active prior to asymmetric division when DNA is damaged (PubMed:9141693, PubMed:16713562). Forms globular foci that rapidly scan along the chromosomes during sporulation, searching for lesions. Its ability to scan through the chromosome rapidly is due to its non-specific DNA-binding. When a lesion is present, DisA pauses at the lesion site (PubMed:21566650). This triggers a cellular response that culminates in a temporary block in sporulation initiation. It is required, at least partially, to inhibit the activity of the transcription factor spo0A, which controls, among others, early sporulation genes. In B.subtilis c-di-AMP is a second messenger that mediates growth, DNA repair and cell wall homeostasis (PubMed:22211522); it is toxic when present in excess (PubMed:26240071).
Participates in a DNA-damage check-point that is active prior to asymmetric division when DNA is damaged. DisA forms globular foci that rapidly scan along the chromosomes during sporulation, searching for lesions. When a lesion is present, DisA pauses at the lesion site. This triggers a cellular response that culminates in a temporary block in sporulation initiation.
Member of the two-component regulatory system DesR/DesK, responsible for cold induction of the des gene coding for the Delta5 acyl-lipid desaturase.
Belongs to the UDP-glucose/GDP-mannose dehydrogenase family.
Catalyzes the conversion of UDP-glucose into UDP-glucuronate, one of the precursors of teichuronic acid.
Homotetramer. Interacts with several proteins involved in DNA metabolism such as PriA, RecQ, RecG, RecS, DnaE, RarA, RecJ, RecO, SbcC, YrrC, XseA and Ung.
Phosphorylated by YwqD, which increases ssDNA affinity; dephosphorylated by YwqE.
Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism (PubMed:21170359). Has a 20-fold higher affinity for ssDNA than SsbB; SsbA and DprA activate the homologous DNA strand exchange function of RecA-ATP (PubMed:25138221).
Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism.
Strongly expressed during exponential growth, decreases 2-4-fold in stationary phase, part of the rpsF-ssbA-rpsR and the ychF-rpsF-ssbA-rpsR operons (PubMed:14762004). The operon is induced by DNA damage by mitomycin C (PubMed:14762004).
Belongs to the glycosyl hydrolase 3 family.
Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides. Cleaves muropeptides, but not peptidoglycan.
Up-regulated during the late phase of exponential growth and during stationary phase.
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in lichenan transport.
Putative transport protein involved in arginine degradative pathway. Probably transports arginine or ornithine.
Cells lacking this gene have a 5-fold increased spontaneous mutation frequency. A triple MutS/MutL/nth disruption has a 280-fold increased spontaneous mutation frequency.
DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.
In stationary phase; under control of SigD (PubMed:11987133). Repressed by LytR.
Possibly involved in cell wall metabolism during spore formation. Enhances the amidase activity approximately threefold.
B.subtilis does not possess a trehalose-specific phosphotransferase enzyme IIA component, however it seems that it use the glucose-specific phosphotransferase enzyme IIA component to delivers trehalose-6-phosphate into the cell.
Induced by trehalose-6-phosphate. Repressed by TreR.
The PTS EIIB type-1 domain is phosphorylated by phospho-EIIA-Glc (EIII-Glc) on a cysteinyl residue. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the PTS EIIC type-1 domain.
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in trehalose transport.
Belongs to the glycosyltransferase 8 family.
By different stresses such as heat shock and salt stress and by starvation.
Belongs to the membrane-bound acyltransferase family.
Consists of a ring of transmembrane domains, which shield a highly conserved extracellular structural funnel extending into the middle of the lipid bilayer. The conserved catalytic His residue is located at the bottom of this funnel and is connected to the intracellular DltC through a narrow tunnel.
O-acyltransferase that catalyzes D-alanylation of both teichoic acid and lipoteichoic acid (LTA) (PubMed:30283133). D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall (PubMed:7797557). Catalyzes D-alanylation from DltC carrier protein (PubMed:30283133).
O-acyltransferase that catalyzes D-alanylation of both teichoic acid and lipoteichoic acid (LTA). D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall. Catalyzes D-alanylation from DltC carrier protein.
Inhibited by dichloroisocoumarin (DCI) and N-p-tosyl-L-phenylalanine chloromethyl ketone (TPCK), but not by other serine protease inhibitors such as sulfonyl fluoride PMSF and 4-(2-aminoethyl)benzenesulfonyl fluoride (AEBSF).
Rhomboid-type serine protease that catalyzes intramembrane proteolysis. Important for normal cell division and sporulation. May act as a glucose exporter.
Catalytic subunit of the KtrAB potassium uptake transporter. The 2 major potassium transporter complexes KtrAB and KtrCD confer resistance to both suddenly imposed and prolonged osmotic stress.
Homodimer, tetramer (dimer of homodimer) and octamer (tetramer of homodimer). Part of the KtrAB complex formed by an octameric catalytic ring of KtrA and a membrane associated dimer of KtrB forming a potassium channel.
Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Binds 2 divalent metal cations per subunit. Can use cobalt, zinc, and possibly also magnesium ions.
SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3'->5' double strand exonuclease that can open hairpins. It also has a 5' single-strand endonuclease activity (By similarity).
SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3'->5' double strand exonuclease that can open hairpins. It also has a 5' single-strand endonuclease activity.
Catalyzes the conversion of a range of fructosamine 6-phosphates to glucose 6-phosphate and a free amino acid.
A triple bsdB-bsdC-bsdD deletion mutant no longer converts vanillin to guaiacol, the conversion stops at vanillic acid (PubMed:26658822).
Belongs to the UbiD family. YclC subfamily.
Binds 1 prenylated FMN (prenyl-FMN) per subunit.
Involved in the non-oxidative decarboxylation and detoxification of phenolic derivatives under both aerobic and anaerobic conditions (PubMed:15979273, PubMed:18388975). Phenolic acid decarboxylase that catalyzes the reversible decarboxylation of 4-hydroxybenzoate and vanillate (PubMed:15979273, PubMed:18388975). Could also catalyze the decarboxylation of salicylate (Probable). Is not active on di- and tri-hydroxybenzoate derivatives (PubMed:18388975).
Involved in the non-oxidative decarboxylation and detoxification of phenolic derivatives.
It is not known, if phenolic acid decarboxylase forms a complex composed of BsdB, BsdC and BsdD. The term subunit is often used in reference to the operon, however there is no experimental evidence to prove the existence of the complex.
Up-regulated by salicylate via the transcriptional regulator BsdA.
Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.
Positively regulated by TnrA under nitrogen-limited conditions. Induced by ArfM.
Belongs to the serine/threonine dehydratase family.
Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2-ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA (By similarity).
Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2-ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.
Although there are Cys and Trp residues in equivalent positions with the residues forming a thioether cross-link in the eukaryotic homologous sequences, no thioether cross-link is formed in this protein.
Belongs to the cysteine dioxygenase family.
Consists of a catalytic RNA component (M1 or rnpB) and a protein subunit.
Consists of a catalytic RNA component (M1 or rnpB) and a protein subunit. Might be a component of the prossible RNA degradosome complex composed of rny, rnjA, rnjB, pnp, pfkA and eno, and possibly also rnpA. Interacts with RNA helicase CshA.
RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Homotetramer. Forms an RuvA(8)-RuvB(12)-Holliday junction (HJ) complex. HJ DNA is sandwiched between 2 RuvA tetramers; dsDNA enters through RuvA and exits via RuvB. An RuvB hexamer assembles on each DNA strand where it exits the tetramer. Each RuvB hexamer is contacted by two RuvA subunits (via domain III) on 2 adjacent RuvB subunits; this complex drives branch migration. In the full resolvosome a probable DNA-RuvA(4)-RuvB(12)-RuvC(2) complex forms which resolves the HJ.
The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Belongs to the CidA/LrgA family. CidA subfamily.
Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidA protein. When a cell is stressed by the addition of antibiotics or by other factors in the environment, CidA possibly oligomerizes within the bacterial cell membrane, creating lesions that disrupt the proton motive force, which in turn results in loss of cell viability. These lesions are also hypothesized to regulate the subsequent cell lysis by either allowing the murein hydrolases access to the cell wall substrate and/or regulating their activity by a possible change in the cell wall pH that results from loss of membrane potential.
Transcriptionally regulated by SigD. Negatively regulated by TnrA under nitrogen-limited conditions.
Catalyzes the dismutation of two molecules of 6,7-dimethyl-8-ribityllumazine, resulting in the formation of riboflavin and 5-amino-6-(D-ribitylamino)uracil.
Homotrimer. Can interact with 6,7-dimethyl-8-ribityllumazine synthase, forming a lumazine synthase/riboflavin synthase complex, also designated as 'heavy riboflavin synthase complex', which consists of a trimer of riboflavin synthase enclosed within an icosahedral structure composed of 60 subunits of 6,7-dimethyl-8-ribityllumazine synthase.
It is uncertain whether Met-1, Met-44 or Met-88 is the initiator.
Cell division protein that is part of the divisome complex and is recruited early to the Z-ring. Probably stimulates Z-ring formation, perhaps through the cross-linking of FtsZ protofilaments. Its function overlaps with FtsA.
Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine, the other is coordinated via 3 cysteines and maybe direct contact with the SboA precursor.
Catalyzes the formation of 3 thioether bonds during production of the sactipeptide subtilosin from SboA. In vitro the thioether bonds cannot be made in the absence of the SboA propeptide, suggesting this is the first reaction in subtilosin maturation (PubMed:22366720). In vitro, in the absence of a second substrate, cleaves S-adenosyl-L-methionine into Met and 5'-dA (PubMed:22366720).
Probable amino-acid or metabolite transport protein.
Induced 3-fold by the beta-lactam antibiotic cefuroxime.
No effect on antibiotic resistance; double sigM-sigX mutants have 130-fold increases sensitivity to the beta-lactam antibiotic cefuroxime (PubMed:22211522). Association with RNAP core increases during many stresses (at protein level) (PubMed:21710567).
Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released. May be involved in the regulation of iron metabolism. Associates with RNAP core during early growth phases, association decreases as cells age (PubMed:21710567).
Could be involved in insertion of integral membrane proteins into the membrane.
Consists mostly of well conserved tandem repeats.
Glucose deprivation induces sporulation and several other adaptive responses.
Glucose or phosphate starvation, and addition of decoyinine. Also by heat shock, salt stress and oxidative stress.
Involved in an adaptive response to nutrient deprivation other than sporulation.
Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction.
Activated by the two-component regulatory system MalK/MalR in response to malate. The regulator MalR binds to the promoter region of maeN.
Acts as a Na(+)-malate symporter, as it catalyzes malate-dependent uptake of Na(+) and Na(+)-dependent uptake of malate.
Component in a DNA repair pathway. Removal of UV LIGHT damaged nucleotides. Recognizes pyrimidine dimers and cleave a phosphodiester bond immediately 5' to the lesion (By similarity).
Component in a DNA repair pathway. Removal of UV LIGHT damaged nucleotides. Recognizes pyrimidine dimers and cleave a phosphodiester bond immediately 5' to the lesion.
Component in a DNA repair pathway. Removal of UV-light damaged nucleotides. Recognizes pyrimidine dimers and cleave a phosphodiester bond immediately 5' to the lesion.
Belongs to the thiamine pyrophosphokinase family.
Catalyzes the phosphorylation of thiamine to thiamine pyrophosphate.
Part of a binding-protein-dependent transport system. Probably responsible for the translocation of the substrate across the membrane (By similarity).
Catalyzes the 2,6-dichlorophenolindophenol-dependent cleavage of acetoin into acetate and acetaldehyde.
Tetramer of 2 alpha and 2 beta subunits.
By Spo0A during nutrient starvation, through its direct negative control of AbrB, repressed by AbrB during regular growth when nutrients are plentiful, and also by SdpR (PubMed:16469701). Induced by expression of SDP (active peptide of sdpC) (PubMed:16469701, PubMed:23687264).
Immunity protein that provides protection for the cell against the toxic effects of SDP, its own SdpC-derived killing factor, and that functions as a receptor/signal transduction protein as well. Once SDP accumulates in the extracellular milieu, SdpI binds to SDP, causing sequestration of SdpR at the bacterial membrane.
Results in increased SigW expression which is dependent on SdpC. Results in weaker growth (70% of wild-type cell density) on LB medium, with more pronounced effects on sporulation medium (15% of wild-type). Concomitant deletion of SigW results in greatly diminished growth (5% of wild-type on LB and 3% on sporulation medium). Over time, single SdpI mutant stops growing on sporulation medium, while the SdpI SigW double mutant eventually lyses. Deletion of RsiW restores growth of the SdpI single mutant to near wild-type levels.
Expressed during sporulation, in the late phase of coat protein synthesis.
Ambiactive repressor and activator of the transcription of genes expressed during the transition state between vegetative growth and the onset of stationary phase and sporulation. It controls the expression of genes spovG and tycA. AbrB binds to the tycA promoter region at two A- and T-rich sites, it may be the sole repressor of tycA transcription.
Belongs to the FADH(2)-utilizing monooxygenase family.
Catalyzes the hydroxylation of 4-hydroxyphenylacetic acid (4HPA), leading to the production of 3,4-dihydroxyphenylacetic acid (DHPA).
Deletion mutant does not show any observable phenotype.
Required for resistance to linearmycins, a family of antibiotic-specialized metabolites produced by some streptomycetes (PubMed:26647299, PubMed:28461449). Member of the two-component regulatory system LnrJ/LnrK, which induces expression of the LnrLMN ABC transporter in response to linearmycins and other polyenes (PubMed:11717295, PubMed:26647299, PubMed:28461449). Probably binds to the promoter region of the lnrLMN operon and directly regulates its expression (Probable). May also promote biofilm formation (PubMed:28461449).
Belongs to the multicopper oxidase family.
Binds 4 copper ions per subunit. The 4 copper centers adopt structures classified as type 1, type 2 and type 3.
CotA is also a promising candidate for the clinical determination of direct bilirubin and total bilirubin, which are significant diagnostic marker of liver function and cancer.
Disruption of the gene does not prevent spore formation, but mutant is blocked in the appearance of the brown pigment characteristic of colonies of wild-type sporulating cells.
Expression is switched on about four to five hours after the onset of sporulation, a time that corresponds approximately to the stage of spore coat synthesis and deposition.
Glu-498, located within the entrance channel of the trinuclear center, plays a key role in the protonation events that occur at the trinuclear center and in its stabilization, controlling therefore the binding of dioxygen and its further reduction (PubMed:20822511, PubMed:20200715). Asp-116, situated in the exit channel of the trinuclear center, and its hydrogen bond connectivity are highly relevant for the overall reactivity of the laccase but do not appear to play a critical structural role (PubMed:22481612).
In vitro, also shows strong bilirubin oxidase (BOD) activity, and can catalyze the oxidation of free bilirubin (UB), direct bilirubin (conjugated with glucuronic acid, DB) and ditaurobilirubin.
Multicopper oxidase that catalyzes the oxidation of a variety of substrates, including phenolic and non-phenolic compounds. Substrates include syringaldazine (SGZ), 2,6-dimethoxyphenol (2,6-DMP) and the non-phenolic compound 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) (PubMed:11514528, PubMed:11884407, PubMed:18307408, PubMed:20200715, PubMed:22481612, PubMed:27050268). Has no tyrosinase activity (PubMed:11514528). Is implicated in the biosynthesis of a brownish pigment that characterizes sporulating colonies of B.subtilis, and which appears to be a melanin-like product and to confer protection against UV light (PubMed:2821284, PubMed:11514528, PubMed:11884407).
When expressed on the surface of E.coli cells, CotA was shown to possess improved enzymatic properties, including higher thermal stability and stronger inhibitor tolerance. It has high enzymatic activity against three industrial dye types: an anthraquinone dye, Acid Blue 62, a triphenylmethane dye, Malachite Green, and an azo dye, Methyl Orange. It may help decrease the costs and simplify wastewater treatment, and therefore, surface-displayed CotA shows a great potential for industrial-scale dye decolorization.
As a fusion partner, can be used for high-level production of other membrane proteins in their native conformations, including many eukaryotic proteins that have previously been intractable to bacterial expression.
Chaperone that facilitates the production and integration of integral membrane proteins into the bacterial lipid bilayer.
Belongs to the type II topoisomerase family. ParE type 2 subfamily.
Binds two Mg(2+) per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) or Ca(2+).
Heterotetramer composed of ParC and ParE.
Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule.
Belongs to the polysaccharide pyruvyl transferase family.
Expression is sigma G-dependent, and to a very small extent sigma F-dependent.
ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner (By similarity). Has been implicated in preventing sigma(G) activity under non-sporulation conditions.
ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
Homohexamer. Organized in a ring with a central cavity (By similarity). Exists as a mixture of small oligomeric species in solution.
Homohexamer. Organized in a ring with a central cavity.
Grows slowly with cystine as sole sulfur source.
Homodimer. Forms homotetramers at higher concentrations of protein. Forms CymR(2):CysK(2) or CymR(4):CysK(4) complexes in the absence of O-acetylserine.
Master repressor of cysteine metabolism in B.subtilis. Controls the expression of genes involved either in cysteine synthesis from sulfide (cysK), sulfonates (ssu), or methionine (mccAB) or in cystine uptake (tcyP). Activity of CymR is positively regulated by CysK in response to cysteine availability. When cysteine is present, the pool of O-acetylserine (OAS) is low, which leads to the formation of a CymR-CysK complex and transcriptional repression of the CymR regulon occurs. In the absence of cysteine, the OAS pool is high and the CymR-CysK complex is mostly dissociated, leading to a faster dissociation of CymR from its DNA targets and the lifting of CymR-dependent repression.
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in N-acetylglucosamine transport (By similarity).
Belongs to the ETF beta-subunit/FixA family.
Was initially thought to be two separate ORFs named yhaJ and yhaK.
May play a role in the activation or the expression of KinB.
Belongs to the dihydroorotate dehydrogenase family. Type 1 subfamily.
Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor.
Heterotetramer of 2 PyrK and 2 PyrD type B subunits.
Belongs to the rhamnose isomerase family.
Catalyzes the interconversion of L-rhamnose and L-rhamnulose.
Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella and sporulation. Involved in prophage SP-beta-mediated cell lysis.
Repressed by AbrB. Induced in stationary phase in LB (rich) medium; the transcript is present in log phase cells grown in modified competence (MC) and MM media.
Suggested to be the precursor for an exported, modified peptide that has antimicrobial and/or signaling properties. Synthesis requires YydG and YydH; the peptide is proposed to be exported by the YydIJ transporter. In the absence of the transporter, the modified peptide activates the LiaRS two-component regulatory system, possibly by eliciting cell envelope stress. This activation can occur in trans in cocultured cells lacking either the transporter or the whole operon.
Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Belongs to the ABC transporter superfamily. Ribose importer (TC 3.A.1.2.1) family.
Part of the ABC transporter complex RbsABC involved in ribose import. Responsible for energy coupling to the transport system.
The complex is composed of an ATP-binding protein (RbsA), two transmembrane proteins (RbsC) and a solute-binding protein (RbsB).
Probably part of the ABC transporter DppBCDE involved in dipeptide transport (Probable). Responsible for energy coupling to the transport system (Probable).
Belongs to the glycerophosphoryl diester phosphodiesterase family.
Deletion mutant retains WTA and ceases growth upon phosphate limitation (PubMed:27780866). Mutants show altered cell morphologies and effects on autolytic activity and antibiotic susceptibilities that, unexpectedly, also occur in phosphate-replete conditions (PubMed:27780866).
Glycerophosphodiester phosphodiesterase hydrolyzes glycerophosphodiesters into glycerol-3-phosphate (G3P) and the corresponding alcohol (PubMed:27780866). Involved in wall teichoic acid (WTA) metabolism during phosphate starvation (PubMed:27780866). Catalyzes the degradation of WTA, enabling the utilization of WTA as a phosphate reserve under limiting conditions (PubMed:27780866). Is highly selective for the poly(gylcerol phosphate) WTA backbone and catalyzes exolytic cleavage of individual monomer units (PubMed:27780866). In vitro is active toward the WTA oligomer mimics glycerophosphoglycerol (GPG) and bis-glycerophosphoglycerol (bGPG) (PubMed:27780866).
Belongs to the thiolase-like superfamily. Thiolase family.
Belongs to the heat shock protein 90 family.
Molecular chaperone. Has ATPase activity.
Participates in transcription elongation, termination and antitermination.
Participates in transcription elongation, termination and antitermination. Stimulates RNA polymerase pausing at U107 and U144 in the trp leader. NusG-stimulated pausing is sequence specific. Does not affect trp leader termination.
Belongs to the methylthioribose kinase family.
Catalyzes the phosphorylation of methylthioribose into methylthioribose-1-phosphate.
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in glucose transport.
The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
Belongs to the DNA polymerase type-C family. PolC subfamily.
Mutant azp12 has a form of DNA polymerase III resistant to hydroxyphenylazopyrimidines.
Required for replicative DNA synthesis. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
Probably interacts with cognate immunity protein YokJ but not with non-cognate immunity proteins. The interaction inhibits the toxic activity of YokJ (Probable).
Toxic component of one of 6 LXG toxin-immunity modules in this strain. They promote kin selection, mediate competition in biofilms, and drive spatial segregation of different strains, indicating that LXG toxins may help avoid warfare between strains in biofilms. Mediates intercellular competition during biofilm formation; disruption of the operon disadvantages the bacteria, but overexpression of the cognate immunity protein restores growth in competition with wild-type. Overexpression alone in situ causes growth arrest but not cell lysis, a large decrease in chromosomal DNA content and the production of anucleate cells. No effect is seen on rRNA. Co-overexpression with cognate immunity protein YokJ does not cause growth arrest. The toxic effect is dependent on the epsA and tapA operons which are required for biofilm formation (PubMed:34280190). The C-terminus (residues 449-571) inhibits growth upon expression in E.coli which is neutralized by cognate immunity protein YokJ, but not by immunity proteins specific to other toxins with the LXG domain (PubMed:22200572).
Belongs to the bacterial ribosomal protein bL27 family.
No effect on sporulation at 37 degrees Celsius, however sporulation decreases at 47 degrees Celsius.
Plays a role in sporulation at high temperatures.
Belongs to the cytochrome ubiquinol oxidase subunit 2 family.
Binds 1 iron-chlorin (heme d or cytochrome d) per heterodimer, in conjunction with CydA.
Binds 1 protoheme IX center (heme b595) per heterodimer, in conjunction with CydA.
Probable member of the two-component regulatory system YkoH/YkoG.
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. NifS/IscS subfamily.
Catalyzes the removal of elemental sulfur from cysteine to produce alanine.
Plays a role in the competence of cells to be transformed. It inhibits the activity of the DNA-entry nuclease.
This protein is a subunit of a 75 kDa protein complex, which governs binding and entry of donor DNA. The complex is a tetramer of two subunits of the DNA-entry nuclease and two subunits of a competence-specific protein. Only the complex is able to bind ds- and ss-DNA.
Transcription starts around hour 2 of sporulation and requires sigma-E.
Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 1 subfamily.
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.
Consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal anticodon-binding domain.
Cells produce PGA but at a greatly reduced level.
Seems to be required for maximum PGA (gamma-polyglutamic acid) production.
Belongs to the acetyltransferase family. GNAT subfamily.
Deletion mutant is susceptible to streptothricin.
Involved in resistance to streptothricin, a broad-spectrum antibiotic produced by streptomycetes. Detoxifies streptothricin via acetylation of the beta amino group of the first beta-lysyl moiety of streptothricin.
Enables the recognition and targeting of unfolded and aggregated proteins to the ClpC protease or to other proteins involved in proteolysis. Also involved in Spx degradation by ClpC (By similarity). Acts negatively in the development of competence by binding ComK and recruiting it to the ClpCP protease. When overexpressed, inhibits sporulation.
Negatively autoregulated. Induced by melibiose and raffinose.
Represses the melibiose operon melREDCA in the absence of melibiose or raffinose. Binds to two binding sites at the promoter region of the operon.
Shows a 3'-5' exoribonuclease activity as well as single-stranded DNA 3'-5'exonuclease activity. Plays a role in the secondary pathway of 23S rRNA 3' end maturation.
Expressed at the postexponential growth phase; regulated by the DegS-DegU system.
Catalyzes the S-adenosyl-L-methionine-dependent formation of N(1)-methyladenine at position 22 (m1A22) in tRNA.
Homodimer. Part of the KtrCD complex formed by an octameric catalytic ring of KtrC and a membrane associated dimer of KtrD forming a potassium channel (By similarity).
Integral membrane subunit of the KtrCD potassium uptake transporter. The 2 major potassium transporter complexes KtrAB and KtrCD confer resistance to both suddenly imposed and prolonged osmotic stress.
DNA helicase used for plasmid rolling-circle replication and also involved in UV repair.
Interacts with YxaL; YwhK and YerB. Interacts with the RNA polymerase core (PubMed:21710567).
Energy-dependent efflux pump responsible for decreased drug accumulation in multi-drug-resistant cells. Probably uses a transmembrane proton gradient as the energy source. Causes the efflux of a variety of toxic substances, including such structurally diverse compounds as ethidium bromide, rhodamine and acridine dyes, tetraphenylphosphonium, puromycin, chloramphenicol, doxorubicin, and fluoroquinolone antibiotics.
Belongs to the ABC transporter superfamily. L-cystine importer (TC 3.A.1.3.14) family.
Part of the ABC transporter complex TcyABC involved in L-cystine import. Responsible for energy coupling to the transport system (Probable).
The complex is composed of two ATP-binding proteins (TcyC), two transmembrane proteins (TcyB) and a solute-binding protein (TcyA).
By degrading DNA that enters the cell, plays a role in the competence of cells to be transformed. Degrades both double-stranded, linear and covalently closed circular DNA.
The activity can be inhibited by the 18 kDa competence-specific protein nin.
Interacts with both the D1 and D2 domains of dynamin-like protein DynA.
Only expressed during growth in minimal medium (PubMed:14762004).
Involved in the uptake of iron. Probably responsible for the translocation of the substrate across the membrane.
Part of the ABC transporter complex FeuABC/YusV involved in import of the catecholate siderophores bacillibactin and enterobactin.
The complex is composed of one ATP-binding protein (YusV), two transmembrane proteins (FeuB and FeuC) and a solute-binding protein (FeuA).
May function as endopeptidase which proteolytically removes the C-terminal three residues of farnesylated peptides containing the CAAX motif where C is cysteine, A is an aliphatic amino acid and X is any amino acid.
Is responsible for site-2 cleavage of the RsiW anti-sigma factor (PubMed:15130127). This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor (PubMed:16899079). Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane (PubMed:21810987).
Regulated intramembrane proteolysis (RIP) occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. A membrane-spanning regulatory substrate protein is first cut extracytoplasmically (site-1 protease, S1P), then within the membrane itself (site-2 protease, S2P, this enzyme), while cytoplasmic proteases finish degrading the regulatory protein, liberating the effector protein.
Negative transcriptional regulator of padC phenolic acid decarboxylase.
Phenolic acids regulate PadR repression activity, by impairing it's binding to the padC promoter.
Catalyzes the biosynthesis of PGA (gamma-polyglutamic acid) from L-glutamate. Both the 44-kDa and the 33-kDa forms are required for PGA synthesis.
Forms membrane-associated dynamic filaments that are essential for cell shape determination (PubMed:11290328, PubMed:19659933). Acts by regulating cell wall synthesis and cell elongation, and thus cell shape (PubMed:19659933). A feedback loop between cell geometry and Mbl localization may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature (By similarity). Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on Mbl polymerization (PubMed:21636745, PubMed:21636744). Organizes peptidoglycan synthesis in the lateral cell wall (PubMed:19659933). Also required for proper chromosome segregation (PubMed:14588250).
Forms polymers (PubMed:11290328, PubMed:19659933). Forms a complex with MreB and MreBH (PubMed:17064365, PubMed:19659933). Interacts with MreC (PubMed:17064365).
Mutants are bent and twisted at irregular angles (PubMed:11290328). Depletion leads to a strong defect in chromosome segregation (PubMed:14588250).
Contains an N-terminal DNA-binding domain and a large C-terminal effector-binding domain. Contains two distinct sugar-binding sites with different affinities.
Homotetramer. Binds primarily as a dimer to each half-site of the full-length operator, with much higher affinity for the right site. Then, both dimers interact, bridging the two-half sites of the operator region.
In the absence of glucose, represses the transcription of the gapA operon, which encodes five key glycolytic enzymes. Binds specifically to the cggR-gapA promoter region and blocks the progression of the RNA polymerase, leading to the arrest of the transcription.
Stability and function are regulated by the effector molecule fructose-1,6-bisphosphate (FBP). In the presence of glucose, binding of FBP to the low-affinity sugar-binding site of CggR disrupts dimer/dimer bridging interactions and triggers a tetramer to dimer transition, which leaves two physically independent dimers on the target DNA and allows transcription of the downstream coding sequences by the RNA polymerase. In addition, FBP and several other phosphorylated compounds can bind to a high-affinity binding-site and protect CggR against aggregation and proteolysis.
Mutation impairs colony surface architecture (PubMed:16430695). Mutant produces fewer and altered amyloid fibers (PubMed:21477127).
Part of the tapA-sipW-tasA operon (PubMed:10464223). Expression is directly repressed by the DNA-binding protein master regulator of biofilm formation SinR and activated by the extracellular matrix regulatory protein RemA (PubMed:16430695, PubMed:23646920). Also positively regulated by the sporulation transcription factors sigma H and Spo0A and repressed by the transition phase regulatory protein AbrB, probably indirectly (PubMed:10464223). Induced by a high concentration of salt (PubMed:10559173). During most conditions of growth, may be present at very low levels or is not synthesized at all, due, at least in part, to post-transcriptional repression (PubMed:10559173).
Required for biofilm formation (PubMed:16430695, PubMed:16430696, PubMed:21477127, PubMed:24488317). Required for the proper anchoring and polymerization of TasA amyloid fibers at the cell surface (PubMed:16430696, PubMed:21477127, PubMed:24488317). Is also a minor component of TasA fibers (PubMed:21477127).
Belongs to the metallophosphoesterase superfamily. YfcE family.
Along with seryl-phosphorylated HPr, phosphorylated Crh is implicated in carbon catabolite repression (CCR) of levanase, inositol dehydrogenase, and beta-xylosidase. Exerts its effect on CCR by interacting with CcpA.
Mixture of monomers and homodimers. Interacts with CcpA as a monomer.
Not phosphorylated by PEP and by enzyme I.
Belongs to the IMPDH/GMPR family. GuaC type 2 subfamily.
Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides (Probable).
Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides.
Part of the ABC transporter complex TcyABC involved in L-cystine import. Probably responsible for the translocation of the substrate across the membrane (Probable).
Expressed in the mother cell compartment from T5 of sporulation.
Expression of ykvP is regulated by SigK and dependent on GerE.
Inactivation of the ykvP gene does not affect vegetative growth, spore resistance to heat, chloroform and lysozyme, or spore germination in the presence of L-alanine.
Cells lacking this gene retain 70% of arabinofuranosidase activity, and the double mutant abfA/abf2 is inactive.
Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the cleavage of terminal alpha-L-arabinofuranosyl residues in different hemicellulosic homopolysaccharides (branched and debranched arabinans) and heteropolysaccharides (arabinoxylans). It is able to hydrolyze the alpha-(1->5)-glycosidic linkages of linear alpha-(1->5)-L-arabinan (debranched), sugar beet arabinan (branched) and wheat arabinoxylan. Moreover, it displays higher activity towards branched arabinan, a molecule comprising a backbone of alpha-(1->5)-linked L-arabinofuranosyl residues decorated with alpha-(1->2)-, and alpha-(1->3)-linked L-arabinofuranosyl units, than towards debranched arabinan. In addition, arabinoxylan, which has L-arabinofuranose residues attached to the main chain by alpha-(1->2)- and/or alpha-(1->3)-glycosidic linkages, is preferred to linear alpha-(1->5)-L-arabinan.
Autolysins are cell wall hydrolases involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella - in particular of its basal body - and sporulation. Has a high affinity for teichoic acid-endowed peptidoglycan. LytC is required for efficient swarming motility but not at the level of cell separation or flagellum biosynthesis. Rather, LytC appears to be important for proper flagellar function.
Expressed under the control of SigD (major), the transcripts being predominants at the exponential growth phase, and SigA (minor). Repressed by LytR and YvrH.
Inactivation of this gene leads to an approximately 90% decrease in the total cell wall hydrolytic activity of stationary-phase cells and extraordinary resistance to cell lysis, even after 6 days of incubation at 37 degrees Celsius. Cells from domesticated laboratory strains lacking this gene show no motility changes on swarm plates; however in combination with an acetylglucosaminidase deletion (lytD, AC P39848) greatly reduced motility is seen. They also show no apparent changes in cell morphology, competence, sporulation, or germination. Cells from an undomesticated strain (3610) lacking this gene show a reduction in the rate of swarming motility.
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.
Binds 1 pyridoxal phosphate per subunit.
May also have succinyldiaminopimelate aminotransferase activity, thus carrying out the corresponding step in lysine biosynthesis.
Probably involved in cell-wall metabolism.
Belongs to the LDH/MDH superfamily. LDH family.
Belongs to the LDH/MDH superfamily. MDH type 3 family.
Catalyzes the reversible oxidation of malate to oxaloacetate.
Required for nitrite assimilation. Required for activity of the reductase (By similarity).
Almost completely inhibited by diethylpyrocarbonate at 5 mM and completely inhibited by phenylmethylsulfonyl fluoride (PMSF) at 50 mM. Dimethyl phosphite achieves only a 53% inhibition. Also inhibited by metal ions (magnesium, manganese and calcium) and chelating agent (EDTA) at the same level.
May play a role in the degradation of type I rhamnogalacturonan derived from plant cell walls. This enzyme has a broad substrate specificity, and shows strong preference for glucose pentaacetate, beta-naphthylacetate, and p-nitrophenyl acetate (pNPA). Also active toward acetylated xylan.
Belongs to the NAGSA dehydrogenase family. Type 1 subfamily.
Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
Bacteriocin active against Gram-positive bacteria. Inhibits B.cereus spore outgrowth, after the germination stage, approximately 1000-fold better than it inhibits exponential growth of the same cells. Inhibits B.subtilis strain ATCC 6633.
Loss of bacteriocin sublancin 168 production, but not resistance to sublancin.
Production of active sublancin-168 requires at least one thiol-disulfide oxidoreductase (BdbB or, in its absence, BdbC). Membrane translocation and cleavage of the precursor are probably performed by SunT.
Was originally (PubMed:9722542, PubMed:11872755) thought to be a lantibiotic but was later shown to be an S-linked glycopeptide.
Negatively regulates ABC transporter complex ytrBCDEF that plays a role in acetoin utilization during stationary phase and sporulation.
Belongs to the universal ribosomal protein uS14 family. Zinc-binding uS14 subfamily.
Cannot be disrupted; as the protein decreases in cells 70S ribosome formation decreases rapidly, with concomitant loss of uS2, uS3 and YugI (general stress protein 13) proteins from the 30S subunit.
Part of the 30S ribosomal subunit (PubMed:30126986, PubMed:17163968). Contacts proteins S3 and S10 (By similarity).
The major uS14 protein in the ribosome. Required for binding of uS2 and uS3 to the 30S subunit and for association of the 30S with the 50S subunit.
Belongs to the major facilitator superfamily. Bcr/CmlA family.
Cells lacking this gene have no acetoin reductase/2,3-butanediol dehydrogenase activity.
Homotetramer (Ref.5). Interacts with BrxC (PubMed:33722570).
Belongs to the ribonucleoside diphosphate reductase small chain family.
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (By similarity).
This gene has an intron within which is encoded YosQ, a putative homing endonuclease.
Forms multimers, possibly octamers; these become larger following DNA damage. Recruited to foci following DNA damage; probably interacts with RecF and RecO.
Involved in recombinational repair of damaged DNA. Seems to be the first protein recruited to repair centers, foci that are the site of double-strand DNA break(s), followed by RecO and then RecF.
May be involved in recombinational repair of damaged DNA.
Cotranscribed with sigma-M and yhdL. YhdK and YhdL negatively regulate sigma-M.
Interacts specifically with YhdL, while the N-terminus of YhdL interacts with sigma-M.
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor contributes to oxidative stress resistance.
Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Belongs to the protoporphyrinogen/coproporphyrinogen oxidase family. Coproporphyrinogen III oxidase subfamily.
Involved in coproporphyrin-dependent heme b biosynthesis (PubMed:7928957, PubMed:9217019). Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin III (PubMed:8288631, PubMed:7928957, PubMed:9217019, PubMed:9784236). Can also oxidize protoporphyrinogen IX to protoporphyrin-IX (PubMed:8288631, PubMed:7928957, PubMed:9217019, PubMed:9784236, PubMed:19944166). The specific activity for the oxidation of coproporphyrinogen III is much higher than that for the oxidation of protoporphyrinogen IX (PubMed:7928957, PubMed:9217019). Can also oxidize mesoporphyrinogen IX, but not uroporphyrinogen III (PubMed:8288631, PubMed:9784236, PubMed:7928957).
Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin III.
Mutations cause the accumulation of coproporphyrinogen III or coproporphyrin III in the growth medium and the accumulation of trace amounts of other porphyrinogens or porphyrins intracellularly.
Only weakly inhibited by acifluorfen, in contrast to eukaryotic family members (PubMed:8288631, PubMed:9784236, PubMed:19944166). Weakly inhibited by methylacifluorfen (PubMed:9784236). Bilirubin, biliverdin and hemin are all competitive inhibitors (PubMed:9784236).
Belongs to the SAICAR synthetase family.
Converts molybdopterin precursor Z into molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD (By similarity).
Heterotetramer of 2 MoaD subunits and 2 MoaE subunits. Also stable as homodimer. The enzyme changes between these two forms during catalysis (By similarity).
Catalyzes the conversion of butyryl-CoA through butyryl phosphate to butyrate.
Belongs to the lipase/esterase LIP3/BchO family.
Constitutively expressed, part of a 5 gene operon with multiple promoters. Not ethanol-stress induced.
Involved in the detoxification of xenobiotics. Shows maximal activity with C6 substrates, with gradually decreasing activity from C8 to C12 substrates. No activity for higher chain length substrates acids rather than long-chain ones (By similarity).
Belongs to the flavin oxidoreductase frp family.
Catalysis proceeds by a classical ping-pong bi-bi reaction mechanism. NADPH is more effective as an electron donor than NADH.
Reduces FMNH(2) to FMN, with NADPH as reductant. It also reduces nitroaromatic compounds, quinones and azo dyes.
Belongs to the polyribonucleotide nucleotidyltransferase family.
Homodimer (Probable). Component of a possible RNA degradosome complex composed of rny, rnjA, rnjB, pnp, pfkA and eno (although rnjA and rnjB's presence is unclear) (PubMed:19193632). RNA helicase CshA may also be a member of this complex (PubMed:20572937).
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. Necessary for competence development in Bacillus subtilis. May be necessary for modification of the srfA transcript (stabilization or translation activation). Involved in processing precursor type I toxin-antitoxin RNAs antitoxin SR4 and SR5 RNAs to their mature forms (PubMed:22229825, PubMed:26940229).
Not essential, doubling time increased slightly. About 800-fold less compentent for plasmid transformation, no effect on sporulation efficiency. Grows poorly at 18 degrees Celsius. Increased sensitivity to several translation inhibiting antibiotics such as tetracycline, erythromycin and chloramphenicol, but increased resistance to streptomycin and nalidixic acid. Forms long filamentous cells, probably due to defective septum formation, cell walls are altered with looser, less dense peptidoglycan. Double pnp-rny mutants grow very slowly, while pnp-rnjA mutants could not be isolated (PubMed:23504012). Accumulation of precursor forms of type I toxin-antitoxin system antitoxin RNAs SR4 and SR5 (PubMed:22229825, PubMed:26940229).
Disruption results in low transformability.
Part of the high-affinity ABC transporter complex ZnuABC involved in zinc import (Probable). Responsible for the translocation of the substrate across the membrane (By similarity). ZnuABC-mediated zinc transport is required for comF expression and competence development.
Activated, directly or indirectly, by endogenous spore dipicolinic acid released in response to nutrients. Is also activated by exogenous Ca(2+)-dipicolinic acid.
Expressed during sporulation; in mother cell compartment, then located in the spore coat.
Probable spore cortex-lytic enzyme involved in the depolymerization of cortex peptidoglycan during germination.
Transcriptionally regulated by sigma-A factor. Down-regulated by rex. Highest expression during the exponential growth phase.
Involved in the isomerization of 5-deoxy-glucuronate (5DG) to 5-dehydro-2-deoxy-D-gluconate (DKG or 2-deoxy-5-keto-D-gluconate).
Transcription factor involved in spore coat assembly and spore resistance. Regulates the transcription of at least cgeA, cotG and cotS.
Belongs to the nitronate monooxygenase family. NMO class I subfamily.
Nitronate monooxygenase that uses molecular oxygen to catalyze the oxidative denitrification of alkyl nitronates. Acts on propionate 3-nitronate (P3N), the presumed physiological substrate. Probably functions in the detoxification of P3N, a metabolic poison produced by plants and fungi as a defense mechanism.
P3N is a potent irreversible inhibitor of the key enzyme succinate dehydrogenase in the Krebs cycle and electron transport chain. P3N has been shown to be a toxic metabolite to bacteria, plants, fungi, mammals or any organism that uses succinate dehydrogenase.
Induced late during sporulation by the sporulation-specific sigma factor sigma-K and negatively regulated by GerE.
Belongs to the OMP decarboxylase family. Type 1 subfamily.
Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
Insertion mutations in this gene partially restore antibiotic resistance to the beta-lactam antibiotic cefuroxime (CEF) in a sigM deletion mutant (PubMed:22211522).
The anti-sigma factor for extracytoplasmic function (ECF) sigma factor SigX, inhibits SigX activity and stabilizes it.
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Belongs to the RNA methyltransferase RsmE family.
Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit (By similarity).
Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Can also bind zinc in vitro, but it does not impair DNA binding.
Metal-responsive transcriptional regulator that represses transcription of the aseR-ydfA operon by binding specifically to its promoter. Binding of arsenite or antimonite causes the repressor to dissociate from the DNA.
Part of the ABC transporter complex YkoCDEF that could transport hydroxymethylpyrimidine (HMP) and/or thiamine. Could also transport other HMP-containing products. Responsible for energy coupling to the transport system (Probable).
The complex is composed of two ATP-binding proteins (YkoD), two transmembrane proteins (YkoC and YkoE) and a solute-binding protein (YkoF).
Complements a S.cerevisiae SUA5 disruption mutant.
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine.
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate. Is also able to catalyze the reverse reaction in vitro, i.e. the formation of ATP from TC-AMP and PPi.
Unlike previously thought, the formation of TC-AMP does not proceed via an ATP-activated HCO(3)(-) intermediate such as carboxy-AMP.
Probably interacts with cognate immunity protein YwqK but not with non-cognate immunity proteins. The interaction inhibits the toxic activity of YwqJ.
Toxic component of one of 6 LXG toxin-immunity modules in this strain. They promote kin selection, mediate competition in biofilms, and drive spatial segregation of different strains, indicating that LXG toxins may help avoid warfare between strains in biofilms. Mediates intercellular competition during biofilm formation; disruption of the operon disadvantages the bacteria, but overexpression of the cognate immunity protein restores growth in competition with wild-type. Overexpression alone in situ causes growth arrest but not cell lysis; no effect is seen on DNA or rRNA. Co-overexpression with cognate immunity protein YwqK does not cause growth arrest. The toxic effect is dependent on the epsA and tapA operons which are required for biofilm formation (PubMed:34280190). Its toxic effects are probably neutralized by its cognate immunity protein YwqK, but not by immunity proteins specific to other toxins with the LXG domain (Probable). May have deaminase activity (Probable).
Belongs to the ArsC family. Spx subfamily.
Global transcriptional regulator that plays a key role in stress response and exerts either positive or negative regulation of genes (PubMed:12642660, PubMed:15659166, PubMed:16885442, PubMed:18662407, PubMed:18687074, PubMed:29271514). Acts by interacting with the C-terminal domain of the alpha subunit of the RNA polymerase (RNAP) (PubMed:12642660, PubMed:15659166, PubMed:18687074, PubMed:20084284). This interaction can enhance binding of RNAP to the promoter region of target genes and stimulate their transcription, or block interaction of RNAP with activator proteins and repress transcription (PubMed:12642660, PubMed:15659166, PubMed:18687074, PubMed:20084284). Exhibits no DNA-binding activity (PubMed:15659166, PubMed:18687074).
Global transcriptional regulator that plays a key role in stress response and exerts either positive or negative regulation of genes. Acts by interacting with the C-terminal domain of the alpha subunit of the RNA polymerase (RNAP). This interaction can enhance binding of RNAP to the promoter region of target genes and stimulate their transcription, or block interaction of RNAP with activator.
Inactivation of the gene results in ClpP-independent competence development as well as partial suppression of the sporulation defect conferred by clpP mutation (PubMed:11703662). Null mutant shows hypersensitivity to disulfide stress and to paraquat (PubMed:14597697, PubMed:18662407). Mutants have increased sensitivity toward cell wall active antibiotics inhibiting both early and late steps in peptidoglycan synthesis (PubMed:29271514). Cells lacking the gene are defective in thermotolerance (PubMed:24417481).
Induces the expression of a large number of genes in response to a variety of stress conditions, such as disulfide, heat and cell wall stress, while concurrently repressing transcription of genes involved in various developmental and growth-related pathways during periods of extreme stress (PubMed:12642660, PubMed:14597697). Functions in the oxidative stress response via induction of the transcription of thioredoxin (trxA) and thioredoxin reductase (trxB) during thiol-specific oxidative (disulfide) stress (PubMed:14597697, PubMed:15659166, PubMed:18687074). Mediates response to oxidative stress caused by paraquat (PQ) via induction of the methionine sulfoxide reductase genes, msrA and msrB (PubMed:18662407). Also acts as a transcriptional activator of the bacillithiol (BSH) biosynthesis genes in response to oxidizing conditions and thio-reactive compounds (PubMed:23894131). Involved in heat stress response and thermotolerance development, which results in diminished cellular protein aggregates (PubMed:24417481). Plays an important adaptive role in the cell wall stress response (PubMed:29271514). Participates in sulfate-dependent control of organosulfur metabolism. Negatively controls, via CymR, the expression of the organosulfur utilization operons ytmI, yxeI and ssu, and directly activates yrrT operon expression during growth in medium containing methionine as sole sulfur source (PubMed:16885442). Negatively affects competence and sporulation (PubMed:11703662, PubMed:12028382). Inhibits biofilm formation in response to disulfide stress by repressing biofilm matrix genes (PubMed:30718304).
Interacts with the C-terminal domain of the alpha subunit of the RNAP (PubMed:12642660, PubMed:16249335, PubMed:19580872, PubMed:20084284, PubMed:22307755). A single Spx monomer interacts with RNAP to form the transcription activation complex (PubMed:22307755). Interacts with the adapter protein SpxH/YjbH (PubMed:19074380, PubMed:24942655, PubMed:30982633).
Interacts with the C-terminal domain of the alpha subunit of the RNAP.
The C-terminal region is essential for structural folding and for interaction with SpxH/YjbH (PubMed:24942655). A conformational change during oxidation of Spx to the disulfide form likely alters the structure of Spx alpha helix alpha4, which contains residues that function in transcriptional activation and Spx/RNAP-promoter interaction (PubMed:20084284).
Transcribed from at least five promoters located in the yjbC regulatory region or in the yjbC-spx intergenic region (PubMed:17158660, PubMed:29271514). Induced by heat, salt, ethanol and disulfide stress and also by phosphate limitation (PubMed:11544224, PubMed:14597697, PubMed:24417481). Induced by cell wall stress but not by membrane stress (PubMed:29271514). Transcribed under partial control of SigM ECF sigma factor (PubMed:17434969, PubMed:29271514). Repressed by YodB and PerR. YodB protects a region that includes the P3 -10 and -35 regions, while PerR binds to a region downstream of the P3 transcriptional start site (PubMed:17158660).
Under non-stress conditions, Spx is degraded by ClpXP and, to a lesser extent, by ClpCP (PubMed:12057962, PubMed:12642660, PubMed:19074380). Efficient dedradation by ClpXP requires the adapter protein SpxH/YjbH (PubMed:17908206, PubMed:19074380). Binding to SpxH/YjbH reduces the overall conformational flexibility of Spx and stabilizes the C-terminal ClpX recognition region of Spx (PubMed:30982633). In addition, activity is modulated by the formation of a disulfide bound within the N-terminal Cys-X-X-Cys (CXXC) motif, which is required for the transcriptional activation of trxA and trxB, or for the activation of msrAB operon expression following paraquat oxidative stress (PubMed:15659166, PubMed:18662407). However, it seems that formation of the disulfide bound is not essential for induction of all Spx-controlled genes, as for example the case of BSH biosynthesis genes (PubMed:23894131). Similarly, induction of the Spx regulon during cell wall stress is not accompanied by oxidation of the disulfide switch, but requires Spx stabilization by the anti-adapter protein SpxO/YirB (PubMed:29271514, PubMed:30001325).
Cells lacking this gene retains about 40% of the capacity to hydrolyze linear arabinan compared to the wild-type.
Induced by arabinose and arabina,n and repressed by glucose.
Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the internal cleavage of alpha-(1->5)-L-arabinofuranosyl residues of linear 1,5-alpha-L-arabinan and of branched sugar beet arabinan. It displays no activity against heavily substituted arabinans or a range of other polysaccharides (larch wood arabinogalactan, wheat arabinoxylan and p-nitrophenyl-alpha-L-arabinofuranoside). The enzyme activity is progressively reduced as alpha-(1->5)-chains become shorter or more highly substituted.
A master regulator required for the expression of late competence genes including comC, comE, comG and the bdbDC operon (PubMed:8196543, PubMed:7783616, PubMed:11744713, PubMed:11918817, PubMed:11948146). Receives signals from SrfA, and possibly other regulatory COM genes, and transduces these signals to the late COM genes (PubMed:8196543, PubMed:7783616). Represses transcription of rok (PubMed:11849533). May repress expression of a few genes (PubMed:7783616).
Expressed in cells competent for DNA transformation; that is 5-10% of the population (PubMed:11918817).
Positively regulates its own expression (PubMed:7783616). Expressed only in glucose-based minimal medium during the transition to stationary phase (PubMed:8196543). Expression is initiated at the time of transition to the post-exponential state, and exclusively in competence-stimulating medium. Repressed by AbrB and Rok (PubMed:11849533).
Transformation deficient (PubMed:8196543). Loss of expression of at least 165 genes (PubMed:11918817, PubMed:11948146).
Was initially thought to be two separate ORFs named yhcO and yhcP.
Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc.
Belongs to the globin family. Two-domain flavohemoproteins subfamily.
Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
By nitric oxide, nitrite, and under oxygen-limited conditions.
Consists of two distinct domains; an N-terminal heme-containing oxygen-binding domain and a C-terminal reductase domain with binding sites for FAD and NAD(P)H.
In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.
Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the bacterium from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress (By similarity).
Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the bacterium from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress.
In the presence of glutamate in the medium, the expression is reduced five-fold, at high potassium concentration (5 mM) (PubMed:33481774). In the absence of glutamate, expression does not respond to the supply of potassium (PubMed:33481774).
Loss of the gene confers resistance to both serine and its toxic analog serine hydroxamate (PubMed:32743959). Deletion mutant is still able to transport serine, but the deletion of the three permease-encoding genes aimA (ybeC), ybxG and bcaP results in an unprecedented resistance to serine up to 100 mM (PubMed:32743959).
Major glutamate and serine transporter (PubMed:32743959, PubMed:33481774). Cannot transport threonine (PubMed:32743959). AimA is the major glutamate transporter under standard growth conditions when glutamate is not limiting in the medium (PubMed:33481774).
Interacts with cognate immunity protein YobK but not with non-cognate putative immunity protein YezG. The interaction inhibits the toxic activity of YobL.
Toxic component of one of 6 LXG toxin-immunity modules in this strain. They promote kin selection, mediate competition in biofilms, and drive spatial segregation of different strains, indicating that LXG toxins may help avoid warfare between strains in biofilms. Mediates intercellular competition during biofilm formation; disruption of the operon disadvantages the bacteria, but overexpression of the cognate immunity protein restores growth in competition with wild-type. Overexpression alone in situ causes growth arrest but not cell lysis, a large decrease in chromosomal DNA content and the production of anucleate cells. No effect is seen on rRNA. Co-overexpression with cognate immunity protein YobK does not cause growth arrest. The toxic effect is dependent on the epsA and tapA operons which are required for biofilm formation.
Was originally thought to be an RNase; when the C-terminus (residues 449-600) is expressed in E.coli it has RNase, not DNase activity, and inhibits growth upon expression in E.coli. In vitro RNase activity and in vivo growth inhibition are neutralized by cognate immunity protein YobK, but not by immunity proteins specific to other LXG toxins. Mutation of His-562 to Ala leads to loss of growth inhibition and RNase activity in E.coli.
Homodimer. Interacts with WalK and YycH.
Induction of WalR-dependent gene expression. Cell wall defect.
Together with YycH, regulates the activity of the two-component system WalR/WalK.
Cells fail to secrete PGA into the medium.
Required for PGA (gamma-polyglutamic acid) biosynthesis.
Aspartyl-phosphate phosphatase which specifically dephosphorylates the sporulation transcription factor Spo0A-P and negatively regulates the sporulation initiation pathway in order to control the proper timing of sporulation.
During exponential phase and in conditions antithetical to sporulation.
Positive regulator of the licABCH operon.
The regulatory activity of LicR is modulated by phosphorylation and dephosphorylation of the various LicR domains. It becomes activated via phosphoryl group transfer from PEP, EI and HPr on the two conserved histidine residues in the PRD 2 domain, whereas phosphorylation of the EIIA-like domain on His-559 by the PTS EIIB component LicB inactivates LicR (By similarity).
Belongs to the inositol monophosphatase superfamily.
Hydrolyzes myo-inositol monophosphate. Catalyzes the dephosphorylation of GMP and IMP.
No visible phenotype during 5 hours of growth, decreased resistance to oxidative stress caused by diamide.
Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.
Disruption of the gene causes a 10-fold reduction in the efficiency of sporulation. Mutants divide asymmetrically but fail to complete engulfment of the forespore by the mother cell.
Catalyzes the phosphorylation of riboflavin to FMN followed by the adenylation of FMN to FAD.
In the N-terminal section; belongs to the site-specific recombinase resolvase family.
Putative site-specific recombinase having a very important role in sporulation. It probably plays a role in the recombination of SpoIIIC and SpoIVCB to form sigma K factor.
Part of the high-affinity ABC transporter complex ZnuABC involved in zinc import (Probable). Responsible for energy coupling to the transport system (By similarity). ZnuABC-mediated zinc transport is required for comF expression and competence development.
Has multiple catalytic activities. Apart from catalyzing the oxidation of (+)-tartrate to oxaloglycolate, also converts meso-tartrate to D-glycerate and catalyzes the oxidative decarboxylation of D-malate to pyruvate.
Belongs to the type-I 3-dehydroquinase family.
Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.
Involved in the regulation of horizontal gene transfer through the integrative and conjugative element ICEBs1. Required for degradation of the ICEBs1 repressor protein ImmR/YdcN.
Belongs to the phosphoenolpyruvate carboxykinase (ATP) family.
Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.
Member of the two-component regulatory system YvcQ/YvcP.
Belongs to the EIF-2B alpha/beta/delta subunits family. MtnA subfamily.
Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Was originally thought to be a translation initiation factor.
Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
In the C-terminal section; belongs to the transferase hexapeptide repeat family.
In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family.
Belongs to the universal ribosomal protein uS15 family.
Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it helps nucleate assembly of the platform of the 30S subunit by binding and bridging several RNA helices of the 16S rRNA.
Part of the 30S ribosomal subunit (PubMed:30126986). Forms a bridge to the 50S subunit in the 70S ribosome, contacting the 23S rRNA (By similarity).
Part of the 30S ribosomal subunit. Forms a bridge to the 50S subunit in the 70S ribosome, contacting the 23S rRNA.
Involved in potassium and divalent cation transport. Enhances the transport activity of the cation/potassium transporter CzcD.
This protein is a multifunctional enzyme, able to activate and polymerize the amino acid Ile as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The activation sites for this amino acid consist of individual domains.
Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Belongs to the binding-protein-dependent transport system permease family. AraH/RbsC subfamily.
Part of the ABC transporter complex RbsABC involved in ribose import. Probably responsible for the translocation of the substrate across the membrane.
Although the bacteria accumulates coproporphyrinogen-III when the gene is disrupted, no oxygen-independent coproporphyrinogen-III oxidase activity or complementation have been shown. The exact role of this protein is unknown.
Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily.
Cells lacking this gene accumulate coproporphyrinogen-III under anaerobic conditions, but show normal growth under aerobic and anaerobic conditions.
Might carry two S-adenosyl-L-methionine binding sites with only one binding to the iron-sulfur cluster.
Part of the lepA-hemN operon; there is a strong transcriptional terminator between the 2 genes, this gene is much less transcribed. There can be further readthough downstream (PubMed:8757728, PubMed:9371469). Induced under anaerobic conditions by resDE, fnr and arfM.
Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently (By similarity). Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine (By similarity).
Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Belongs to the bacterial ribosomal protein bS6 family.
Binds together with bS18 to 16S ribosomal RNA.
Deletion of the gene confers a weak resistance to growth inhibition by serine (PubMed:32743959). The deletion of the three permease-encoding genes aimA (ybeC), ybxG and bcaP results in an unprecedented resistance to serine up to 100 mM (PubMed:32743959).
Probable threonine transporter (PubMed:32743959). Is also active as a minor serine permease (PubMed:32743959).
Cells lacking this gene show normal growth on inosine as the purine source, normal hypoxanthine-guanine phosphoribosyltransferase activity, and are resistant to azaguanine.
Expression is regulated by both purR and xptR regulons. Negatively regulated by hypoxanthine and guanine.
Involved in the uptake of the purine bases hypoxanthine and guanine.
Little effect on the percentage of cells with partition defects and no change in sporulation frequency. However, yopP disruption strongly increases the extent of the partitioning defects seen in codV mutant strains (by about two-fold) and, to a lesser extent, those seen in ripX and dif mutant strains.
Probable recombinase that does not seem to have a role in chromosome dimer resolution per se but rather may have some facilitative role during chromosome partitioning in general.
Not essential for growth; loss of trans-translation (PubMed:11395451). Significantly decreased growth at 16 and 52 degrees Celsius (PubMed:17369301).
Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation (By similarity). Required for trans-translation (PubMed:11395451). Probably required for sporulation; deletion of the gene for tmRNA impairs sporulation via its effect on trans-translation, and as smpB is required for trans-translation under non-stress conditions, it is also probably required during sporulation (PubMed:18673456).
Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation.
Belongs to the TPP enzyme family. MenD subfamily.
Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
Used to include what was called 'MenCF'.
Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. It decarboxylates selectively the malonyl group attached on the acyl-carrier-protein AcpK (Mal-AcpK).
Belongs to the cation diffusion facilitator (CDF) transporter (TC 2.A.4) family. SLC30A subfamily.
Involved in divalent cation and potassium homeostasis in the cell. Catalyzes the active efflux of zinc, cadmium and cobalt, in exchange for potassium and H(+) ions.
Belongs to the thiamine-monophosphate kinase family.
Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.
Reaction mechanism of ThiL seems to utilize a direct, inline transfer of the gamma-phosphate of ATP to TMP rather than a phosphorylated enzyme intermediate.
Mutations that block the onset of sporulation in Bacillus subtilis are called stage 0 mutations, or spo0 mutations, and at least eight genetic loci have been identified in which a mutation can result in a stage 0 phenotype. Stage 0 mutants lack the ability to form the asymmetric septum characteristic of the initiation of the sporulation process. In addition, these mutations have many pleiotropic effects on the synthesis of a variety of transcripts by minor forms of RNA polymerase in this organism.
Probably degraded by FtsH, the last 14 residues seem to form the FtsH recognition site.
Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA).
Belongs to the MIP/aquaporin (TC 1.A.8) family.
Mediates glycerol diffusion across the cytoplasmic membrane via a pore-type mechanism.
Belongs to the bacterial sugar transferase family.
Acetylates the N-terminal alanine of ribosomal protein S5.
Belongs to the acetyltransferase family. RimJ subfamily.
Deletion of the gene increases the expression of the ComA-dependent genes rapA and rapC itself.
Homodimer (PubMed:12950917). Interacts specifically with the C-terminal DNA-binding domain of ComA (PubMed:12950917, PubMed:15968044). Interacts with CSF (PubMed:12950917).
Inhibited by the competence and sporulation stimulating factor (CSF), encoded by phrC, which prevents RapC-ComA interaction.
Involved in the regulation of genetic competence development (PubMed:12950917, PubMed:16816200). Inhibits the activity of ComA, a transcriptional factor that regulates the development of genetic competence (PubMed:12950917, PubMed:16816200). Acts by binding to ComA, independently of its phosphorylation state, leading to the inhibition of ComA DNA-binding activity (PubMed:12950917). Does not dephosphorylate phospho-ComA and does not affect the phosphorylation level of the ComP-ComA system (PubMed:12950917).
Part of the rapC-phrC operon, which is controlled by the P1 promoter (PubMed:10464187). Transcription from the P1 promoter is activated by high cell density through the phosphorylated form of ComA (PubMed:10464187). RapC is part of an autoregulatory loop, and it negatively regulates its own expression (PubMed:10464187).
Component of the menaquinol:cytochrome c reductase complex.
Negatively regulated by IolR. Induced by inositol.
When iolT is inactivated, inositol uptake is almost abolished even though iolF is active.
Deletion mutant requires hemin for growth.
Involved in coproporphyrin-dependent heme b biosynthesis (PubMed:25646457, PubMed:25908396). Catalyzes the insertion of ferrous iron into coproporphyrin III to form Fe-coproporphyrin III (PubMed:25646457, PubMed:25908396). It can also insert iron into protoporphyrin IX (PubMed:1459957, PubMed:8119288, PubMed:21052751, PubMed:25646457). Has weaker activity with 2,4 disulfonate, deuteroporphyrin and 2,4 hydroxyethyl (PubMed:25646457, PubMed:12761666). In vitro, can also use Zn(2+) or Cu(2+) (PubMed:8119288, PubMed:16140324, PubMed:21052751, PubMed:12761666).
Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the insertion of ferrous iron into coproporphyrin III to form Fe-coproporphyrin III.
Monomer (PubMed:8119288). Interacts with frataxin/Fra (PubMed:25826316).
Stimulated by Mg(2+) (PubMed:12761666). Inhibited by Cd(2+) (PubMed:12761666). Inhibited by N-methylmesoporphyrin (N-MeMP) and 2,4-disulfonic acid deuteroporphyrin IX (dSDP) (PubMed:10704318, PubMed:16140324, PubMed:18423489).
Probably functions as a manganese efflux pump.
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln) (By similarity).
Induced by glucose when readily available sources of nitrogen, such as ammonia or glutamine, are scarce.
Transcriptional repressor of the kip gene-containing operon.
Belongs to the universal ribosomal protein uL14 family.
Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome.
Part of the 50S ribosomal subunit (PubMed:30126986). Forms a cluster with proteins L3 and L19. In the 70S ribosome, L14 and L19 interact and together make contacts with the 16S rRNA in bridges B5 and B8 (By similarity).
Part of the 50S ribosomal subunit. Forms a cluster with proteins L3 and L19. In the 70S ribosome, L14 and L19 interact and together make contacts with the 16S rRNA in bridges B5 and B8.
Belongs to the oxidase-dependent Fe transporter (OFeT) (TC 9.A.10.1) family.
Part of the iron transporter system efeUOB/M involved in iron import (Probable) (PubMed:23764491). Mediates the uptake of Fe(3+) ions, delivered by EfeM, across the cell membrane (PubMed:23764491).
Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family.
Unknown, does not resemble components of ABC transporters.
Belongs to the bacterial ribosomal protein bS1 family.
Constitutively transcribed in minimal and rich medium, in exponential and stationary phase. May not be transcribed with the upstream gene (cmk), there is a probable transcription terminator between the 2 genes.
No visible effect on growth (PubMed:7704259). Decreased sporulation at 37 and 47 degrees Celsius (PubMed:14586115).
Plays a role in sporulation (PubMed:14586115). Cannot be expressed in wild-type E.coli, does not complement an E.coli rpsA deletion (PubMed:7704259).
Belongs to the bacterial ribosomal protein bL19 family.
This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site.
Transcriptional regulator with a possible role in regulation of amino acid metabolism. Plays a role in the growth phase transition.
Belongs to the enoyl-CoA hydratase/isomerase family. MenB subfamily.
Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA).
The hydrogencarbonate anion plays the same catalytic role (proton acceptor) as the side-chain carboxylate group of the essential 'Asp-185' found in actinobacteria, archaea, bacteroidetes, and deltaproteobacteria.
Required for production of the bacteriocin subtilosin. Could catalyze some step in the processing of presubtilosin.
A putative methylase, recognizes the double-stranded sequence 5'-GGCC-3', methylates C-?. There is no known cognate restriction enzyme.
Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.
Belongs to the pyruvate, phosphate/water dikinase regulatory protein family. PDRP subfamily.
Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation.
Lowers the level of gapB and pckA transcription threefold under both glycolytic and gluconeogenic conditions.
Binds a DNA inverted repeat of the yfmPO operon.
Repressor of the yfmOP operon. A mutation in yfmP leads to overexpression of yfmO, probably causing a decrease in cellular copper that is eventually responsible for a reduced copper induction of copZA.
YfmP is autoregulated. There is no induction with copper or other metals.
Constitutively expressed throughout the growth phase.
Involved in cell division and chromosome segregation (PubMed:24097947, PubMed:29378890). May influence the activity of FtsZ (PubMed:24097947). Binds DNA, but does not seem to function as a transcription factor (PubMed:24097947).
Involved in cell division and chromosome segregation.
Mutant grows slower and cells are longer compared to the wild-type strain. Mutation has a relatively mild effect on the sporulation. Mutant is sensitive to reduced FtsZ concentrations. Deletion of the gene in a zapA mutant background results in very filamentous cells that are blocked in proper Z-ring formation (PubMed:24097947). Mutant shows increased internucleoid distances (PubMed:29378890).
Not essential for growth on minimal or rich media.
Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine (PubMed:23282011). The other is coordinated via 3 cysteines and maybe direct contact with the SkfA precursor (Probable).
Catalyzes the formation of the thioether bond required for production of the sporulation killing factor (SKF) from SkfA (PubMed:12817086). Forms the cysteine-methionine thioether bond found in SKF; the acceptor amino acid can be hydrophobic, aromatic or a small hydrophilic amino acid but not a larger hydrophilic amino acid, i.e. Met=Ala, Phe, Leu, Tyr>Asn, Ser>>Gln, Glu, Lys (PubMed:23282011). The relative position of Cys and Met in the substrate cannot be inverted, in vitro the thioether bond cannot be made in the absence of the SkfA propeptide, suggesting this is the first reaction in SKF maturation (PubMed:23282011). In vitro, in the absence of a second substrate, cleaves S-adenosyl-L-methionine into Met and 5'-dA (PubMed:23282011).
Belongs to the type II topoisomerase GyrA/ParC subunit family. ParC type 2 subfamily.
Mutants have spores sensitive to heat, lysozyme and chloroform, and in which the cortex is absent.
StoA and ykvU are cotranscribed under the control of sigma E.
Thiol-disulfide oxidoreductase with a reductive function, involved in spore cortex synthesis. It could be involved either in breaking disulfide bonds in cortex components or in proteins that are important for cortex synthesis, or in thiol/disulfide bond interchange.
Belongs to the glucose-1-phosphate cytidylyltransferase family.
Catalyzes the transfer of a CMP moiety from CTP to glucose 1-phosphate.
In the phosphorylated form it could act as an anti-anti-sigma factor that counteracts SpoIIAB and thus releases sigma f from inhibition.
Phosphorylated by SpoIIAB on a serine residue.
Belongs to the fluoride channel Fluc/FEX (TC 1.A.43) family.
Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Na(+) is not transported, but it plays an essential structural role and its presence is essential for fluoride channel function.
Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. TrmE GTPase family.
Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Decreases expression from the aprE promoter.
Part of the rapH-phrH operon, which is transcribed from the SigA-driven rapH promoter (PubMed:21908671). phrH is also transcribed from a putative SigA-driven promoter embedded within the rapH gene sequence (PubMed:21908671).
Signaling molecule involved the regulation of both sporulation and competence (PubMed:17581123, PubMed:21908671). Secreted during production, but the mature peptide acts intracellularly, indicating that it needs to be imported into the cell to function (PubMed:21908671). Acts by inhibiting RapH activity (PubMed:17581123, PubMed:21908671). Can inhibit both RapH activities, the dephosphorylation of Spo0F and the sequestration of ComA (PubMed:21908671).
Binds cyclic di-AMP (c-di-AMP), which may regulate the activity.
Required for activity of the potassium/proton antiporter KhtU (PubMed:14987767, PubMed:17679694). Involved in protection of the cell from methylglyoxal, a toxic by-product of glycolysis (PubMed:24330391).
The transporter is composed of the integral membrane protein KhtU and the regulatory protein KhtT.
Binds 10 calcium ions (PubMed:16682770, PubMed:17449691, PubMed:19193638). The calcium may have a structural role. Requires calcium or manganese for activity (PubMed:16682770, PubMed:17449691).
Pectinolytic enzyme that degrades type I rhamnogalacturonan from plant cell walls and releases oligosaccharide products (PubMed:16682770, PubMed:17449691, PubMed:19193638). Degrades rhamnogalacturonan, polygalacturonic acid, pectic acid and pectin (PubMed:16682770, PubMed:17449691).
Rhamnose is bound near the active site, but there are also additional rhamnose-binding sites far away from the active site, which possibly function as a carbohydrate-binding region.
Acts as a magnesium transporter (PubMed:24415722). MgtE is the dominant transporter under rich-medium growth conditions, and it may provide the primary route of magnesium import in B.subtilis, while the other putative transport proteins are likely to be utilized for more-specialized growth conditions (PubMed:24415722).
Belongs to the SLC41A transporter family.
Deletion of the gene results in a significant growth defect under rich-medium growth conditions and in strong dependency on supplemental extracellular magnesium.
Expression is under strict control of the medium composition. Induced by citrate, via the two-component regulatory system CitT/CitS. Repressed by rapidly metabolized carbon sources like glucose, glycerol and inositol, via the carbon catabolite repression system. Is also repressed by succinate and glutamate, albeit to a lesser extent.
Proton motive force-driven secondary transporter that mediates the transport of citrate complexed to Mg(2+). Cotransports at least two protons per Mg(2+)-citrate complex. Can also transport citrate in complex with Ni(2+), Mn(2+), Co(2+), and Zn(2+).
The uptake activity increases with increasing Mg(2+) concentrations. Inhibited by FCCP, TCC and nigericin.
5'-3' exonuclease acting preferentially on double-stranded DNA.
Phe-155 is present instead of the conserved Tyr which is expected to be an active site residue.
Cells lacking this gene cannot grow on either mannitol or glucitol as sole carbon source.
Positively regulates the expression of the mtlAFD operon involved in the uptake and catabolism of mannitol.
The regulatory activity of MtlR is modulated by phosphorylation and dephosphorylation of the various MtlR domains. It becomes activated via phosphoryl group transfer from PEP, EI and HPr on the two conserved histidine residues in the PRD 2 domain, whereas phosphorylation of the EIIA-like domain on His-599 by the PTS EIIB-Mtl domain of MtlA inactivates MtlR (By similarity).
Cells lacking this gene show a reduction in transformation efficiency and in fraction of cells that express competence.
Displays ATPase and GTPase activities. Can also hydrolyze pNPP. May affect the expression of competence via the phosphorylation of a cellular component.
Belongs to the alkaline phosphatase family.
Negatively regulates the transcription of the opuC operon. In the absence of GbsR, is also a negative regulator of the opuB operon. Binds to an inverted repeat in the promoter region of the operons.
Proteolytically cleaved in the N-terminus by SpoIIGA to yield the active peptide.
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is responsible for the expression of sporulation specific genes.
Belongs to the bacterial ribosomal protein bL32 family.
Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Homohexamer (By similarity). Interacts with FloT at midcell (Probable) (PubMed:23651456, PubMed:26297017). Interacts with FloA at midcell (Probable). Another study shows only minor colocalization with FloA or FloT (PubMed:27362352).
In the C-terminal section; belongs to the peptidase M41 family.
In the central section; belongs to the AAA ATPase family.
In vitro partially degrades Spo0E, the phosphatase that acts on Spo0A-P. Recognition requires the last 14 residues of Spo0E (PubMed:19332814). Its stabile accumulation requires FlotA and Flot (PubMed:24222488). May degrade EzrA (Probable).
Induced by osmotic shock (0.8 M NaCl) and by heat shock (52 degrees Celsius).
Necessary only for stage 0 of sporulation.
Required for expression of the stage 0 sporulation gene Spo0A, as well as for a normal heat or osmotic stress response, cells lacking this gene grow as long filaments and tend to lyse upon entry into stationary phase. Secretion of some extracellular proteins is also reduced (PubMed:9076729). Loss of biofilm formation (PubMed:22882210).
4000-fold reduction in sporulation efficiency.
Required during sporulation for activation of sigma factor SpoIIIG/SigG after engulfment is completed in the prespore. Overexpression in the absence of SpoIIIJ is synthetically lethal.
Part of the binding-protein-dependent transport system YqgGHIJK. Probably responsible for the translocation of the substrate across the membrane (By similarity).
Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Induced early in sporulation under the control of sigma-H. Interferes with sporulation at an early stage. Seems to play a positive role in allowing cells to progress beyond stage V of sporulation.
Homodimer in vitro. In vivo, may be a part of an ABC transporter complex which is composed of two ATP-binding proteins (YkoD), two transmembrane proteins (YkoC and YkoE) and a solute-binding protein (YkoF) (Probable).
Part of the ABC transporter complex YkoCDEF that could transport hydroxymethylpyrimidine (HMP) and/or thiamine. Could also transport other HMP-containing products. Binds thiamine via its HMP moiety.
By several proteins including Spo0A, Spo0H, Sin, AbrB, DegS, DegU, ComA, ComB and ComK.
Plays a role in type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino group of the newly exposed N-terminal phenylalanine. Substrates include proteins required for biogenesis of the type II general secretory apparatus.
Zinc is required for the N-terminal methylation of the mature pilin, but not for signal peptide cleavage.
Mutant shows a reduced rate of spore germination in L-alanine.
Probably contributes, directly or indirectly, to early events in germination.
Very low induction by mitomycin C and UV irradiation; probably a member of the yhaONM operon.
Involved in the catabolism of branched amino acids such as leucine.
Heptamer of 7 subunits arranged in a ring. Interacts with the chaperonin GroEL.
Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel.
Deletion of the gene leads to aberrantly formed spores (PubMed:8755877). Mutant spores release their dipicolinic acid (DPA) via germinant receptor (GR)-dependent germination more rapidly than wild-type spores. Spores are also more sensitive to UV radiation and outgrow slowly (PubMed:22522895).
Homotetramer (PubMed:18996130) (Probable). Two monomers dimerize via their N-terminal swapped-hairpin domains. These dimers further associate into tetramers through helical interactions between their C-terminal GAF-like domains (PubMed:18996130).
The N-terminal domain binds DNA non-specifically and the C-terminal GAF-like domain is crucial to its correct folding and function. The non-specific DNA-binding activity of the N-terminal domain is modulated by the C-terminal domain, which perhaps in combination with another unknown factor, confers activity and specificity.
Transcriptional factor that regulates positively or negatively the expression of a large number of forespore-specific sigma G-dependent genes. May provide a mechanism of feedback control that is important for forespore development (PubMed:8755877). SpoVT levels during spore formation have a major impact on the germination and the resistance of the resultant spores (PubMed:22522895).
Cells lacking this gene do not lose the ability to grow on 2SC as the sulfur source because of the presence of other deacetylases that can compensate for scmP (yxeP) deficiency. In a triple mutant lacking this gene, ytnL and yhaA, the levels of NAC highly increases after addition of 2SC.
Probably catalyzes the deacetylation of N-acetylcysteine (NAC) to acetate and cysteine. Is involved in a S-(2-succino)cysteine (2SC) degradation pathway that allows B.subtilis to grow on 2SC as a sole sulfur source, via its metabolization to cysteine.
Regulates sporulation prior to stage II. Positively controls the competence regulator ComK at a post-transcriptional level. May modulate the translation, stability or activity of ComS. May work together with YmcA to regulate community development.
Binds 2 heme b groups non-covalently with two histidine residues as axial ligands.
Binds one heme group covalently by a single cysteine link with no axial amino acid ligand.
This cytochrome b is similar to other bacterial and plant chloroplast cytochrome b6 proteins in binding one of three hemes with a single thioether bond.
Transaminates branched-chain amino acids and ketoglutarate.
Belongs to the SMC family. SbcC subfamily.
Performs the first step in the degradation of the flavonoid quercetin by a dioxygenase reaction. The enzyme catalyzes the cleavage of the O-heteroaromatic ring of the flavonol quercetin yielding the depside 2-protocatechuoyl-phloroglucinol carboxylic acid and carbon monoxide. This involves the remarkable dioxygenolytic cleavage of two carbon-carbon bonds.
Acetylates the N-terminal alanine of ribosomal protein S18.
Acetylates the N-terminal alanine of ribosomal protein bS18.
Belongs to the acetyltransferase family. RimI subfamily.
Belongs to the PgpH phosphodiesterase family.
In strain 168 grown in minimal medium and glutamate, 3.5-fold increase in c-di-AMP levels, while a double pgpH-gdpP mutant has 4.2-fold increased levels of in c-di-AMP; double mutants die on solid medium after 2 days (PubMed:26240071).
Probably has phosphodiesterase (PDE) activity against cyclic-di-AMP (c-di-AMP); may be the major c-di-AMP PDE in the cell (PubMed:26240071). In B.subtilis c-di-AMP is a second messenger that mediates growth, DNA repair and cell wall homeostasis; it is toxic when present in excess (PubMed:26240071).
Mediates uptake of L-cystine, the oxidized form of L-cysteine. Although it is more specific for L-cystine, it could also transport a much broader range of amino acids and sulfur compounds including S-methylcysteine.
More strongly expressed in the presence of methionine than in presence of sulfate. Strongly inhibited by seleno-DL-cystine.
Intracellular choline sensor. Binding to choline induces conformational changes and relieves the repressing effects of GbsR on expression.
Negatively regulates the expression of the gbsAB and opuB operons. Required to control expression of these genes in response to choline availability. Also required to down-regulate glycine betaine production once cellular adjustment to high osmolarity has been achieved.
Negatively regulated by both YxlD and YxlE.
Positively autoregulated. Induced upon nitrogen starvation.
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Positively regulates the expression of the sigY-yxlCDEFG operon upon nitrogen starvation. Also positively regulates ybgB.
Catalyzes the conversion of cystathionine to cysteine, and homocysteine to sulfide.
Belongs to the CPA3 antiporters (TC 2.A.63) subunit D family.
Catalyzes the hydrolysis of aryl-phospho-beta-D-glucosides such as 4-methylumbelliferyl-phospho-beta-D-glucopyranoside (MUG-P), phosphoarbutin and phosphosalicin. Plays a major role in the utilization of arbutin or salicin as the sole carbon source. BglA and BglH are the major proteins contributing to hydrolysis of MUG-P by extracts of late-exponential-phase or stationary-phase B.subtilis cells.
Expressed during stationary-phase and exponential-phase of growth.
Up-regulated by the aryl-beta-D-glucoside salicin.
Mutation abolishes swarming motility, reduces swimming speed and torque of tethered flagella. It does not affect flagellar assembly, flagellar number or surfactant production.
Required for swarming motility. Increases flagellar power, probably via the flagellar stator components MotA and MotB.
Belongs to the phosphohexose mutase family.
Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate (By similarity). Glucosamine-1-phosphate is used for cell wall biosynthesis (Probable).
Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
Homodimer, may form a complex with CdaA.
Catalyzes the interconversion between glucose-6-phosphate and alpha-glucose-1-phosphate. This is the first step in the biosynthesis of diglucosyl-diacylglycerol (Glc2-DAG), i.e. the predominant glycolipid found in B.subtilis membrane, which is also used as a membrane anchor for lipoteichoic acid (LTA). Has a role in the biosynthesis of all phosphate-containing envelope polymers, since glucose-1-phosphate is the precursor of UDP-glucose, which serves as a glucosyl donor not only for the biosynthesis of LTA but also for wall teichoic acids (WTAs). Is required for biofilm formation. This is likely due to another role of UDP-glucose, which might also act as a metabolic signal regulating biofilm formation or may be involved in some unknown biosynthetic pathway essential for biofilm formation, e.g. the synthesis of an exopolysaccharide.
Part of the ABC transporter complex FhuBGCD involved in iron(3+)-hydroxamate import. Responsible for the translocation of the substrate across the membrane (By similarity).
May play a role in the degradation of rhamnogalacturonan derived from plant cell walls.
No chromogen 5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside (X-Gal) hydrolyzation.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. LepA subfamily.
Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner.
Belongs to the acetylglutamate kinase family. ArgB subfamily.
Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Member of the two-component regulatory system ResD/ResE. Required for the expression of resA, ctaA, qcrABC and fnr; activation role in global regulation of aerobic and anaerobic respiration.
Belongs to the inorganic phosphate transporter (PiT) (TC 2.A.20) family.
Belongs to the transketolase family. DXPS subfamily.
Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
Required for resistance to linearmycins, a family of antibiotic-specialized metabolites produced by some streptomycetes (PubMed:26647299, PubMed:28461449). Part of the ABC transporter complex LnrLMN that probably facilitates linearmycin removal from the membrane. Responsible for energy coupling to the transport system (PubMed:28461449). Also mediates KinC-dependent biofilm morphology (PubMed:28461449).
Necessary for insertion of copper into the active site of cytochrome c oxidase. May play a role in copper homeostasis or redox signaling.
Protein phosphatase that dephosphorylates PrkC and EF-G (elongation factor G, fusA). prpC and prkC are cotranscribed, which suggests that they form a functional couple in vivo, PrpC's primary role being possibly to counter the action of PrkC. May be involved in sporulation and biofilm formation. Does not seem to be involved in stress response. Dephosphorylates phosphorylated CgsA, EF-Tu and YezB (PubMed:19246764).
Disulfide cross-linked either to itself or to CotZ.
Belongs to the bacteriocin class V family.
Has bacteriocidal activity against some Gram-positive bacteria such as Listeria, some species of Bacillus and E.faecium (PubMed:10572140, PubMed:19633086, PubMed:3936839). A single mutation (Thr-14-Ile) confers hemolytic activity against rabbit and human blood (PubMed:19633086).
PubMed:3936839 sequence does not report residues in positions 30 and 39 probably due to their modification, and reports a cyclic permutation of the peptide sequence.
The production of subtilosin A begins at the end of vegetative growth and finishes before spore formation.
This sactipeptide undergoes unique processing steps that include proteolytic cleavage after Glu-8, and covalent linkage of the alpha-amino of Asn-9 with the carboxyl of Gly-43 to form a cyclopeptide (PubMed:12696888, PubMed:22366720). Thioether cross-links are formed between cysteines and the alpha-carbons of other amino acids, Cys-12 to Phe-39, Cys-15 to Thr-36, and Cys-21 to Phe-30 (PubMed:12696888, PubMed:22366720). In forming these cross-links, Thr-36 and Phe-39 are converted to D-amino acids (PubMed:12696888). Propeptide cleavage and cyclopeptide formation only occur after all 3 thioether cross-links are formed (PubMed:22366720).
Induced by succinate and fumarate. Expression of dctA requires the DctB, DctS and DctR proteins and is decreased in the presence of malate.
Responsible for the transport of dicarboxylates such as succinate, fumarate, and malate across the membrane.
Responsible for the transport of succinate and fumarate, but not malate, across the membrane.
Belongs to the purine/pyrimidine phosphoribosyltransferase family.
Purine salvage pathway enzyme that catalyzes the transfer of the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to the N9 position of the 6-oxopurines hypoxanthine and guanine to form the corresponding ribonucleotides IMP (inosine 5'-monophosphate) and GMP (guanosine 5'-monophosphate), with the release of PPi.
Could be expressed in the forespore during sporulation.
Expression is probably sigma F-dependent.
Could be held inactive when BofA provides a fourth zinc ligand, preventing access to a water molecule and the sequence of pro sigma-K.
Forms a complex with SpoIVFA and BofA localized in the mother-cell membrane surrounding the forespore.
Implicated in the coupling of mother cell to forespore gene expression. Required for spore formation. Processes the pro-sigma K factor.
Transcribed during the stage II, but not required until stage IV of sporulation.
Immunity component of one of 6 LXG toxin-immunity modules in this strain. They promote kin selection, mediate competition in biofilms, and drive spatial segregation of different strains, indicating that LXG toxins may help avoid warfare between strains in biofilms. Mediates intercellular competition during biofilm formation; disruption of the operon disadvantages the bacteria, but overexpression of the cognate immunity protein restores growth in competition with wild-type. In situ neutralizes the toxic effect of cognate toxin YxiD (PubMed:34280190). Neutralizes the toxic activity of cognate toxin YxiD upon expression in E.coli. Does not have immunity protein activity on other LXG toxins (PubMed:22200572).
Probably interacts with cognate toxin YxiD but not with other non-cognate toxins. The interaction inhibits the toxic activity of YxiD (Probable).
Belongs to the bacterial ribosomal protein bL9 family.
According to PubMed:10714992, cells have an altered coat protein composition; CotT, YeeK, YxeE, CotF, SafA and SpoIVA proteins are present at increased levels and/or exist as precursors. According to PubMed:16751597, cells show no effects on vegetative growth or spore resistance to heat, chloroform or lysozyme. The germination of YabG mutant spores in L-alanine and in a mixture of L-asparagine, D-glucose, D-fructose and potassium chloride was the same as that of the wild-type spores. Heat treatment for 20 minutes at 60 degrees Celsius, which maximally activates the Tgl enzymatic activity, causes cross-linking of GerQ in isolated YabG-deleted spores but not in Tgl/YabG double-mutant spores. Additionally, the germination frequency of the Tgl/YabG double-mutant spores in the presence of L-alanine with or without heat activation at 60 degrees Celsius is lower than that of wild-type spores.
Cleaves the spore coat proteins SpoIVA and SafA. May cooperate with tgl to mediate the temperature-dependent cross-linking of coat proteins like GerQ.
B.subtilis has only one biosynthetic pathway from agmatine to spermidine to produce polyamines.
Belongs to the spermidine/spermine synthase family.
Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
Involved in the cell growth and proliferation. Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine (Probable).
Belongs to the GTP cyclohydrolase I type 2/NIF3 family.
Belongs to the helicase family. RecG subfamily.
Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-DNA) (By similarity).
Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-DNA).
May be a morphogenetic protein that is required for the incorporation of protein CotB into the spore coat.
Belongs to the metal hydrolase YfiT family.
Binds 1 zinc ion per subunit. Is able to bind nickel instead of zinc.
Positively regulated by WalR. Expressed primarily during exponential growth, with levels decreasing rapidly at the beginning of the stationary phase.
Catalyzes the 2,6-dichlorophenolindophenol-dependent cleavage of acetoin into acetate and acetaldehyde. The alpha subunit is probably the catalytic subunit of the enzyme (By similarity).
Cells lacking this gene are unable to utilize acetoin as carbon source.
Strongly induced by acetoin. Transcriptionally up-regulated by AcoR and sigma-L factor. Subject to catabolite repression by glucose, in a CcpA-independent manner.
Belongs to the glycosyl hydrolase 18 family. Chitinase class II subfamily.
Expressed in the mother cell compartment from T2 of sporulation.
Inactivation of the gene does not impair vegetative growth nor prevent the development of resistance to heat, chloroform and lysozyme (PubMed:10419957). According to Kodama et al, the germination of the mutant spores induced by L-alanine is defective. However Chirakkal et al reported that the mutant shows wild-type germination kinetics in L-alanine (PubMed:12177332, PubMed:10419957).
N-acetylglucosaminidase involved in cortex peptidoglycan degradation during germination. Cleaves only partially degraded spore peptidoglycans. Recognizes muramic acid delta-lactam residues specific to spore peptidoglycans.
Was originally thought to have epimerase activity.
Null mutant is very sensitive to manganese.
Probably part of ATP-binding cassette (ABC) transport system MntABCD involved in manganese import (Probable). Binds manganese and delivers it to the membrane permease for translocation into the cytoplasm (Probable).
The complex is probably composed of two ATP-binding proteins (MntB), two transmembrane proteins (MntC and MntD) and a solute-binding protein (MntA) (Probable). Interacts with FloT (PubMed:23651456).
Binds 2 Fe(2+) or Co(2+) ions per subunit.
Part of the bacABCDEF operon responsible for the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin, composed of L-alanine and L-anticapsin. Bacilysin is an irreversible inactivator of the glutaminase domain of glucosamine synthetase (PubMed:15609023, PubMed:20052993). BacB catalyzes the allylic isomerization of the endocyclic-delta(4),delta(8)-7R-dihydro-hydroxyphenylpyruvate (en-H2HPP) to generate a mixture of 3E,7R- and 3Z, 7R-olefins (E/Z ration of 3/1) of the exocyclic-delta(3),delta(5)-dihydro-hydroxyphenylpyruvate (ex-H2HPP) (PubMed:20052993, PubMed:22483065, PubMed:22765234, PubMed:19776011).
Allosterically inhibited by NADP and activated by quinolinic acid. Strongly inhibited by HgCl(2).
Divalent metal ions. Both Ca(2+) and Mn(2+) ions are more effective activators than zinc, cobalt, copper and magnesium ions at low concentrations.
Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP. It can use ATP and other nucleoside triphosphates (GTP, UTP) as well as inorganic polyphosphate (poly(P)) as a source of phosphorus.
Asparagine synthetase involved in sporulation.
Deletion mutant is manganese sensitive and accumulates high levels of intracellular manganese. Effects are exacerbated in a mneP-mneS double mutant.
Primary efflux pump for manganese. May prevent manganese intoxication.
Belongs to the FtsQ/DivIB family. DivIB subfamily.
Cell division protein that may be involved in stabilizing or promoting the assembly of the division complex.
Cell division protein that may be involved in stabilizing or promoting the assembly of the division complex. Plays an essential role in division at high temperatures, maybe by protecting FtsL from degradation or by promoting formation of the FtsL-DivIC complex. May modulate the transpeptidase activity of PBP-2B. Also required for efficient sporulation at all temperatures. Could be directly involved in the engulfment process or be required to form a sporulation septum competent for engulfment. Influences the Spo0J/Soj system of chromosome segregation.
Mutants show a drastic decrease in sporulation efficiency. Polar septation is delayed and less efficient, and the completed septa are thicker than those of the wild type. Mutants are also unable to undergo engulfment.
The extracellular region contains three distinct subdomains: a membrane proximal alpha domain, a central beta domain and an unstructured C-terminal gamma domain. The C-terminal region of the beta domain is critical for interaction with PBP-2B. Contains multiple septal localization epitopes that are located within the transmembrane region and within the extracellular region. These epitopes may represent sites of interaction with other divisomal proteins.
Part of the bacABCDEF operon responsible for the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin, composed of L-alanine and L-anticapsin. Bacilysin is an irreversible inactivator of the glutaminase domain of glucosamine synthetase (PubMed:20052993). Catalyzes the reductive amination of the C2 ketone of tetrahydro-hydroxyphenylpyruvate (H4HPP), with L-Phe as an amino donor, to yield tetrahydrotyrosine (H4Tyr) diastereomer (PubMed:22765234). D-Phe is not an effective amino donor (PubMed:22765234). BacF associated to BacG converts 3E,7R- and 3Z,7R-ex-H2HPP to 2S,4R,7R- and 2S,4S,7R-H4Tyr, respectively. Given that bacilysin has the 2S,4S stereochemistry in its anticapsin moiety, it is likely that the 2S,4S-H4Tyr is the diastereomer used for the biosynthesis (PubMed:22765234).
Activated by phosphorylation; inhibited by dephosphorylation.
Phosphorylated by YwqD and dephosphorylated by YwqE in vitro.
Catalyzes the NADP(+) dependent oxidation of succinate semialdehyde to succinate.
Cells lacking this gene are unable to use GABA as sole nitrogen source (PubMed:12123465). No effect on vanillin degradation (PubMed:26658822).
Expressed from the major gabT promoter and from an additional gabD promoter.
Transcriptionally regulated by GabR in the presence of GABA. Up-regulated under low pH conditions and ethanol. Expression from the gabD promoter was induced by growth in the presence of glutamate.
A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
Belongs to the topoisomerase GyrA/ParC subunit family.
Belongs to the type II topoisomerase GyrA/ParC subunit family.
Few gyrases are as efficient as E.coli at forming negative supercoils. Not all organisms have 2 type II topoisomerases; in organisms with a single type II topoisomerase this enzyme also has to decatenate newly replicated chromosomes.
Heterotetramer, composed of two GyrA and two GyrB chains. In the heterotetramer, GyrA contains the active site tyrosine that forms a transient covalent intermediate with DNA, while GyrB binds cofactors and catalyzes ATP hydrolysis.
Involved in transformation (competence for DNA uptake).
May be a S-adenosyl-L-methionine (SAM)-dependent methyltransferase.
Interacts with CdaA (PubMed:23192352, PubMed:26240071).
Upon coexpression in E.coli stimulates the diadenylate cyclase activity of CdaA about 20-fold (PubMed:23192352). In B.subtilis c-di-AMP is a second messenger that mediates growth, DNA repair and cell wall homeostasis; it is toxic when present in excess (PubMed:26240071).
Probably part of the ABC transporter SkfEF involved in the export of the bacteriocin SKF. Probably responsible for the translocation of bacteriocin SkfA across the membrane.
Belongs to the ABC transporter superfamily. UvrA family.
Forms a heterotetramer with UvrB during the search for lesions.
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate.
Highly up-regulated by aryl-beta-D-glucosides such as salicin or 4-methylumbelliferyl-beta-D-glucopyranoside (MUG).
Significantly expressed throughout all stages of growth or development.
Belongs to the universal ribosomal protein uL13 family.
Part of the 50S ribosomal subunit (PubMed:30126986). Binds to Obg (AC P20964) (PubMed:10781545).
This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.
Involved in both the tricarboxylic acid (TCA) and methylcitric acid cycles (PubMed:28956599). Has both 2-methylcitrate dehydratase and citrate dehydratase activities. Catalyzes the dehydration of 2-methylcitrate (2-MC) to yield 2-methyl-cis-aconitate, and the dehydration of citrate to yield cis-aconitate. Cannot form isocitrate. Uses either (2S,3R)- or (2R,3S)-2-methylcitrate (PubMed:28956599).
Allosterically regulated by its own products; pppGpp simulates synthesis 10-fold more than ppGpp. 2 pppGpp molecules bind in a regulatory cleft in the middle of the tetramer in an asymmetric manner. There is a specific contact of Lys-25 to the gamma-phosphate of pppGpp, explaining why pppGpp stimulates activity but ppGpp does not (PubMed:26460002).
Expressed during exponential growth through the transition to the stationary phase, but not during entry of cells into stationary phase (PubMed:18067544). Protein continuously expressed with a peak at 2 hours after inoculation, decreasing until 3.5 hours as cells enter stationary phase (at protein level) (PubMed:22950019).
Functions as a (p)ppGpp synthase; GDP can be used instead of GTP, resulting in an increase of (p)ppGpp synthesis (PubMed:18067544). The enzyme binds ATP, then GDP or GTP and catalysis is highly cooperative (PubMed:26460002). In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. Probably has a minor role in the stringent response (PubMed:18067544).
The synthase activity of YjbM is greater than that of YwaC (PubMed:18067544).
In spo-63 (loss of residues 27-255); no spores develop, no induction of sporulation-associated enzymes.
Interaction with SpoIIAB inhibits sigma-F activity throughout the cell before the formation of the asymmetric septum; after septation the interaction is confined to the mother cell, and sigma-F activity is released in the prespore (PubMed:8358793). Fin, a second, forespore-specific anti-sigma factor is induced in 2 successive waves by sigma-F and sigma-G, by antagonizing sigma-F it allows the switch to sigma-G factor and progression to the late sporulation development stages (PubMed:21037003).
Produced in the predivisional sporangium, but does not become active in directing gene expression until after septum formation when its activity is restricted to the forespore (at protein level).
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is responsible for the expression of sporulation specific genes (PubMed:8759874). Interaction with SpoIIAB inhibits sigma-F activity throughout the cell before the formation of the asymmetric septum; after septation the interaction is confined to the mother cell, and sigma F activity is released in the prespore. Responsible for expression of csfB (the anti-sigma-G factor Gin) (PubMed:8759874). Associates with the RNAP core only in stationary phase cells (PubMed:21710567).
Belongs to the MsrA Met sulfoxide reductase family.
Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. May deal with oxidative damage to alpha/beta-type SASP in spores.
Binds 1 pyruvoyl group covalently per subunit.
Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
Heterooctamer of four alpha and four beta subunits.
Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus.
Mutation impairs colony surface architecture.
Part of the tapA-sipW-tasA operon (PubMed:10464223). Expression is directly repressed by the DNA-binding protein master regulator of biofilm formation SinR and activated by the extracellular matrix regulatory protein RemA (PubMed:16430695, PubMed:23646920). Expressed constitutively at a low level (PubMed:9694797). Also positively regulated by the sporulation transcription factors sigma H and Spo0A and repressed by the transition phase regulatory protein AbrB, probably indirectly (PubMed:10464223).
Required for the cleavage of the signal sequence of TasA and TapA, which are involved in biofilm formation.
To B.subtilis YqaT and phage SPP1 terminase large subunit.
Global transcriptional regulator of carbon catabolite repression (CCR) and carbon catabolite activation (CCA), which ensures optimal energy usage under diverse conditions.
Global transcriptional regulator of carbon catabolite repression (CCR) and carbon catabolite activation (CCA), which ensures optimal energy usage under diverse conditions. Interacts with either P-Ser-HPr or P-Ser-Crh, leading to the formation of a complex that binds to DNA at the catabolite-response elements (cre). Binding to DNA allows activation or repression of many different genes and operons.
Homodimer. Interacts with P-Ser-HPr and P-Ser-Crh.
Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring.
Cell division protein that is required for the assembly of the Z ring (PubMed:16159787). May serve as a membrane anchor for the Z ring (By similarity). Binds and hydrolyzes ATP (PubMed:11298280). Also involved in sporulation (Probable).
Homodimer (PubMed:11298280). Interacts with FtsZ (PubMed:16159787).
In B.subtilis, unlike the situation in E.coli, the role of FtsA in the recruitment of other division proteins to the division site appears to be an indirect one, through ensuring that FtsZ forms a proper ring.
Transcription is controlled by three promoters. Two of these promoters, P1 and P3 are expressed mainly during vegetative growth. The third one, P2, is up-regulated around the onset of sporulation.
Belongs to the bacterial ribosomal protein bL35 family.
Probable member of the two-component regulatory system YxdK/YxdJ. Positively regulates the expression of the yxdLMyxeA operon by direct interaction with its promoter region. Could also indirectly regulate the expression of the dlt operon.
Belongs to the CPA3 antiporters (TC 2.A.63) subunit F family.
Involved in cholate and Na(+) efflux activities, which may be mechanistically coupled. Does not require other Mrp proteins for its own function.
Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis.
Belongs to the glycogen phosphorylase family.
Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.
Allosterically activated by HslU binding.
Belongs to the peptidase T1B family. HslV subfamily.
Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
Protease subunit of a proteasome-like degradation complex.
Belongs to the GTP-binding SRP family. SRP54 subfamily.
Composed of three domains: the N-terminal N domain, which is responsible for interactions with the ribosome, the central G domain, which binds GTP, and the C-terminal M domain, which binds the RNA and the signal sequence of the RNC.
Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY.
Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY. Interaction with FtsY leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individual components (Probable).
Part of the signal recognition particle protein translocation system, which is composed of SRP and FtsY (By similarity). Interacts with a small cytoplasmic RNA (sc-RNA).
Part of the signal recognition particle protein translocation system, which is composed of SRP and FtsY.
Channel that opens in response to stretch forces in the membrane lipid bilayer. Forms a nonselective ion channel with a conductance of about 4 nanosiemens. May participate in the regulation of osmotic pressure changes within the cell.
Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell.
Deoxyadenosine inhibits deoxycytidine phosphorylation and deoxycytidine inhibits deoxyadenosine phosphorylation. Deoxyadenosine/deoxycytidine kinase is inhibited by both dATP and dCTP.
Plays an essential role in generating the deoxyribonucleotide precursors dATP and dCTP for DNA metabolism. The phosphate acceptor specificity is strict toward deoxyadenosine (dAdo) and deoxycytidine (dCyd). The specificity toward the sugar moiety of the nucleoside is less strict. Both 2-deoxyribose, ribose, and arabinose nucleosides are phosphorylated, although the 2-deoxyribonucleosides are preferred. The phosphate donor specificity is dependent on the deoxyribonucleoside substrate, but GTP is efficient with both deoxycytidine and deoxyadenosine. Only nucleoside triphosphates can act as phosphate donors.
Contains a small N-terminal 3-helix bundle domain and a large C-terminal TPR domain, connected by a linker region.
Inhibited in vitro by the competence and sporulation stimulating factor (CSF), encoded by phrC (PubMed:23526881). However, CSF has at least three targets (RapB, RapC, and RapJ) and the physiological importance of RapJ inhibition by CSF is unknown (PubMed:23526881). Interaction with CSF induces a conformational change in RapJ (PubMed:23526881).
Involved in the regulation of sporulation (Probable). Acts as a phosphatase that specifically dephosphorylates the sporulation initiation phosphotransferase Spo0F and inhibits its activity (PubMed:21346797, PubMed:23526881).
Monomer in solution (PubMed:23526881). Homodimer (PubMed:21346797).
Belongs to the ATPase gamma chain family.
F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c (Probable). The F(1)F(0) complex interacts with SpoIIIJ and YqjG; YqgA is found in the same complex (By similarity) (PubMed:19717609). Interacts with FloT (PubMed:23651456).
Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Belongs to the TRAFAC class YlqF/YawG GTPase family. RsgA subfamily.
Has been described as essential (PubMed:9743119, PubMed:16485133, PubMed:18344364), but also as non-essential (PubMed:15828870). Cells have a slow growth phenotype (PubMed:15828870, PubMed:16485133, PubMed:18344364, PubMed:22544754). Disrupted strain grows as chains of filaments, a cell curvature phenotype is also present, resulting in long wavy cells or short curved rods (PubMed:15828870, PubMed:22544754). Depleted cells form aberrant, swollen cells (PubMed:16485133, PubMed:18344364). Depleted cells DNA staining shows fragmented and/or disturbed nucleoid segregation; effects are seen most in minimal E-medium (PubMed:16485133). Depleted cells have an irregular deposition of cell wall and 15% have abnormal septal cleavage planes (PubMed:18344364).
In vitro phosphorylated mostly on Thr (with lower signal on Ser) by PrkC in the presence of poly-L-Lys or myelin basic protein, dephosphorylated by PrpC (PubMed:19246764). Most in vitro phosphorylation occurs on Thr-166, in vivo phosphorylation has not been detected, but it might vary during the cell cycle (PubMed:22544754).
Monomer, but able to form dimers (PubMed:16485133). Associates with 30S ribosomal subunit; a phospho-mimetic mutation increases association (PubMed:22544754). Probably binds 16S rRNA.
Monomer. Associates with 30S ribosomal subunit, binds 16S rRNA.
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit.
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase with a low level of activity and slow catalytic turnover, does not act on ATP (PubMed:16485133). GTPase activity is stimulated by the presence of 30S or 70S ribosomes, phosphorylation increases stimulation (PubMed:22544754). Depletion results in increased sensitivity to protein synthesis inhibitors that block the peptide channel or peptidyl transferase center on the ribosome, suggesting this protein functions in conjunction with the ribosome in vivo (PubMed:15828870). Decreasing levels of protein lead to an increase in free 30S and 50S ribosomal subunits and a decrease in assembled 70S ribosomes (PubMed:15828870). Suggested to serve as a specific transcription factor for proteins involved in late stages of peptidoglycan synthesis (PubMed:18344364).
Associates with the 50S ribosomal subunit.
Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. EngA (Der) GTPase family.
Cofractionates with the 70S ribosome; association is stabilized by the non-hydrolyzable GTP analog GMPPNP, and inhibited by GTP or GDP.
Essential for growth, it cannot be disrupted. Depletion experiments show that cells become longer and abnormally curved, with nucleoid condensation. Cells have many fewer 70S ribosomes; the large ribosomal subunit is 45S and is missing proteins L16, L27, L36 and interacts with 2 large non-ribosomal proteins.
Estimated to be present at 7000 copies per cell.
GTPase that plays an essential role in the late steps of ribosome biogenesis.
Cells lacking this gene are markedly impaired (but not totally blocked) in growth on L-lactate minimal medium but not impaired in growth on glucose minimal medium.
Is the principal permease for the uptake of L-lactate in B.subtilis.
Involved in the regulation of sporulation (PubMed:10629174). Acts as a phosphatase that specifically dephosphorylates the sporulation initiation phosphotransferase Spo0F and inhibits its activity (PubMed:10629174). Probably plays a dispensable role in the overall context of sporulation initiation (PubMed:10629174).
Phosphatase activity is inhibited by the phosphatase regulator PhrE.
Transcription is under the control of the ComA-ComP two-component system.
Belongs to the RNase H family. EbsB subfamily.
Not known; does not have RNase H activity.
Required for spore cortex hydrolysis during germination. Appears to be required for either expression, localization, activation or function of SleB.
DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria.
DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
Belongs to the bacterial solute-binding protein ModA family.
To B.subtilis YqaS and B.subtilis phage SPP1 terminase small subunit.
Auxiliary enzyme of beta-oxidation. It participates in the metabolism of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA (By similarity).
Belongs to the short-chain dehydrogenases/reductases (SDR) family. 2,4-dienoyl-CoA reductase subfamily.
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Belongs to the SEDS family. FtsW subfamily.
Peptidoglycan polymerase that is essential for cell division.
Destabilization of ComFA (PubMed:17630974).
Expression activated by ComK (PubMed:11948146).
The comE operon is required for the binding and uptake of transforming DNA. ComEC is required for internalization but is dispensable for DNA binding.
To H.influenzae REC2, N.gonorrhoeae ComA and E.coli YcaI.
The acyl carrier 1 domain binds alanine.
Aids in the defense against invading fungal pathogens by degrading their cell wall chitosan.
Belongs to the glycosyl hydrolase 46 family.
Activator of the glucitol dehydrogenase gene (gutB).
May promote colonization of plant roots. May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. Has very low expansin activity (in vitro). No enzymatic activity has been found. Binds to peptidoglycan and to plant cell walls.
Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. May have a role in the decarboxylation of the (S)-3-methylglutaryl group attached to PksL.
Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives.
Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia.
Expressed only during limited or partially limited nitrogen conditions. Can be induced to high levels in the presence of purines or intermediates of the purine catabolic pathway. Expression seems indirectly controlled by TnrA and GlnR.
Belongs to the metallo-dependent hydrolases superfamily. HutI family.
Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.
Belongs to the glycosyl hydrolase-like 10 (GHL10) family.
Part of the ABC transporter complex FhuCBGD involved in iron(3+)-hydroxamate import. Binds the iron(3+)-hydroxamate complex and transfers it to the membrane-bound permease. Partially required for the transport of desferrioxamine.
Competitively inhibited by UDP-glucose. Activated by phosphorylation, which may increase affinity for NAD(+); inhibited by dephosphorylation.
Phosphorylated on tyrosine residue(s). Phosphorylated by YwqD and dephosphorylated by YwqE in vitro.
Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily.
Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues.
Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues. Has lower activity with substrates ending with His or Trp.
Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.
No visible growth defects, DNA is still methylated on A-5 of 5'-GACGAG-3'.
Activates the expression of pucFG, pucH, pucI, pucJKLM and guaD, while it represses pucABCDE and its own expression.
Expression is very low in excess nitrogen (glutamate plus ammonia) and is induced during limiting-nitrogen conditions (glutamate). Expression slightly decreases when allantoin is added during limiting-nitrogen conditions.
Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.
Heterotetramer of two alpha and two beta chains.
Some bacteria possess a monofunctional ArgJ, i.e. capable of catalyzing only the fifth step of the arginine biosynthetic pathway.
Some bacteria possess a monofunctional ArgJ, i.e., capable of catalyzing only the fifth step of the arginine biosynthetic pathway.
Expression starts 5 hours after onset of sporulation and peaks at 6 hours after onset.
No visible effect on vegetative growth, heat resistance of spores or their germination properties.
Involved in pectin degradation (PubMed:29240795). Part of the ABC transporter complex YtcQP-YteP involved in the uptake of polygalacturonan and rhamnogalacturonan type I (PubMed:17449691, PubMed:29240795). Responsible for the translocation of the substrate across the membrane (Probable).
Essential for sporulation, disruption affects the expression of prespore-specific genes but not early mother-cell-specific genes, i.e. cells do not progress beyond stage III of sporulation. A double spoIIIJ-yqjG deletion is lethal. Genetic competence increases about 20-fold in the single disruption.
Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins (By similarity). Also involved in protein secretion processes. Essential for sporulation by activating sigma factor SpoIIIG/SigG after engulfment is completed in the prespore, maybe by acting on SpoIIIAE. It has an overlapping, although partly distinct, function compared to YqjG(MisCB).
SpoIIIJ is required only after engulfment and turned off at the onset of sporulation. While it is predominantly expressed in vegetative cells, its low expression after the onset of sporulation is essential for sporulation to occur.
Activated by a monovalent cation that binds near, but not in, the active site. The most likely occupant of the site in vivo is potassium. Ion binding induces a conformational change that may alter substrate affinity.
Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.
Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway.
Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate.
Binds 1 heme group covalently per subunit.
Catalyzes the C-C bond cleavage of fatty acid linked to acyl carrier protein (ACP) to generate pimelic acid for biotin biosynthesis. It has high affinity for long-chain fatty acids with the greatest affinity for myristic acid.
Essential for cell growth and for normal cell shape.
Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. All amino acids serve as attractants in B.subtilis, they appear to cause an increase in the turnover methyl groups, leading to methylation of an unidentified acceptor, while repellents have been shown to cause a decrease in methyl group turnover. The methyl groups are added by a methyltransferase and removed by a methylesterase. McpC is required for taxis to cysteine, proline, threonine, glycine, serine, lysine, valine and arginine and for aspartate, glutamine, histidine and glutamate. Primarily mediates response to positive stimulus of PTS carbohydrates. Greatly influences the duration or magnitude of the response to negative PTS carbohydrate stimulus.
Induced by SigD. Expression increases in the late-exponential growth-phase and is maximal during the early-stationary phase.
Belongs to the CcmF/CycK/Ccl1/NrfE/CcsA family.
Disruption of the gene results in the reduction of aprE expression.
Part of the rapG-phrG operon (PubMed:12950930). Transcription of phrG only is controlled by the sigma-H factor (PubMed:12950930). Expression is rapidly induced in the transition state to stationary phase (PubMed:12950930).
Signaling molecule involved in the regulation of expression of DegU-controlled genes (PubMed:12950930). Secreted during production, but the mature peptide acts intracellularly, indicating that it needs to be imported into the cell to function (By similarity). Stimulates the DegU-dependent expression of aprE, an extracellular alkaline protease (PubMed:12950930). Acts by inhibiting RapG activity (PubMed:12950930). At high concentrations, represses the DegS-dependent aprE expression (PubMed:12950930).
Belongs to the DmpD/TodF/XylF esterase family.
Can also use Mg(2+) and Ca(2+), with lower efficiency.
Homodimer (PubMed:11923303). Interacts with its substrate, phosphorylated Spo0F, and its inhibitor, the PhrA pentapeptide (PubMed:11923303, PubMed:22267516). The RapA dimer forms a stable complex with two molecules of phosphorylated Spo0F (PubMed:11923303). The complex is dissociated after dephosphorylation of Spo0F by RapA (PubMed:11923303).
Involved in the regulation of sporulation (PubMed:1624431, PubMed:8001132, PubMed:11923303, PubMed:22267516). Acts as a phosphatase that specifically dephosphorylates the sporulation initiation phosphotransferase Spo0F and inhibits its activity (PubMed:8001132, PubMed:11923303, PubMed:22267516).
Phosphatase activity is inhibited by the phosphatase regulator PhrA (PubMed:8643670, PubMed:9238025, PubMed:11923303, PubMed:22267516). Interaction with PhrA dissociates the RapA-Spo0F complex (PubMed:11923303). Activity is abolished in the presence of EDTA (PubMed:11923303).
The N-terminal half of RapA contains the necessary structural determinants for substrate binding and enzymatic activity, and the C-terminal half contains the binding site for PhrA peptide (PubMed:22267516). The central TPR3 to TPR5 repeats provide the binding specificity toward the Phr peptide inhibitor (PubMed:22267516).
Under all conditions of nutrient limitation, and by addition of decoyinine.
In CydC the ATP-binding domain (NBD) and the transmembrane domain (TMD) are fused.
Part of the ABC transporter complex CydDC that exports the reduced low-molecular-weight thiols cysteine and glutathione from the cell. Export of these thiol-containing redox-active molecules may be crucial for redox homeostasis, permitting correct assembly of various respiratory complexes and formation of correct disulfide bonds in secreted proteins. CydC contains transmembrane domains (TMD), which form a pore in the membrane, and an ATP-binding domain (NBD), which is responsible for energy generation.
Belongs to the acetolactate synthase small subunit family.
Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine.
Activated by inorganic phosphate, and to a lesser extent by sulfate ions (PubMed:2169413). In addition to form a complex with ATP, Mg(2+) also acts as a cofactor (PubMed:2169413). Strongly inhibited by ADP through competitive binding at the activation site and at a specific allosteric site (PubMed:2169413, PubMed:16008562). Less strongly inhibited by alpha,beta-methylene ATP (mADP), AMP, GDP, GMP and UTP (PubMed:2169413, PubMed:16008562).
Belongs to the ribose-phosphate pyrophosphokinase family. Class I subfamily.
Binds 2 Mg(2+) ions per subunit. Each Mg(2+) binds only one residue (His-136 and Asp-175, respectively) of this protein, however the magnesium ions also bind substrates and water molecules to complete their coordination spheres (PubMed:2169413, PubMed:11790837). Can also use Mn(2+) and Cd(2+) ions, but the activity is less than that obtained with Mg(2+) ions (PubMed:2169413, PubMed:11790837).
Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P).
This enzyme uses a steady state ordered mechanism, where Mg(2+) binds first, followed by Mg-ATP and lastly, ribose 5-phosphate.
Is essential for L-lactate degradation and allows cells to grow with lactate as the sole carbon source. May also allow cells to utilize an alternative carbon source during biofilm formation, since it contributes to the formation of architecturally complex communities when lactate is present.
Is involved in L-lactate degradation and allows cells to grow with lactate as the sole carbon source.
May work together with YlbF to regulate community development.
3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs (By similarity). Involved in degradation of type I toxin-antitoxin system bsrG/SR4 RNAs (PubMed:22229825).
3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs.
Belongs to the RNR ribonuclease family. RNase R subfamily.
No visible phenotype (PubMed:17369301). Increased half-life of type I toxin-antitoxin system RNAs of BsrG/SR4 (PubMed:22229825).
Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Lacks the C-terminal region present in SsbA and thus is probably not able to participate in DNA replication and/or DNA repair.
Not essential for replication of the chromosome, but is required for optimal competence (PubMed:14762004). Binds ssDNA, binding is facilitated by DprA, acts as an accessory factor for homologous DNA strand exchange (PubMed:25138221).
Only expressed during growth in minimal medium, strongly induced when cells enter stationary phase with highest levels reached about 2 hours after transition to stationary phase (PubMed:14762004). Expression activated by ComK (PubMed:11918817, PubMed:11948146, PubMed:14762004).
Preferentially expressed in cells competent for DNA transformation; that is 5-15% of the population (PubMed:11918817, PubMed:16009133, PubMed:17630974).
Transformation efficiency drops 10- to 50-fold (PubMed:11918817, PubMed:11948146, PubMed:14762004). Destabilization of DprA (PubMed:17630974).
Required for maturation of 30S ribosomal subunits.
Belongs to the PHP hydrolase family. HisK subfamily.
Belongs to the glucose-1-phosphate thymidylyltransferase family.
Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis.
Belongs to the methyltransferase superfamily. YrrT family.
Could be a S-adenosyl-L-methionine-dependent methyltransferase.
Interacts with MreB (PubMed:21964069). Interacts with FloT (PubMed:23651456).
Single mutant has no effect on cell growth or morphology under normal growth conditions. Triple disruption of tagTUV genes is not viable (PubMed:21964069). Cells lacking this gene display a considerably increased transcription frequency of lytR and lytABC operon expression (PubMed:1357079).
This protein is unrelated to LytR from S.aureus, which is part of a two-component regulatory system that, together with LytS, is involved in autolysis and cell wall metabolism. The B.subtilis ortholog of S.aureus LytR is LytT (AC P94514).
Was originally thought to be involved in transcriptional regulation.
May be involved in the biosynthesis of molybdopterin.
Belongs to the metallo-dependent hydrolases superfamily. Adenine deaminase family.
In the C-terminal section; belongs to the UPF0157 (GrpB) family.
The acyl carrier 2 domain binds glycine.
Was originally thought to be two separate ORFs named pksJ and pksK.
Probably functions as a cell separation enzyme in addition to LytE and LytF.
The cell shape is not significantly different from that of the wild-type.
Transcribed during the late vegetative and early stationary phases.
Overall loss in complex colony architecture and lack of fruiting body-like structures.
Required for complex colony architecture.
Up-regulated by DegU and Spo0A. Repressed by AbrB.
Belongs to the TRAFAC class YlqF/YawG GTPase family.
Essential for growth, it cannot be disrupted. In depletion experiments cells become 1.5 to 2-fold longer and nucleoid distribution is dispersed. The number of replication origins increases, suggesting an increase in chromosome replication.
Estimated to be present at 2000 copies per cell.
A methylase, recognizes the double-stranded sequence 5'-YTCGAR-3', methylates C-3 on both strands, and protects the DNA from cleavage by the BsuMI endonuclease.
Constitutively expressed during exponential growth. Encoded in an operon with ydiP and in a second with groES, groEL, ydiM and ydiN. This second operon is heat-inducible.
Essential for growth, it can be disrupted once one of the components of the corresponding BsuMI restriction endonuclease complex (AC O34303, O34885, O35025, YdjA, YdiS and YdiR respectively) has been disrupted (PubMed:11751814). Triple deletions ydiO-ydiP-ydiR, ydiO-ydiP-ydiS and ydiO-ydiP-ydjA lead to loss of susceptibility to MspJI, which only digests C-methylated DNA (PubMed:32324221).
Monomer (PubMed:3150363). May form a complex with YdiP, also seems to be active alone (Probable).
Somewhat inhibited by MgCl(2) and spermidine, strongly inhibited by MnCl(2).
The characterized enzyme was reported to be a monomer of approximately 45 kDa; it is not clear whether this corresponds to YdiO, YdiP or to another activity altogether.
Belongs to the NAD(P)-dependent epimerase/dehydratase family. SDR39U1 subfamily.
Belongs to the pseudouridine synthase RsuA family.
The EIIC type-2 domain forms the PTS system translocation channel and contains the specific substrate-binding site.
The PTS EIIB type-2 domain is phosphorylated by phospho-EIIA on a cysteinyl residue. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the PTS EIIC type-2 domain.
Was originally thought to be a longer ORF that encodes what is now known to be mtlA and mtlF.
Part of the bacilysin biosynthesis operon. May be involved in self-resistance to bacilysin by permitting efflux of this antibiotic.
The compound ppGpp is essential for the transcription of the bacABCDE operon and GTP regulates the transcription of both this operon and ywfH via the CodY-mediated regulation system.
Belongs to the GGGP/HepGP synthase family. Group I subfamily.
Cells lacking this gene show a cloggy growth and do not produce the dephosphorylated and acetylated derivatives of HepGP.
Prenyltransferase that catalyzes in vivo the transfer of the heptaprenyl moiety of heptaprenyl pyrophosphate (HepPP; 35 carbon atoms) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P), producing heptaprenylglyceryl phosphate (HepGP). This reaction is an ether-bond-formation step in the biosynthesis of archaea-type G1P-based membrane lipids found in Bacillales.
Prenyltransferase that catalyzes in vivo the transfer of the heptaprenyl moiety of heptaprenyl pyrophosphate (HepPP; 35 carbon atoms) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P), producing heptaprenylglyceryl phosphate (HepGP). This reaction is an ether-bond-formation step in the biosynthesis of archaea-type G1P-based membrane lipids found in Bacillales. To a much lesser extent, is also able to use geranyl diphosphate (GPP; C10) and geranylgeranyl diphosphate (GGPP; C20) as the prenyl donors, but not farnesyl pyrophosphate (FPP; C15). Cannot use glycerol-3-phosphate (G3P) or 3-phosphoglycerate (3PG) as an acceptor.
The HepGP product, which is the first archaea-type G1P-based ether lipid being identified within the phylogenetic domain of the bacteria, was found to be subsequently dephosphorylated and acetylated in vivo. However, HepG and its acetylated derivatives represent only a minor fraction of the total lipid in B.subtilis.
Belongs to the prokaryotic pantothenate kinase family.
Could have a role in maltodextrin utilization.
Belongs to the GcvP family. N-terminal subunit subfamily.
The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein (By similarity).
The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
The glycine cleavage system is composed of four proteins: P, T, L and H. In this organism, the P 'protein' is a heterodimer of two subunits.
May be involved in multidrug export. Transmembrane domains (TMD) form a pore in the cell membrane and the ATP-binding domain (NBD) is responsible for energy generation (By similarity).
The ATP-binding domain (NBD) and the transmembrane domain (TMD) are fused.
A null mutation abolishes the ability of a proline auxotroph to grow in a medium containing the dipeptide Pro-Gly as sole proline source.
Probably part of the ABC transporter DppBCDE involved in dipeptide transport.
Forms a complex with SpoIVFA and SpoIVFB localized in the mother cell membrane surrounding the forespore.
Involved in the mediation of the intercompartmental coupling of pro-sigma K processing to events in the forespore. Inhibits SpoIVFB-processing activity until a signal has been received from the forespore. Could inhibit SpoIVFB metalloprotease activity by coordinating a zinc in the SpoIVFB active site, preventing access of a water molecule and the sequence of pro-sigma K, which are necessary for peptide bond hydrolysis to produce sigma-K.
Expressed during sporulation. Detected in mature spores (PubMed:3080407).
Probably involved in peptidoglycan modification during cortex synthesis.
Mutation impairs pellicle formation, complex colony architecture and motility inhibition in a sinR mutant background.
Regulates the biosynthesis of the extracellular matrix and the biofilm formation. May act as an enhancer of biofilm gene expression. Acts in parallel to the pathway that governs SinR derepression.
Member of the two-component regulatory system YcbM/YcbL. Probably activates YcbL by phosphorylation.
Belongs to the calycin superfamily. ZinT family.
Involved in nucleotide metabolism: produces dUMP, the immediate precursor of thymidine nucleotides and decreases the intracellular concentration of dUTP, so that uracil cannot be incorporated into DNA (PubMed:9679200). The Ser-62 side chain changes its position upon ligand-binding to make contacts with the nucleotide phosphates (PubMed:21358047).
The uracil deoxyribose moiety interacts with the protein through Ile-79 and Tyr-83, which discriminate against the ribose form of the nucleotide.
ATPase essential both for efficient CtsR-dependent gene derepression during heat stress and for rerepression. Together with ClpP, degrades the global regulator CtsR after heat shock. Is also involved in disaggregation of heat-denatured proteins. Has thus a role in overall protein quality control in response to heat stress.
Belongs to the ClpA/ClpB family. ClpE subfamily.
By heat shock via the relief of repression carried out by the transcriptional regulator CtsR.
Cells lacking this gene display a retardation of CtsR-dependent gene induction as well as a delayed restoration of the repressed stage. They also show a significant delay in disaggregation of heat-generated insoluble protein aggregates.
ClpE is a very short-lived protein, that is, at least in the soluble cell fraction, degraded mainly by ClpCP.
By Spo0A during nutrient starvation through its direct negative control of AbrB, repressed by AbrB during regular growth when nutrients are plentiful (PubMed:16469701). Represses its own transcription (PubMed:16469701). Induced by expression of SDP (active peptide of sdpC) (PubMed:16469701, PubMed:23687264).
Represses the transcription of the sdpIR operon and of several other operons that probably contribute to delaying commitment to sporulation.
Involved in formation of the rod shape of the cell. May also contribute to regulation of formation of penicillin-binding proteins (By similarity).
Belongs to the universal ribosomal protein uL29 family.
Transaminates branched-chain amino acids and ketoglutarate. Involved in the final step of the methionine regeneration pathway, where ketomethiobutyrate (KMTB) is converted to methionine via a transamination. The amino donor preference is isoleucine, leucine, valine, phenylalanine, and tyrosine.
Required for YwqD kinase activity. May bring YwqD and its substrates into contact. Probably involved in the regulation of capsular polysaccharide biosynthesis.
50% inhibited by vanadate; it has been suggested that vanadate fully inhibits the dimer but not the monomer (PubMed:15766260). Activated by 15 uM reserpine then inhibited by higher concentrations.
An efflux transporter able to transport Hoechst 33342, ethidium bromide, doxorubicin and a number of other drugs in vitro into inside out vesicles. The endogenous substrate is unknown. It has been suggested that NBD dimerization induced by ATP-binding causes a large conformational change responsible for substrate translocation (PubMed:18215075). Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable).
In BmrA the ATP-binding domain (NBD) and the transmembrane domain (TMD) are fused. This is considered to be a half-size transporter that undergoes homodimerization to be functional.
Belongs to the helicase family. AddB/RexB type 1 subfamily.
The heterodimer acts as both an ATP-dependent DNA helicase and an ATP-dependent single-stranded exonuclease, acting in both directions. Recognizes the B.subtilis chi site (5'-AGCGG-3') which transforms the enzyme from a helicase which degrades both DNA strands to one with only 5' to 3' exonuclease activity. This generates a double-stranded DNA with a protruding 3'-terminated single-stranded tail suitable for the initiation of homologous recombination (chi fragment). The AddB nuclease domain is not required for chi fragment generation; this subunit has 5' -> 3' nuclease activity. RecA thread formation during DNA double-strand break repair requires RecJ or AddAB.
The heterodimer acts as both an ATP-dependent DNA helicase and an ATP-dependent, dual-direction single-stranded exonuclease. Recognizes the chi site generating a DNA molecule suitable for the initiation of homologous recombination. The AddB nuclease domain is not required for chi fragment generation; this subunit has 5' -> 3' nuclease activity.
This enzyme is a functional homolog of the RecBCD enzyme; unlike the RecBCD enzyme it degrades both duplex strands symmetrically.
Allosterically activated by GTP. Can also be activated by dGTP and 3'-anthraniloyl-2'-deoxyguanosine-5'-triphosphate (Ant-dGTP). Inhibited by UTP, 5-bromo-UTP and 5-iodo-UTP.
Allosterically activated by GTP. Inhibited by UTP.
Catalyzes the reversible phosphorylation of UMP to UDP, with ATP or dATP as the most efficient phosphate donors. Is also able to phosphorylate 5-fluoro-UMP and 6-aza-UMP.
Catalyzes the reversible phosphorylation of UMP to UDP.
Homohexamer (PubMed:12869195). Interacts with BrxC (PubMed:33722570).
The peripheral distribution of PyrH is related most probably to its role in the synthesis of membrane sugar components and its putative role in cell division.
Belongs to the glycosyl hydrolase 13 family. BbmA subfamily.
Hydrolyzes beta-cyclodextrin to maltose and glucose, soluble starch to maltose and glucose, and pullulan to panose with trace amounts of maltose and glucose. It is also able to hydrolyze acarbose. Can also exhibit a transglycosylation activity transferring glucose or maltose to another moiety of sugars by forming alpha-(1,6)- and alpha-(1,3)-glycosidic linkages upon the hydrolysis of substrate at concentrations of 5% or higher (By similarity).
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. Some bacteria have evolved a zinc-coordinating structure that stabilizes the LID domain.
Catalyzes the dephosphorylation of the riboflavin precursor 5-amino-6-(5-phospho-D-ribitylamino)uracil and of flavin mononucleotide (FMN) in vitro (PubMed:26316208). Also catalyzes the dephosphorylation of phosphorylated 5-6 carbon sugars and monophosphate nucleotides (NMP) in vitro (PubMed:25848029).
Belongs to the RNA polymerase subunit omega family.
Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits (By similarity). In vitro reconstitution experiments this subunit is dispensible (PubMed:18289874).
Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
Seems to be complexed to phosphorylated HPr.
Transcriptional regulator involved in catabolite repression of several operons.
Belongs to the methyltransferase superfamily. PrmA family.
This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Glu and Ala/Val as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The Ala/Val residue is further epimerized to the D-isomer form. The activation sites for these amino acids consist of individual domains.
Belongs to the ATPase delta chain family.
F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains (Probable). The F(1)F(0) complex interacts with SpoIIIJ and YqjG; YqgA is found in the same complex (By similarity) (PubMed:19717609) (Probable). Interacts with FloT (PubMed:23651456).
This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.
Expression is constant during late log phase and for at least 2 hours in stationary phase (at protein level) (PubMed:11849533). Probably repressed by AbrB and SinR, as well as partially by ComK (PubMed:11849533). Probably negatively regulates its own expression (PubMed:11849533, PubMed:21085634). There are 1000-3000 proteins/chromosome in exponential phase grown in minimal medium (PubMed:21085634).
Increased expression of comK, increases transformation about 5-fold, decreases sporulation efficiency about 5-fold (PubMed:11849533). Increased excision of mobile element ICEBs1 (PubMed:21085634).
Repressor of comK, the master regulator of competence development (PubMed:11849533). Overexpression seems to be lethal (PubMed:11849533). Represses at least 20 genes that specify membrane-localized and secreted proteins, including some that encode products with antibiotic activity (PubMed:15743949). Binds to many AT-rich sites in the chromosome, many of which are known or thought to derive from horizontal gene transfer; helps keep mobile element ICEBs1 quiescent in the genome (PubMed:21085634). Binds to its own promoter and is thus probably autoregulatory (PubMed:21085634).
The C-terminus (residues 95-191) binds DNA (PubMed:21085634).
Belongs to the class-I DAHP synthase family.
Probably interacts with cognate immunity protein YqcF but not with non-cognate immunity proteins. The interaction inhibits the toxic activity of YqcF (Probable).
Toxic component of one of 6 LXG toxin-immunity modules in this strain. They promote kin selection, mediate competition in biofilms, and drive spatial segregation of different strains, indicating that LXG toxins may help avoid warfare between strains in biofilms. Mediates intercellular competition during biofilm formation; disruption of the operon disadvantages the bacteria, but overexpression of the cognate immunity protein restores growth in competition with wild-type. Overexpression alone in situ causes growth arrest but not cell lysis, a large decrease in chromosomal DNA content and the production of anucleate cells. No effect is seen on rRNA. Co-overexpression with cognate immunity protein YqcF does not cause growth arrest. The toxic effect is dependent on the epsA and tapA operons which are required for biofilm formation.
Was originally thought to be an RNase; when the C-terminus (residues 379-531) is expressed in E.coli it has RNase, not DNase activity, and inhibits growth upon expression in E.coli. In vitro RNase activity and in vivo growth inhibition are neutralized by cognate immunity protein YobK, but not by immunity proteins specific to other LXG toxins.
Belongs to the metallo-dependent hydrolases superfamily. DHOase family. Class I DHOase subfamily.
Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Belongs to the bacterial ribosomal protein bL31 family. Type A subfamily.
Binds 1 zinc ion per subunit. This zinc stabilizes the protein.
Only accumulates during exponential growth.
Part of the 50S ribosomal subunit during exponential growth.
While neither of the L31 paralogs is essential, this protein seems to function as the main L31 protein. Has a lower affinity for 70S ribosomes than the non-zinc-containing paralog L31B (ytiA); is displaced by it to varying extents, even under zinc-replete conditions.
Belongs to the large terpene synthase family.
Catalyzes the transformation of a linear C35 prenyl diphosphate chain to form tetraprenyl-beta-curcumene.
Interacts directly with the sensor histidine kinase ComP and stimulates its activity.
Part of a major quorum-sensing system that regulates the development of genetic competence (PubMed:8168130, PubMed:11751817, PubMed:16091051, PubMed:12067344). Acts through the activation of the two-component regulatory system ComP/ComA composed of a sensor histidine kinase, ComP, and a response regulator, ComA (PubMed:8168130, PubMed:16091051). Activation of ComA leads to the direct regulation of over 20 genes and expression of over 150 additional genes, including those involved in competence development, appears to be controlled indirectly (PubMed:16091051). Under certain conditions plays a role in sporulation (PubMed:8168130).
The DNA sequences encoding comQ, comX and the N-terminal two-thirds of comP show a striking polymorphism, which determines the specificity of the quorum-sensing system in the different pherotypes of Bacillus. In ComX, the sole conserved residue is the modified tryptophan essential for the activity.
Trp-53 is modified by farnesylation, which is essential for activity (PubMed:8168130, PubMed:12067344, PubMed:18323630). Modified by the tryptophan prenyltransferase ComQ before export to the extracellular environment (PubMed:8168130, PubMed:12067344). The type of isoprenyl derivative differs among the different pherotypes and depends on ComX primary sequence (PubMed:12067344, PubMed:14679219).
May be involved in the degradation of peptidoglycan by catalyzing the cleavage of the terminal D-alanine residue from cytoplasmic murein peptides.
Belongs to the serine/threonine dehydratase family. DsdA subfamily.
Can be both biotinylated and lipoylated on Lys-35 upon overexpression in E.coli depending on the growth medium; the nature of the modification in situ in B.subtilis is unknown.
Detected in log-phase B.subtilis cells (at protein level).
Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly.
Regulates the expression of extracellular-protein genes of Bacillus subtilis.
Not known; does not seem to be involved in host cell lysis.
A triple bsdB-bsdC-bsdD deletion mutant no longer converts vanillin to guaiacol, the conversion stops at vanillic acid.
Involved in the non-oxidative decarboxylation and detoxification of phenolic derivatives under both aerobic and anaerobic conditions, however the precise biochemical function of BsdD in metabolism of phenolic acid is unknown.
GTP-binding protein that is not required for the biosynthesis of Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor, and not necessary for the formation of active molybdoenzymes using this form of molybdenum cofactor. May act as an adapter protein to achieve the efficient biosynthesis and utilization of MGD. Displays a weak intrinsic GTPase activity (By similarity).
Belongs to the auxin efflux carrier (TC 2.A.69) family.
Probably interacts with cognate immunity protein YxxD but not with non-cognate immunity proteins. The interaction inhibits the toxic activity of YxxD (Probable).
Toxic component of one of 6 LXG toxin-immunity modules in this strain. They promote kin selection, mediate competition in biofilms, and drive spatial segregation of different strains, indicating that LXG toxins may help avoid warfare between strains in biofilms. Mediates intercellular competition during biofilm formation; disruption of the operon disadvantages the bacteria, but overexpression of the cognate immunity protein restores growth in competition with wild-type. Overexpression alone in situ causes growth arrest but not cell lysis, a large decrease in chromosomal DNA content and the production of anucleate cells. No effect is seen on rRNA. Co-overexpression with cognate immunity protein YxxD does not cause growth arrest. The toxic effect is not dependent on the epsA and tapA operons which are required for biofilm formation.
Was originally thought to be an RNase; when the C-terminus (residues 409-569) is expressed in E.coli it has RNase, not DNase activity, and inhibits growth upon expression in E.coli. In vitro RNase activity and in vivo growth inhibition are neutralized by cognate immunity protein YxxD, but not by immunity proteins specific to other toxins with the LXG domain. Mutation of His-548 to Ala leads to loss of growth inhibition and RNase activity in E.coli.
Processing of ComGE in competent cells requires ComC.
Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
In B.subtilis succinate dehydrogenase forms part of an enzyme complex containing three subunits: a flavoprotein, an iron-sulfur protein and cytochrome b-558.
Involved in the germination response to the combination of glucose, fructose, L-asparagine, and KCl.
Belongs to the RNase HII family. RnhC subfamily.
Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho's RNA-dependent ATPase activity, and release of the mRNA from the DNA template.
Homohexamer. The homohexamer assembles into an open ring structure.
Belongs to the NtaA/SnaA/DszA monooxygenase family.
Induced when methionine is the sulfur source, but not by sulfate.
Involved in a cysteine salvage pathway from S-alkylcysteine. Catalyzes the C-S bond cleavage in N-acetyl-S-benzyl-L-cysteine sulfoxide leading to N-acetyl-S-hydroxy-L-cysteine and benzaldehyde. This pathway is likely important in the catabolism of alkylated cysteine generated by proteolysis of alkylated glutathione formed in the detoxification of a wide range of electrophiles. Has much less efficient activity with N-acetyl-S-methyl-L-cysteine sulfoxide as substrate. Cannot use S-alkylated L-cysteine sulfones and ketone analogs as substrates, demonstrating that the sulfoxide is required for activity.
Reduced growth with methionine or methionine sulfoxide as unique source of sulfur.
Decreased growth rate in pyrimidine-free medium, extreme derepression of the pyrimidine biosynthetic operon, and decreased, but detectable dihydroorotate dehydrogenase activity.
Responsible for channeling the electrons from the oxidation of dihydroorotate from the FMN redox center in the PyrD subunit to the ultimate electron acceptor NAD(+).
Responsible for channeling the electrons from the oxidation of dihydroorotate from the FMN redox center in the PyrD type B subunit to the ultimate electron acceptor NAD(+).
In the N-terminal section; belongs to the FabD family.
Probably involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. Probably has an acyl transferase activity and could also have a flavin mononucleotide-dependent oxidoreductase activity.
No visible phenotype; grows as well as wild-type at 25-49 degrees Celsius, no apparent impairment in sporulation or phage SP01 growth.
Participates in both the initiation and recycling phases of transcription. In the presence of the delta subunit, RNAP displays an increased specificity of transcription, a decreased affinity for nucleic acids, and an increased efficiency of RNA synthesis because of enhanced recycling.
Participates in both the initiation and recycling phases of transcription. In the presence of the delta subunit, RNAP displays an increased specificity of transcription, a decreased affinity for nucleic acids, and an increased efficiency of RNA synthesis because of enhanced recycling. May function in sigma factor switching. It displaces RNA bound to RNA polymerase in a binary complex.
RNAP is composed of a core of 2 alpha, a beta and a beta' subunits. The core is associated with a delta subunit and one of several sigma factors.
The beta chain is an electron transfer unit containing four cysteine clusters involved in the formation of iron-sulfur centers. Electrons are transferred from the gamma chain to the molybdenum cofactor of the alpha subunit.
Part of the ABC transporter complex TcyABC involved in L-cystine import.
No visible phenotype in growth, sporulation, spore germination, outgrowth, or spore heat resistance (PubMed:8830698). No visible phenotype in the absence of antibiotics; loss of resistance to oxacillin and cephalexin but not penicillin G. It cannot be deleted in the absence of a catalytically inactive copy of penicillin-binding protein 2B (pbpB) (PubMed:28792086).
Penicillin-binding proteins (PBPs) function in the late steps of murein biosynthesis (Probable). Probably required for both cortical and vegetative peptidoglycan synthesis (Probable). Although not usually required for cell division, in the absence of PBP 2B (pbpB) it becomes essential. Confers resistance to oxacillin and cephalexin (PubMed:28792086).
Present in all growth stages and in both inner and outer forespore membranes.
Transcribed during vegetative growth, drops off after entry into stationary phase and the onset of sporulation. Transcription rises again 70-80 minutes after germination.
Deletion of the gene results in decreased expression of genes activated by ComA, including rapA and the srfA operon (PubMed:15968044, PubMed:16816200). It significantly changes the expression of 72 operons (PubMed:16816200).
Interacts with RapF and inhibits its interaction with ComA.
Part of the rapF-phrF operon, which is controlled by ComA (PubMed:15968044). Transcription of phrF is also regulated by the sigma-H factor (PubMed:15968044).
RapF and PhrF pair of proteins acts synergistically with RapC and CSF in the overall regulation of the ComA transcription factor (PubMed:15968044). CSF, PhrF and PhrK stimulate ComA-dependent gene expression to different levels and are all required for full expression of genes activated by ComA (PubMed:16816200).
Signaling molecule involved in the regulation of genetic competence development (PubMed:15968044, PubMed:16816200). Secreted during production, but the mature peptide acts intracellularly, indicating that it needs to be imported into the cell to function (By similarity). Stimulates expression of the genes controlled by ComA, a transcriptional factor that regulates the development of genetic competence (PubMed:15968044, PubMed:16816200). Acts by inhibiting RapF, which regulates the activity of ComA (PubMed:15968044, PubMed:16816200, PubMed:22215984, PubMed:23526880).
Component of the MPD complex composed of SpoIIM, SpoIIP and SpoIID.
Expression starts 2 hours post-sporulation.
Required for complete septum migration and engulfment of the forespore compartment during sporulation. Required for stabilizing and recruiting of SpoIIP to the septal membrane.
Results in a block at stage II of sporulation. No fully engulfed forespores. SpoIIP mislocalization from the septal membrane.
Involved in biofilm formation (PubMed:18978066, PubMed:21742882). Self-polymerizes and forms a layer on the surface of biofilms that confers hydrophobicity to the biofilm (PubMed:22571672, PubMed:23904481). The layer is stable and capable of resistance to high mechanical force compression (PubMed:28701036). Required for complex colony architecture (PubMed:18978066). May function synergistically with exopolysaccharides and TasA amyloid fibers to facilitate the assembly of the biofilm matrix (PubMed:21742882).
Overall loss in complex colony architecture and lack of fruiting body-like structures (PubMed:18978066). Disruption of the gene results in the loss of surface repellency and alters the biofilm surface microstructure (PubMed:22571672).
Acts as both a kinase and a phosphatase on SacT.
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in sucrose transport.
Cys-15 is oxidized by organic peroxides to cysteine sulfenic acid (Cys-SOH). This can react with the alpha-amido of the following residue to form the sulfenamide cross-link. Oxidation or cross-linking results in the loss of DNA-binding activity and the inactivation of repressor function. Both the cysteine sulfenic acid and the sulfenamide cross-link can react with free cysteine or bacillithiol (BSH) to form mixed disulfides. Further reduction of OhrR by free sulfhydryl compounds restores repressor activity.
Inactivated by oxidation of Cys-15 to a sulfenic acid.
Organic peroxide sensor (PubMed:11418552). Represses the expression of the peroxide-inducible gene ohrA by cooperative binding to two inverted repeat elements (PubMed:11418552, PubMed:24313874).
Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.
Essential for murein biosynthesis (PubMed:29280348). Probably catalyzes the conversion of L-2-acetamido-6-oxopimelate to N-acetyl-LL-2,6-diaminopimelate (Probable).
Increases in stationary phase in a strain lacking the WprA protease.
Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively.
Homohexamer and homododecamer. In the presence of PdxT, forms a dodecamer of heterodimers.
In the presence of PdxT, forms a dodecamer of heterodimers.
In vitro, is able to catalyze the acetylation of beta-lysine to N6-acetyl-beta-lysine, an archaeal osmolyte produced by methanogenic archaea. Its physiological function has not yet been elucidated.
N6-acetyl-beta-lysine is not synthesized by B.subtilis as part of its cellular defense against high salinity.
The use of YodP from B.subtilis for N6-acetyl-beta-lysine synthesis opens the bottleneck for the large-scale production of N6-acetyl-beta-lysine to investigate its properties as a compatible solute.
Up-regulated during sporulation, under the control of the sigma-E transcription factor (SigE).
Heterotetramer of two alpha and two beta chains. Directly associated with ODBB in the E1 complex.
The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
Divisome component that associates with the complex late in its assembly, after the Z-ring is formed, and is dependent on DivIC and PBP2B for its recruitment to the divisome. Together with EzrA, is a key component of the system that regulates PBP1 localization during cell cycle progression. Its main role could be the removal of PBP1 from the cell pole after pole maturation is completed. Also contributes to the recruitment of PBP1 to the division complex. Not essential for septum formation.
Forms polymers through the coiled coil domains. Interacts with PBP1, MreC and EzrA.
Belongs to the zinc-associated anti-sigma factor (ZAS) superfamily. Anti-sigma-W factor family.
Binds 1 Zn(2+) ion per subunit. Absence of the Zn(2+) (in a residue 1-80 fragment) does not prevent interaction with SigW, nor does it change the overall conformation of RsiW, although a disulfide bond can form between Cys-3 and Cys-37 (PubMed:28319136).
By different stresses causing damage to the cell envelope, such as alkaline shock (PubMed:11454200), salt shock (PubMed:11544224), phage infection and certain antibiotics that affect cell wall biosynthesis (PubMed:12207695, PubMed:15870467).
Forms a heterodimer with cognate sigma factor SigW, which probably prevents SigW from binding to DNA (PubMed:28319136).
Is processed by successive proteolytic events. First, the extracellular region of RsiW is cleaved by PrsW (site-1 cleavage) in response to cell envelope stresses (PubMed:16816000, PubMed:17020587). In a reconstituted E.coli system PrsW cuts between Ala-168 and Ser-169 followed by trimming by E.coli Tsp; the endogenous extracellular exopeptidase responsible for the event in B.subtilis has not been identified (PubMed:19889088). Next, it undergoes cleavage at an intramembrane site (site-2 cleavage) mediated by RasP (PubMed:15130127). This cleavage uncovers a cryptic proteolytic tag with conserved alanine residues in the transmembrane segment, that is recognized mainly by the ClpXP protease, which completely degrades the protein in the cytoplasm and leads to the induction of the sigma-W-controlled genes (PubMed:16899079).
The anti-sigma factor for extracytoplasmic function (ECF) sigma factor sigma-W (SigW). Holds SigW, its cognate ECF sigma factor, in an inactive form until released by regulated intramembrane proteolysis (RIP). SigW and RsiW mediate cell response to cell wall stress (PubMed:12207695). RIP occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein is first cut periplasmically (site-1 protease, S1P, PrsW) (PubMed:16816000, PubMed:17020587), then within the membrane itself (site-2 protease, S2P, RasP) (PubMed:15130127), while cytoplasmic proteases finish degrading the anti-sigma factor, liberating sigma-W (PubMed:16899079).
The cytoplasmic domain is able to inactivate SigW and the extracellular and transmembrane domains are crucial for sensing and transducing the signal that triggers SigW activation (PubMed:15130127). The N-terminus binds the zinc ion and is followed by a long helix (about residues 40-80) that fits into a hydrophobic surface groove on SigW, probably blocking its ability to interact with the -10 and -35 promoter elements (PubMed:28319136).
Belongs to the cyclophilin-type PPIase family.
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Confers resistance to puromycin, tosufloxacin and norfloxacin.
Expression is dependent on the growth phase and decreases in the late log phase.
Bacitracin is thought to be involved in the inhibition of peptidoglycan synthesis by sequestering undecaprenyl diphosphate, thereby reducing the pool of lipid carrier available.
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Disruption results in a marked decrease of resistance to bacitracin.
Expression is sigma M, sigma X and sigma I-dependent. Induced by vancomycin and bacitracin, via sigma M. Expression is maximal during early exponential phase and decreases during stationary phase.
Belongs to the thioredoxin family. ResA subfamily.
Thiol-disulfide oxidoreductase which is required in disulfide reduction during c-type cytochrome synthesis. May accept reducing equivalents from CcdA, leading to breakage of disulfide bonds in apocytochrome c; following this reduction heme can be covalently attached.
Thiol-disulfide oxidoreductase which is required in disulfide reduction during c-type cytochrome synthesis. May accept reducing equivalents from CcdA, leading to breakage of disulfide bonds in apocytochrome c; following this reduction heme can be covalently attached. Does not play a role in sporulation.
Required for the development of competence.
Transcriptional repressor of the gluconate operon (gntRKPZ), which encodes the proteins for gluconate utilization. Represses mRNA synthesis by binding to the gnt operator; the binding is suppressed by gluconate or glucono-delta-lactone.
Expression is repressed by the HTH-type transcriptional regulator GamR.
The PTS EIIA type-1 domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the PTS EIIB type-1 domain.
The PTS EIIC type-1 domain forms the PTS system translocation channel and contains the specific substrate-binding site.
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system may be involved in glucosamine transport.
Cells lacking this gene show normal growth and sporulation.
Displays serine protease activity. Seems to have a broad substrate specificity.
Is completely inhibited by phenylmethanesulphonylfluoride (PMSF) in vitro.
Is expressed during the late stationary phase of growth. Is down-regulated by SinR.
ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner (By similarity).
Homohexamer. Organized in a ring with a central cavity (By similarity).
Restricted to the prespore compartment of sporulating cells.
Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis.
This enzyme is monofunctional, and its activity is unaffected by the end-product aromatic amino acids.
Negative regulatory protein for the citA gene for citrate synthase I.
Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella and sporulation. Could play a role in mother cell lysis with CwlC.
Expressed during the late sporulation phase.
Forms a complex with TatCd. Two types of complexes exist: one composed of TatAd and TatCd, and another composed only of TatAd. Soluble TatAd forms homomultimers bigger than 100 kDa. Soluble TatAd associates in homomultimeric micelle-like particles with a size of about 12 or 25 nm in diameter as well as in elongated particles of 12 nm in diameter.
Membrane-localization and maintenance of TatAd is assisted by TatCd.
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system. Required for PhoD secretion. The cytosolic fraction of TatAd binds the precursor of PhoD.
Asporogeneous; spore development starts but does not develop the spore cortex.
Expressed during sporulation; strong expression 60-150 minutes after sporulation onset, falls to background expression by 240 minutes. Found only in mother cells.
Penicillin-binding protein with an unknown catalytic activity. May have a specialized role in the morphogenesis of spore cortex, which is a modified form of peptidoglycan. Spore cortex formation is determined primarily by the mother cell.
Catalyzes the sodium-dependent uptake of extracellular L-proline.
Catalyzes the uptake of extracellular proline under high-osmolarity growth conditions. Essential for the use of proline present in the environment as an osmoprotectant.
Disruption of the gene eliminates the osmotically stimulated proline transport activity and practically abolishes the ability to use proline as an osmoprotectant.
Induced under high-osmolarity growth conditions. Has two osmoregulated and tightly spaced promoters. The first promoter is sigma A-dependent and the second promoter is controlled by the general stress transcription factor sigma B.
Belongs to the arabinose isomerase family.
Catalyzes the conversion of L-arabinose to L-ribulose.
Expressed only in the forespore compartment of sporulating cells. Disappears after 45 minutes of spore germination.
By oxidative stress and by growth in minimal medium lacking iron (Fe(3+)), or one of the divalent cations manganese, copper or cobalt.
Forms highly stable, multimeric protein-DNA complexes which accumulate in stationary-phase cells and protect against oxidative killing.
Belongs to the helicase family. PriA subfamily.
Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA.
Protein that helps load RecA onto ssDNA during transformation (PubMed:17803906, PubMed:25138221). Binds cooperatively to circular ssDNA, is able to bridge different segments of DNA (PubMed:17803906). Favors the loading of RecA onto SsbA- or SsbB-coated ssDNA and formation of RecA-DNA filaments (PubMed:25138221). RecA-ATP cannot catalyze homologous DNA strand exchange; SsbA and DprA activate strand exchange by RecA-ATP (PubMed:25138221).
Transformation efficiency drops 50- to 100-fold (PubMed:11918817, PubMed:11948146).
Disruption of this gene has no effect on vegetative growth but causes a sporulation defect, characterized by very low sporulation frequencies and heat-sensitive spores devoid of DPA, which can be cured by supplementation with dipicolinate.
Together with DpaA, catalyzes the conversion of dihydrodipicolinate to dipicolinate (DPA), which constitutes up to 10% of the dry weight of the spore.
Together with DpaA, catalyzes the conversion of dihydrodipicolinate to dipicolinate (DPA).
Catalyzes the formation of agmatine from arginine.
Was originally (Ref.1) thought to be a lysine decarboxylase and was consequently named cad.
Involved in the metabolism of the antibiotic polyketide bacillaene which is involved in secondary metabolism. The substrate is dihydrobacillaene.
Induced by mitomycin C (MMC) and UV, and this requires RecA. Also induced by hydrogen prexoxide.
Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
Cells lacking this gene are auxotrophic for glycerol.
Involved in the biosynthesis of the sn-glycerol 3-phosphate required for phospholipid synthesis.
Slightly inhibited by sn-glycerol 3-phosphate.
Responsible for synthesis of pseudouridine from uracil-2633 in 23S ribosomal RNA.
Putative monooxygenase that may contribute to the degradation of aromatic compounds.
Strongly induced by stress due to exposure to 6-brom-2-vinyl-chroman-4-on (chromanon) and less strongly induced after exposure to 2-methylhydroquinone (2-MHQ) or catechol stress.
Active between T2 and T6 of sporulation.
May be involved in fructose recognition during germination.
Stimulates the phosphotransfer from phospho-DegS to DegU. Affects protease and levansucrose production.
Transcriptionally regulated by fur; repressed by iron.
Belongs to the AzlD/HI_1737/HP1330 family.
4'-phosphopantetheine is transferred from CoA to a specific serine of apo-DCP.
Carrier protein involved in the D-alanylation of lipoteichoic acid (LTA). The loading of thioester-linked D-alanine onto DltC is catalyzed by D-alanine--D-alanyl carrier protein ligase DltA. The DltC-carried D-alanyl group is further transferred to cell membrane phosphatidylglycerol (PG) by forming an ester bond, probably catalyzed by DltD. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall.
Part of the ABC transporter complex YfmCDEF involved in citrate-dependent Fe(3+) import. Binds citrate-dependent Fe(3+) and delivers it to the surface of YfmDE (Probable).
Branched-chain amino acid transport system which is involved in the uptake of isoleucine, valine and probably leucine (PubMed:25645558). Can also transport threonine, and is active as a minor serine permease (PubMed:25645558, PubMed:32743959). May be an amino acid permease of rather broad specificity, because several amino acids, albeit at 100-fold excess, are able to prevent isoleucine uptake (PubMed:25645558). Probably does not transport methionine (PubMed:25645558). Together with BraB and BrnQ, plays an important role in the activation of CodY, a branched-chain amino acid-responsive transcriptional regulator that controls the expression of several dozen transcription units in B.subtilis (PubMed:25645558).
Expression is repressed by the transcriptional regulator CodY (PubMed:12618455, PubMed:21097623). Contains two CodY-binding sites in the bcaP regulatory region, which both contribute to repression in vivo and do so independently of each other (PubMed:21097623). A single CodY-binding site is apparently sufficient for substantial CodY-dependent regulation, but both upstream and downstram CodY-binding regions are required for maximal repression of bcaP (PubMed:21097623). Efficient bcaP repression by CodY requires the simultaneous presence of isoleucine, leucine and valine, and other amino acids in the growth medium (PubMed:21097623).
Isoleucine uptake is efficiently reduced in the presence of 100-fold excess valine, leucine, alanine, threonine, serine, cysteine, asparagine, and a nonproteinaceous amino acid 4-azaleucine.
Mutant is still able to take up isoleucine, leucine and valine (PubMed:25645558). Deletion of the gene confers a weak resistance to growth inhibition by serine (PubMed:32743959). The deletion of the three permease-encoding genes aimA (ybeC), ybxG and bcaP results in an unprecedented resistance to serine up to 100 mM (PubMed:32743959).
Probable component of primosome involved in the initiation of DNA replication. It is essential for both replication initiation and membrane attachment of the origin region of the chromosome and plasmid pUB110.
The two mutants dna-1 (dnaBI) and dnaB-19 (dnaBII) show different characteristics for replication and membrane binding of plasmid pUB110. DnaBI is essential for both chromosome and pUB110 replication, whereas dnaBII is necessary only for chromosome replication.
GudB seems to be intrinsically inactive, however spontaneous mutations removing a 9-bp direct repeat within the wild-type gudB sequence activated the GudB protein and allowed more-efficient utilization of amino acids of the glutamate family (called gutB1). This 3 amino acid insertion presumably causes severe destabilization of the fold of the protein, leading to an inactive enzyme that is very quickly degraded. The cryptic GudB serves as a buffer that may compensate for mutations in the rocG gene and that can also be decryptified for the utilization of glutamate as a single carbon source in the absence of arginine. It is unable to synthesize glutamate.
No visible phenotype. Cells lacking this gene show no growth defect; a double rocG-gudB disruption has the same phenotype as a single rocG disruption.
Can also bind other divalent metal ions (zinc, cobalt and nickel), but these metals are poor regulators of DNA binding.
Cells lacking this gene display a slightly enhanced ability to grow into medium containing high levels of copper.
Copper-sensitive repressor that has a key role in copper homeostasis. Negatively regulates expression of the copZA operon and of ycnJ. In the absence of copper ions, binds with high affinity to the copZA promoter and represses the transcription. In the presence of copper ions, CsoR binds Cu(1+), which significantly decreases its DNA binding affinity and leads to the transcription of the genes.
Homotetramer. Binds DNA with a stoichiometry of 2 tetramers per DNA.
Maximally expressed at stationary phase.
Regulates expression of the cell division protein ftsW, and is essential for cell viability during stationary phase.
Belongs to the DNA polymerase type-C family.
The glycine cleavage system catalyzes the degradation of glycine.
The glycine cleavage system is composed of four proteins: P, T, L and H.
In the presence of nicotinic acid represses transcription of the nadBCA and nifS-nadR operons. Also binds to DNA upstream of the niaP gene, probably regulating it as well. May bind nicotinic acid.
It is uncertain whether Met-1 or Met-8 is the initiator.
No visible phenotype when grown in the absence of nicotinic acid.
Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end.
Required for the morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end (By similarity).
Part of the ABC transporter complex TcyJKLMN involved in L-cystine import. Probably responsible for the translocation of the substrate across the membrane (Probable). Is also involved in cystathionine, djenkolate, and S-methylcysteine transport.
Catalyzes the two successive C-2 and C-7 methylation reactions involved in the conversion of uroporphyrinogen III to precorrin-2 via the intermediate formation of precorrin-1. It is a step in the biosynthesis of both cobalamin (vitamin B12) and siroheme.
Belongs to the 3-oxoacid CoA-transferase subunit B family.
Activated by phosphoenolpyruvate (PEP) and by high concentrations of monovalent cations, NH(4)(+) being most effective. Is inhibited by two types of compounds which apparently act on the enzyme at different sites. The first group consists of nucleoside monophosphates (most effective are AMP and dAMP), phosphorylated coenzymes, and denatured DNA and RNA, whose inhibition is competed by PEP. The second group, whose inhibition is not competed by PEP, consists of highly phosphorylated nucleotides (pppGpp and pppApp are most effective), nucleoside di- and triphosphates, and PPi.
Constitutively expressed. Expressed at a fairly constant level in cells undergoing glycolysis or gluconeogenesis.
Disruption of fbp alone (or ywjI alone) does not affect growth on various carbon sources. But the ywjI fbp double mutant is unable to grow with carbon sources demanding FBPase activity, i.e. glycerol, malate, and a mixture of succinate and glutamate.
Belongs to the FNT transporter (TC 2.A.44) family.
Together with YxlD is important for negative regulation of sigma Y activity.
Part of the ABC transporter complex GlnHMPQ involved in glutamine transport.
Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
Folds into two domains, a large PLP-binding domain (residues 63-276) and a small C-terminal domain.
Involved in pectin degradation (PubMed:29240795). Part of the ABC transporter complex YtcQP-YteP involved in the uptake of polygalacturonan and rhamnogalacturonan type I (PubMed:29240795). Responsible for the translocation of the substrate across the membrane (Probable).
Polyol dehydrogenase that catalyzes the NAD(+)-dependent oxidation of various sugar alcohols. Is mostly active with D-sorbitol (D-glucitol), xylitol and L-iditol as substrates, leading to the C2-oxidized products D-fructose, D-xylulose and L-sorbose, respectively.
Component of a complex that catalyzes the oxidation of glycolate to glyoxylate.
Forms a heterotetramer with UvrA during the search for lesions. Interacts with UvrC in an incision complex.
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
The beta-hairpin motif is involved in DNA binding.
Negative regulation of glyA transcription and kinB-dependent sporulation.
Contains a small N-terminal 3-helix bundle domain and a large C-terminal TPR domain, connected by a linker region (PubMed:22215984, PubMed:23526880). The 3-helix bundle domain and the linker region form the ComA binding surface (PubMed:22215984, PubMed:23526880). A RapF surface mimics DNA to block ComA binding to its target promoters (PubMed:22215984). Interacts with PhrF via the TPR domain (PubMed:23526880).
Inhibited by PhrF, which prevents RapF-ComA interaction (PubMed:15968044, PubMed:16816200, PubMed:22215984, PubMed:23526880). Interaction with PhrF induces a conformational change in RapF, which is propagated to the ComA binding site and causes the dissociation of ComA from RapF (PubMed:22215984, PubMed:23526880).
Involved in the regulation of genetic competence development (PubMed:15968044, PubMed:16816200). Inhibits the activity of ComA, a transcriptional factor that regulates the development of genetic competence (PubMed:15968044, PubMed:16816200, PubMed:22215984, PubMed:23526880). Acts by binding to ComA, leading to the inhibition of its DNA-binding activity (PubMed:15968044, PubMed:22215984, PubMed:23526880). May also affect transcription independently of ComA (PubMed:16816200).
Monomer (PubMed:22215984). Is monomeric either alone or in complex with PhrF (PubMed:22215984). Interacts specifically with the C-terminal DNA-binding domain of ComA (PubMed:15968044, PubMed:22215984). Interacts with PhrF (PubMed:15968044, PubMed:22215984, PubMed:23526880).
Part of the rapF-phrF operon, which is controlled by ComA.
RapF and PhrF pair of proteins acts synergistically with RapC and CSF in the overall regulation of the ComA transcription factor.
Unknown; dispensable for production of the lantibiotic sublancin 168 and for competence for DNA uptake.
A Cys to Ala mutation in SufU (Cys-41-Ala) has been described to be a competivie inhibitor of SufS activity and a non-competitive inhibitor (PubMed:21236255, PubMed:24321018).
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. Csd subfamily.
Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine.
Homodimer (PubMed:27382962). Interacts with SufU; this interaction induces an opening of the active site pocket of SufS (PubMed:27382962). Interacts with frataxin/Fra (PubMed:27382962).
Type II cysteine desulfurase that acts as the initial step in the SUF-like Fe-S cluster assembly pathway. Catalyzes the removal of elemental sulfur atoms from L-cysteine by using the cofactor pyridoxal 5'-phosphate (PLP), resulting in the production of L-alanine and persulfide (PubMed:31587510). Activity is stimulated by SufU, which acts as a sulfurtransferase that receives sulfur from SufS via a zinc-ligand swapping mechanism and transfers it to SufB (PubMed:29235855, PubMed:27382962).
Belongs to the TACO1 family. YeeN subfamily.
Component of a cohesin-like complex composed of ScpA, ScpB and the Smc homodimer, in which ScpA and ScpB bind to the head domain of Smc. The presence of the three proteins is required for the association of the complex with DNA.
Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpB that pull DNA away from mid-cell into both cell halves.
Represses sigma(D)-dependent flagellar genes and activate the eps and yqxM operons. Repressor activity is regulated by SlrA. Controls the initiation of biofilm formation.
Belongs to the mandelate racemase/muconate lactonizing enzyme family. MenC type 2 subfamily.
Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 2-succinylbenzoate (OSB) (PubMed:10194342). Does not show detectable N-acylamino acid racemase (NAAAR) activity with N-acetyl-S-methionine as substrate (PubMed:10194342).
Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 2-succinylbenzoate (OSB).
Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.
Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers.
Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.
Proteome analysis shows that a mutant overexpresses SAM synthase by comparison to wild-type.
A SwrC-deficient strain is susceptible to acriflavine and ethidium bromide, and showed severer growth inhibition as surfactin concentration increased up to 100ug/ml.
Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family.
Required for self-resistance to surfactin, an antimicrobial lipopeptide surfactant produced by B.subtilis. Also required for swarming motility.
Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria.
Binds c-di-AMP (PubMed:31061098, PubMed:33619274, PubMed:35130724, PubMed:35714772). Binding of c-di-AMP to DarB inhibits the interaction with RelA and PYC (PubMed:33619274, PubMed:35130724).
Homodimer (PubMed:33619274, PubMed:35714772). Forms a homodimer with a parallel, head-to-head assembly of the monomers (PubMed:35714772). Under conditions of potassium starvation and corresponding low c-di-AMP levels, apo-DarB specifically interacts with the N-terminal region of the RelA (PubMed:33619274). Under the same conditions, apo-DarB also specifically interacts with the C-terminal part of the pyruvate carboxylase (PubMed:35130724).
Involved in the c-di-AMP-dependent regulation of the bacterial stringent response (PubMed:33619274, PubMed:35130724). Modulates the activities of at least two enzymes under conditions of potassium limitation (PubMed:33619274, PubMed:35130724). Apo-DarB regulates the activity of the GTP pyrophosphokinase RelA by interacting directly with RelA, leading to stimulation of (p)ppGpp synthesis and induction of the stringent response (PubMed:33619274). Apo-DarB also regulates pyruvate carboxylase (PYC) at two levels: directly at the protein level by binding to the enzyme and stimulating the synthesis of oxaloacetate and indirectly, by interaction with RelA, which leads to activation of the stringent response and to the increased expression of the pycA gene (PubMed:35130724). Stimulation of these enzymes by DarB is prevented in the presence of cyclic di-AMP (c-di-AMP) (PubMed:33619274, PubMed:35130724).
No conformational changes occur upon c-di-AMP binding.
Belongs to the bacterial ribosomal protein bL34 family.
Belongs to the Ap4A hydrolase YqeK family.
Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate (Ap4A) to yield ADP.
Mutant shows increased levels of Ap4G, Ap4U, Ap3A and Ap4A (PubMed:32152217). Cells form pellicles that are initially flat and thin. The pellicles finally become thicker, their flat surfaces are broken by a number of broad pits, the inner surface of which are covered with fruiting bodies. The colonies also show a defect in gross morphology, in that their central region is flat ang glossy (PubMed:15175311).
Abolishes riboflavin uptake, cell growth less inhibited by roseoflavin.
Belongs to the prokaryotic riboflavin transporter (P-RFT) (TC 2.A.87) family.
Forms a stable energy-coupling factor (ECF) transporter complex composed of a membrane-embedded substrate-binding protein (S component), 2 ATP-binding proteins (A component) and 2 transmembrane proteins (T component). May be able to interact with more than 1 S component at a time (By similarity).
Inhibited by excess of riboflavin or FMN. Also inhibited by protonophores such as CCCP and FCCP or in the absence of glucose.
Mediates uptake of riboflavin and roseoflavin, a toxic riboflavin analog; may also transport FMN. Probably a riboflavin-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. The substrates themselves are bound by transmembrane, not extracytoplasmic soluble proteins (By similarity).
Probably a riboflavin-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex.
Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
Cells form colonies in which certain architectural features are absent or less prominent than those observed in wild-type colonies. The Ecs activity could be important for the development of communities.
Presumed to form part of an ABC-transporter, it may form a transport channel.
A possible function for this protein is to guide the assembly of the membrane sector of the ATPase enzyme complex.
Expression is initiated around the second hour of sporulation and continues throughout development. May be expressed predominantly in the mother cell.
Required for assembly of a normal spore coat. May be a component of the innermost layer of the spore coat that aids in its adherence to the prespore.
Immunity component of one of 6 LXG toxin-immunity modules in this strain. They promote kin selection, mediate competition in biofilms, and drive spatial segregation of different strains, indicating that LXG toxins may help avoid warfare between strains in biofilms. Mediates intercellular competition during biofilm formation; disruption of the operon disadvantages the bacteria, but overexpression of the cognate immunity protein restores growth in competition with wild-type. In situ neutralizes the toxic effect of cognate toxin YqcG (PubMed:34280190). Probably neutralizes the ability to inhibit growth of cognate toxin YwqJ. Probably does not have immunity protein activity on other LXG toxins (Probable).
Probably interacts with cognate toxin YwqJ but not with other non-cognate LXG toxins. The interaction inhibits the toxic activity of YwqJ.
The phosphoserine observed at Ser-999 and Ser-2040 in PubMed:17218307 may result from the secondary neutral loss of pantetheine from the phosphodiester linked cofactor.
Catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to produce 2-keto-3-deoxy-6-phosphogluconate (KDPG).
Belongs to the ribonucleoside diphosphate reductase large chain family.
Under complex allosteric control mediated by deoxynucleoside triphosphates and ATP binding. The type of nucleotide bound at the specificity site determines substrate preference. It seems probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction (By similarity).
8-fold induction by growth at 15 degrees Celsius.
Cells grow much more slowly at 15 degrees Celsius.
Controls the transcription of the pur operon for purine biosynthetic genes, binds to the control region of the operon. DNA binding is inhibited by 5-phosphoribosyl 1-pyrophosphate.
Belongs to the adenylate cyclase family. DacB/CdaS subfamily.
Expressed under control of the sigma-G factor in the forespore.
Forms dimers and probably also hexamers; the dimer may be active while the hexamer may not be active.
No effect on antibiotic sensitivity to the beta-lactam antibiotic cefuroxime (CEF), upon overexpression of the c-di-AMP phosphodiesterase GdpP increased sensitivity to CEF (PubMed:22211522). Double disA-cdaA mutants cannot be made, suggesting they are lethal, while double disA-cdaS and cdaA-cdsS mutants are viable (PubMed:22211522, PubMed:23192352). In single deletions of this gene, germination efficiency is decreased (PubMed:24939848).
One of 3 paralogous diadenylate cyclases (DAC) in this bacteria, catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP) (Probable). Upon expression in E.coli leads to c-di-AMP synthesis (PubMed:23192352, PubMed:24939848). Overexpression of the hyperactive mutant (L44F) in the absence of c-di-AMP phosphodiesterase GdpP leads to growth defects in log phase (long curly cell filaments) that disappear upon sporulation; spore formation is normal, showing sporulation is insensitive to the excess c-di-AMP (PubMed:23192352). In B.subtilis c-di-AMP is a second messenger that mediates growth, DNA repair and cell wall homeostasis; it is toxic when present in excess.
Probably expressed only during sporulation in the forespore.
The N-terminus (residues 1-69) is thought to form 2 alpha-helices that allow dimerization and probable hexamerization; this region inhibits DAC activity of the rest of the protein (PubMed:24939848).
Part of the ABC transporter complex YkoCDEF that could transport hydroxymethylpyrimidine (HMP) and/or thiamine. Could also transport other HMP-containing products. Probably responsible for the translocation of the substrate across the membrane (Probable).
Response regulator in the two-component regulatory system ComP/ComA involved in a major quorum response pathway that regulates the development of genetic competence. Regulates directly the expression of over 20 genes, including genes of the srfA operon, degQ, rapA, rapC, rapE, rapF, etc. Regulates indirectly, through the regulation of comK transcription, the expression of late competence genes.
Binds with high affinity to both apo-bacillibactin and iron-bacillibactin.
In iron-limited conditions, activates expression of the feuABCybbA operon, which encodes the bacillibactin uptake system. Acts by binding directly to a conserved direct repeat element upstream of the feuA promoter. Activity is increased in the presence of bacillibactin.
Cells lacking this gene reveal a loss of rod shape, irregular septation, multicompartmentalized cells, and thickened cell walls. It also induces a decrease in isoprene production.
Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP).
By rhamnogalacturonan type I (RG-I), a component of pectin from the plant cell wall.
Probable transcription factor regulating the pathway responsible for rhamnogalacturonan depolymerization.
Required specifically for induction of eps and yqxM operons by antagonizing SinR. Regulates SlrR activity. Controls the initiation of biofilm formation.
Belongs to the UPF0073 (Hly-III) family.
Belongs to the GTP cyclohydrolase IV family.
Converts GTP to 7,8-dihydroneopterin triphosphate.
Was originally thought to be a zinc uptake system.
Belongs to the Orn/Lys/Arg decarboxylase class-II family. LysA subfamily.
Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine.
By different stresses, such as ethanol, salt, and phosphate starvation, in a partially sigma-B dependent manner. Transcribed under partial control of SigM ECF sigma factor (PubMed:17434969).
Cells lacking this gene display decreased survival rates during salt stress conditions.
Heterodimer of a subunit alpha and a subunit beta.
No visible phenotype. Spores have normal morphology, heat-resistance, cortex structure, and germination and outgrowth properties.
Penicillin-binding protein with an unknown catalytic activity. Penicillin-binding proteins (PBPs) function in the late steps of murein biosynthesis. Beta-lactams inactivate the PBPs by acylating an essential serine residue in the active site of these proteins, thereby interrupting normal cell wall synthesis.
Sporulation specific. Expression starts 1 to 2 hours after the initiation of sporulation. Found only in mother cells.
CWBP52 is a serine-type protease that could be involved in proteoglycan peptide bridges.
Cells lacking this gene have no discernible phenotype with respect to sporulation, motility or growth (PubMed:9004506). Significantly increased amounts of BglS, Epr, Vpr, YclQ and YwsB; decreased amounts of AbnA, PorE, Csn, YncM, Yxal and YweA are detected in the extracellular proteome (PubMed:11987133).
Proteolytically cleaved to yield CWBP23 and CWBP52.
The CWBP52 polypeptide was originally called CWBP55 based on its apparent molecular weight.
Binds 2 divalent metal cations per subunit. Magnesium or manganese.
Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.
In the C-terminal section; belongs to the GTP cyclohydrolase II family.
In the N-terminal section; belongs to the DHBP synthase family.
May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with Spo0H (a sigma factor) to control the expression of some genes that are critical to the sporulation process. Repressor of abrB, activator of the spoIIa operon. Binds the DNA sequence 5'-TGNCGAA-3' (0A box).
May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with spo0H (a sigma factor) to control the expression of some genes that are critical to the sporulation process.
Stage 0 mutants lack the ability to form the asymmetric septum characteristic of the initiation of the sporulation process.
Mediates positive regulation of the glucanase operon (licST) by functioning as an antiterminator factor of transcription. Prevents termination at terminator lic-t.
Required for sporulation. Plays an important role in cortex and coat formation.
Monomer and homodimer. Part of the essential Sec protein translocation apparatus which comprises SecA, SecYEG and auxiliary proteins SecDF. Other proteins may also be involved.
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Part of the essential Sec protein translocation apparatus which comprises SecA, SecYEG and auxiliary proteins SecDF. Other proteins may be involved. Monomer and many different homodimers can be isolated (PubMed:16989859), some of which are not formed in the presence of a synthetic signal peptide. A single SecA monomer interacts with SecY in the channel. Only shows some colocalization with FloA or FloT membrane assemblies (PubMed:27362352).
Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Major component for energy conversion during vegetative growth. Subunit II transfers the electrons from a quinol to the binuclear center of the catalytic subunit I (By similarity).
Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Subunit II transfers the electrons from a quinol to the binuclear center of the catalytic subunit I.
Positively regulated by SigO and its coactivator RsoA.
Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Prokaryotic type I sub-subfamily.
Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Disruption mutant contains no phosphatidylethanolamine and accumulates phosphatidylserine, but it grows well without supplementation of divalent cations.
Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit.
Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase.
Catalyzes DD-carboxypeptidase and transpeptidation reactions.
Expression starts at the end of the exponential phase and peaks two hours into sporulation. There is no enzyme activity in spores.
Between 94.7% and 99.7% of the 5'-GACGAG-3' motifs are methylated on A-5 in strain NCIMB 3610 and PY79 respectively. The sites are enriched on the left chromosomal arm.
No visible growth defects, no A-5 methylation of 5'-GACGAG-3' in strains NCIMB 3610 or PY79. Decreased promoter activity for promoters with the target sequence very close to the -35 SigA-binding box (scpA, hbs, rnhC, yumC and zapA).
Recognizes the double-stranded sequence 5'-GACGAG-3' and methylates A-5, yielding m6A. m6A methylation functions as a transcriptional modifier, promoting transcription of a number of genes (at least scpA, hbs, rnhC, yumC and zapA). One studied mechanism is via transcriptional repressor ScoC (also called hpr) which binds to non-methylated scpA promoter; when the m6A target is methylated ScoC no longer binds and scpA transcription is up-regulated. Other mechanisms for gene expression regulation probably exist. Binds DNA with and without the target sequence. Although it resembles a restriction-modification system, it does not have detectable endonuclease activity under tested conditions (PubMed:32324221). A gamma subtype methylase (PubMed:12654995).
Belongs to the HAD-like hydrolase superfamily. NagD family.
Catalyzes the dephosphorylation of 2-6 carbon acid sugars in vitro.
Catalyzes the hydrolysis of various purine and pyrimidine 5'-nucleotides, showing preference for 5'-nucleoside monophosphates and exhibiting the highest catalytic activity toward 5'-XMP (PubMed:27907199). Shows also a relatively high phosphohydrolase activity toward the nucleotide precursors ribose-5-phosphate (R5P) and 5-phosphoribosyl-1-pyrophosphate (PRPP), and toward the non-natural substrate p-nitrophenyl phosphate (pNPP) (PubMed:27907199).
Cotranscribed with the two upstream genes, yutD and yutE. YutF overproduction increases the level of yutDEF operon expression, and this up-regulation is enhanced in the presence of inorganic phosphate.
Divalent metal ions. Mg(2+) is the most effective.
Inactivation of the gene has essentially no effect on cell growth in rich or minimal medium but results in a drop in pNPP hydrolysis in the crude extracts of B.subtilis cells to undetectable levels.
In the C-terminal section; belongs to the PEP-utilizing enzyme family.
Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-phosphate.
In the C-terminal section; belongs to the HTP reductase family.
In the N-terminal section; belongs to the cytidine and deoxycytidylate deaminase family.
Plays a role in DNA replication and termination (fork arrest mechanism). Two dimers of rtp bind to the two inverted repeat regions (IRI and IRII) present in the termination site. The binding of each dimer is centered on an 8 bp direct repeat.
Involved in the biosynthesis of kanosamine (3-amino-3-deoxy-D-glucose), which is known to have antibiotic and antifungal properties, and to be a precursor of the antibiotic neotrehalosadiamine (3,3'-diamino-3,3'-dideoxy-alpha,beta-trehalose (NTD)). Catalyzes the oxidation of glucose 6-phosphate to 3-oxo-D-glucose 6-phosphate. It can only use NAD.
Could be the product of a pseudogene. This sequence is shorter than orthologs and lacks the NAD(P)-binding motif.
Acts on ADP-mannose and ADP-glucose as well as ADP-ribose. Prevents glycogen biosynthesis. The reaction catalyzed by this enzyme is a limiting step of the gluconeogenic process (By similarity).
Belongs to the Nudix hydrolase family. NudF subfamily.
To type I restriction system adenine methylases.
Di-heme cytochrome of the succinate dehydrogenase complex.
Part of an enzyme complex containing three subunits: a flavoprotein, an iron-sulfur protein and cytochrome b-558.
Belongs to the vitamin uptake transporter (VUT/ECF) (TC 2.A.88) family. Q precursor transporter subfamily.
Involved in the import of queuosine (Q) precursors, required for Q precursor salvage.
Called 'metalloprotease', but clearly belongs to the S1B family of serine proteases.
Belongs to the class-II aminoacyl-tRNA synthetase family. HisZ subfamily.
Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine (By similarity).
Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
This function is generally fulfilled by the C-terminal part of HisG, which is missing in some bacteria such as this one.
Belongs to the LeuD family. LeuD type 1 subfamily.
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Belongs to the 'phage' integrase family. XerC subfamily.
Belongs to the pantothenate synthetase family.
Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
The reaction proceeds by a bi uni uni bi ping pong mechanism.
It is involved in the activation of genes necessary for anaerobic respiration.
The cysteine cluster which is probably involved in the coordination of the [4Fe-4S] cluster is located at the C-terminal part of the protein.
Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization.
Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization. The MinCD complex plays an important role in asymmetric septum formation during sporulation of B.subtilis cells.
Homotetramer in the absence of SinI. Heterodimer with SinI. Interaction with SinI disrupts the SinR tetramer and its repressor activity. Interacts with hpr.
Negative as well as positive regulator of alternate developmental processes that are induced at the end of vegetative growth in response to nutrient depletion. Binds to the alkaline protease (aprE) gene at two sites. Also acts as a repressor of the key sporulation gene spo0A. Negatively regulates transcription of the eps operon, which is responsible for the biosynthesis of an exopolysaccharide involved in biofilm formation; therefore it could govern the transition between a state in which bacteria swim or swarm and a state in which bacteria assemble into multicellular communities. Acts with Hpr as a corepressor of epr expression. Also negatively regulates transcription of the lutABC operon, which is required for lactate utilization. Repressor activity is regulated by SinI.
Repressed by fur. Induced by Btr in iron-limited conditions.
Strains lacking this gene show a reduction in growth stimulation by the catecholate siderophores enterobactin and bacillibactin.
Binding to the yetM cis sequence is clearly inhibited by kaempferol, morin, apigenin and luteolin, slightly inhibited by quercetin and galangin, but no inhibition is observed with the other flavonoids (PubMed:19329649). Flavonoid binding may induce conformational changes and modulate interaction with DNA (PubMed:35367827).
Homodimer (PubMed:19329649, PubMed:35367827). The N- and C-terminal helices from both subunits stabilize YetL dimer via extensive intersubunit interactions (PubMed:35367827).
Negatively regulates yetM expression and its own expression (PubMed:19329649). Binds specifically to corresponding single sites in the divergent yetL and yetM promoter regions, with higher affinity to the yetM region (PubMed:19329649). Recognizes a 28-mer operator of double-stranded DNA that contains a palindromic sequence (PubMed:35367827).
Belongs to the adenylosuccinate synthetase family.
Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Belongs to the thiolase-like superfamily. FabH family.
Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for branched chain acyl-CoA, determining the biosynthesis of branched-chain of fatty acids instead of straight-chain.
Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH.
Interacts with UvrB in an incision complex.
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
Binds a DNA inverted repeat of copZA operon.
Transcriptional activator of the copZA operon.
Phosphorylates the sporulation-regulatory proteins spo0A and spo0F. It also autophosphorylates in the presence of ATP.
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Resistance to tetracycline by an active tetracycline efflux. This is an energy-dependent process that decreases the accumulation of the antibiotic in whole cells. This protein functions as a metal-tetracycline/H(+) antiporter.
Part of the SecDF-YidC-YajC translocase complex. The SecDF-YidC-YajC translocase forms a supercomplex with SecYEG, called the holo-translocon (HTL).
The SecYEG-SecDF-YajC-YidC holo-translocon (HTL) protein secretase/insertase is a supercomplex required for protein secretion, insertion of proteins into membranes, and assembly of membrane protein complexes. While the SecYEG complex is essential for assembly of a number of proteins and complexes, the SecDF-YajC-YidC subcomplex facilitates these functions.
Involved in the response to the germinative mixture of L-asparagine, glucose, fructose and potassium ions (AGFK). Could be an amino acid transporter. Cannot stimulate germination in the absence of gerD and gerK gene products (fructose and glucose receptors, respectively).
Belongs to the glycosyltransferase 1 family. Bacterial/plant glycogen synthase subfamily.
Synthesizes alpha-1,4-glucan chains using ADP-glucose.
5'->3' double-stranded DNA exonuclease (By similarity). May play a role in mutation mismatch repair (MMR) (By similarity). Required for accurate coordination of cell division with DNA replication (PubMed:21169496). May play a role in cell wall metabolism (PubMed:21169496).
Binds 2 metal ions per subunit. The endogenous metal is unknown.
More frequent cell division over unsegregated chromosomes (PubMed:21169496). Increases frequency of nucleoid bisection (PubMed:21169496). Induces SOS induction in a subpopulation of cells (PubMed:21169496). Slightly elongated cells (PubMed:21169496). More sensitive to some cephalosporin antibiotics, such as cefotaxime, cefuroxime, and cefmetazole but not to cefoxitin or cefoperazone (PubMed:21169496). Increased sensitivity to moxalactam, a beta-lactam closely related to the cephalosporins, but not to the penicillin-like beta-lactam carbenicillin (PubMed:21169496).
Not essential for growth on minimal medium.
Belongs to the aldolase class II family. AraD/FucA subfamily.
Involved in the degradation of L-arabinose. Catalyzes the interconversion of L-ribulose 5-phosphate (LRu5P) and D-xylulose 5-phosphate (D-Xu5P) via a retroaldol/aldol mechanism (carbon-carbon bond cleavage analogous to a class II aldolase reaction).
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
Was originally suggested to be a nuclease that resolves Holliday junction intermediates during genetic recombination.
Belongs to the limonene-1,2-epoxide hydrolase family.
Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the internal cleavage of alpha-(1->5)-L-arabinofuranosyl residues of the alpha-1,5-L-arabinan to produce arabino-oligosaccharides and L-arabinose. It is also active toward linear branched sugar beet arabinan, and pectin from apple.
No visible phenotype. Double mutant abn2/abnA induce an almost complete loss of this activity.
Repressed by glucose, and induced by pectin and arabinan.
Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily.
Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding.
Homodimer. The tRNA molecule binds across the dimer.
Autophosphorylates on a histidine and transfers the phosphate group onto an aspartate in ComA, thus activating it.
Sensor in the two-component regulatory system ComP/ComA involved in a major quorum response pathway that regulates the development of genetic competence. Plays a role in sporulation, at least partly interchangeable with that of SpoIIJ. Probably activates ComA by phosphorylation.
Cells lacking this gene are unable to grow in medium containing glucose as a sole carbon source but presents the same growth rate as the wild-type in asparagine-containing medium.
Involved in the glycolysis. Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG.
Repressed by CggR and indirectly stimulated by CcpA.
May be involved in some transport function.
Belongs to the DNA mismatch repair MutS family. MutS2 subfamily.
Endonuclease that is involved in the suppression of homologous recombination and may therefore have a key role in the control of bacterial genetic diversity.
Belongs to the endoribonuclease YbeY family.
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
Belongs to the bacterial ribosomal protein bL25 family. CTC subfamily.
Cells sporulate poorly at 48 degrees Celsius.
Expressed at the end of exponential growth under conditions in which the enzymes of the TCA cycle are repressed.
Not required for exponential growth; probably functions in vegetatively growing cells, maybe required for accurate translation under stress conditions.
Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA. Binds to the 5S rRNA independently of L5 and L18.
Part of the ribosome (presumably the 50S subunit) under heat-stress but not control growth conditions. Binds 5S rRNA.
This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance.
Belongs to the thiazole tautomerase family.
Catalyzes the irreversible aromatization of 2-((2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene)ethyl phosphate (cThz*-P) to 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate (cThz-P), a step in the biosynthesis of the thiazole phosphate moiety of thiamine. Cannot use cThz* as substrate, indicating that the phosphate group is essential. Has no thiamine phosphate synthase activity, despite a high sequence similarity with ThiE.
Inactivation of this gene causes a delay in sporulation, but does not affect cell growth and the production of extracellular enzymes.
A probable RNA chaperone. Forms a complex with KhpA which binds to cellular RNA and controls its expression. Plays a role in peptidoglycan (PG) homeostasis and cell length regulation.
Belongs to the KhpB RNA-binding protein family.
Has an N-terminal Jag-N domain and 2 RNA-binding domains (KH and R3H).
By the natural cationic antimicrobial peptide LL-37 and the synthetic cationic antimicrobial peptide poly-L-lysine (PLL).
Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.
Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.
Involved in the modulation of the chemotaxis system; catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by CheR. B.subtilis has an effective methylation-independent adaptation system but must utilize the methylation system for adaptation to high concentrations of attractant.
Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Belongs to the NhaC Na(+)/H(+) (TC 2.A.35) antiporter family.
Is a secondary, electrogenic Na(+)/H(+) antiporter that catalyzes Na(+) uptake and proton efflux. Makes modest contributions to pH homeostasis in the alkaline range of pH but is not contributor to Na(+) resistance. Appears to have a repressive effect on growth and on alkaline phosphatases production in the presence of sodium, by affecting the transcription of the phoP/phoR two-component regulatory system.
The antiport activity is markedly inhibited by both valinomycin and CCCP, and modestly by nigericin.
This protein regulates the transcription of sigK, which encodes mother cell chamber RNA polymerase sigma-factor (sigma K).
By forming a complex with tryptophan-activated TRAP, and masking its RNA binding site, it inhibits TRAP's RNA binding ability, thereby abolishing TRAP regulation of gene expression, leading to antitermination and increased trp operon expression. AT acts by competing with messenger RNA for the RNA binding domain of TRAP.
By uncharged Trp tRNA, via the T-box transcription antitermination mechanism.
Expressed during both exponential and post-exponential growth (at protein level).
Is essential and sufficient to confer resistance to the bacteriocin sublancin 168.
Loss of resistance to the bacteriocin sublancin 168.
Belongs to the helicase family. DinG subfamily. Type 2 sub-subfamily.
Cells lacking this gene entirely lose the ability to produce bacilysocin and display a 10-fold reduction in the ability to form spores.
Phospholipase involved in the biosynthesis of the antibiotic bacilysocin. It probably catalyzes the hydrolysis of the 2-sn-acyl moiety of phosphatidylglycerol to produce bacilysocin (lysophosphatidylglycerol). Is also able to catalyze the hydrolysis reaction of one acyl bond in phosphatidylcholine in vitro (actual cleavage point is unknown), resulting in lysophosphatidylcholine.
Belongs to the shikimate dehydrogenase family.
Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
B.subtilis SleB could not be detected with anti-B.cereus SleB antiserum and vice versa.
Could be a lytic transglycosylase. Required for spore cortex hydrolysis during germination. Interacts strongly but noncovalently with spore components.
Expressed during sporulation and active during germination. Exists as mature but inactive form in the dormant spore.
Member of a two-component regulatory system MalK/MalR. Activates transcription of maeA, maeN and yflS in presence of malate by binding to their promoter region.
Activity is sensitive to salt concentration, a high concentration of KCL (500 mM) is needed for complete inactivation.
Does not impair growth on acetate. Disruption together with other acetoin utilization genes acuB and acuC results in poor growth and sporulation on acetoin or butanediol. Triple deletion of acuA, acuC and srtN improves the growth on acetate but it does not reach that of wild-type under low-acetate conditions.
Expression is maximal in stationary phase and is repressed by the addition of glucose to the growth medium. CcpA protein is required for glucose repression. Acetoin does not act as an inducer. Up-regulated during the 80 to 100 minutes of spore germination and into the outgrowth phase.
Part of the acuABC operon, which is possibly involved in the breakdown of acetoin and butanediol. Acts as an acetyltransferase inactivating acetyl-CoA synthetase AcsA via acetylation at a Lys residue.
Belongs to the UbiX/PAD1 family. YclB subfamily.
Involved in the non-oxidative decarboxylation and detoxification of phenolic derivatives under both aerobic and anaerobic conditions (PubMed:18388975). Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for phenolic acid decarboxylase (By similarity).
Involved in the non-oxidative decarboxylation and detoxification of phenolic derivatives. Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for phenolic acid decarboxylase.
Cells lacking this gene exhibit a slight increase in OxdC accumulation under acidic growth conditions and a huge increase under nonstress growth conditions.
Expression activated by ComK (PubMed:11918817). Positively regulated by SigO and its coactivator RsoA.
Negatively regulates RNA polymerase sigma factor SigO-dependent transcription. Prevents the expression or secretion of OxdC under nonstress conditions. May act as an anti-sigma factor.
Preferentially expressed in cells competent for DNA transformation; that is 5-15% of the population (PubMed:11918817).
Catalyzes both 1,3- and 1,5-keto-enol tautomerization of the diacid 2-hydroxymuconate (2-hydroxy-2,4-hexadienedioate) to produce 2-oxo-4-hexenedioate. This reaction is highly stereoselective and produces a mixture of stereoisomers, where the (3S)-isomer of 2-oxo-4-hexenedioate predominates. Also catalyzes the tautomerization of 2-hydroxymuconate to 2-oxo-3-hexenedioate, however this reaction is slower and occurs after the tautomerization of 2-hydroxymuconate to 2-oxo-4-hexenedioate. Using 2-hydroxy-2,4-pentadienoate, phenylenolpyruvate, (p-hydroxyphenyl)-enolpyruvate and 2-hydroxy-2,4-heptadiene-1,7-dioate, YwhB is a highly efficient 1,3-keto-enol tautomerase, but clearly not a 1,5-keto-enol tautomerase. Tautomerization of the two monoacids 2-hydroxy-2,4-pentadienoate and phenylenolpyruvate produces a mixture of stereoisomers, where the (3R)-isomers predominate.
The mono- and diacids apparently bind in different orientations in the active site of YwhB, but the highly stereoselective nature of the YwhB reaction using a diacid suggests that the biological substrate for YwhB may be a diacid.
Belongs to the sirtuin family. Class U subfamily.
NAD-dependent protein deacetylase which modulates the activities of several enzymes which are inactive in their acetylated form.
Cleaves the linkage of the L-alanine-D-glutamic acid of B.subtilis cell wall.
Expressed during vegetative growth phase.
Lack flagella. Altered cell surface properties including greater softness and lower density of the charged groups in the polymer layer.
Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body.
The basal body constitutes a major portion of the flagellar organelle and consists of a number of rings mounted on a central rod.
The basal body constitutes a major portion of the flagellar organelle and consists of a number of rings mounted on a central rod. In Gram-negative bacteria, at least four rings, L, P, S and M are present, whereas Gram-positive bacteria lack the L and P rings. The rod consists of about 26 subunits of FlgG in the distal portion, and FlgB, FlgC and FlgF build up the proximal portion of the rod with about 6 subunits each. Rod assembly occurs by export via the flagellum-specific pathway of its constituent proteins and by their incorporation into the rod structure in the probable order of FlgB, FlgC, FlgF and FlgG. Another protein, FliE, also assembles onto the stable rod structure.
Catalyzes the first step in the biosynthesis of NAD from nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate.
Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP.
Transiently phosphorylated on a His residue during the reaction cycle. Phosphorylation strongly increases the affinity for substrates and increases the rate of nicotinate D-ribonucleotide production. Dephosphorylation regenerates the low-affinity form of the enzyme, leading to product release.
Cleaves, in an endo-type manner, the gamma-glutamyl bond between D-glutamate and L-glutamate of poly-gamma-glutamate (PGA).
In stationary phase; under control of SigD.
Inhibited by pretreatment with 1 mM 4-(hydroxymercuri)benzoate, a sulfhydryl inhibitor.
DNA repair enzyme involved in the repair of deaminated bases. Selectively cleaves double-stranded DNA at the second phosphodiester bond 3' to a deoxyinosine leaving behind the intact lesion on the nicked DNA.
Deletion of the ywqH-ywqI-ywqJ-ywqK-nfi operon has no visible phenotype, however it is out-competed by wild-type cells.
Belongs to the bacterial solute-binding protein 2 family.
Part of the ABC transporter complex RbsABC involved in ribose import. Binds ribose.
The complex is composed of an ATP-binding protein (RbsA), two transmembrane proteins (RbsC) and a solute-binding protein (RbsB) (By similarity). Interacts with FloT (PubMed:23651456).
Belongs to the universal ribosomal protein uL23 family.
One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome.
Part of the 50S ribosomal subunit (PubMed:30126986). Contacts protein L29, and trigger factor when it is bound to the ribosome (By similarity).
Part of the 50S ribosomal subunit. Contacts protein L29, and trigger factor when it is bound to the ribosome.
Belongs to the universal ribosomal protein uL18 family.
Part of the 50S ribosomal subunit (PubMed:30126986). Part of the 5S rRNA/L5/L18/L25 subcomplex (Probable). Contacts the 23S rRNA and 5S rRNA (Probable). Required for catalysis of RNase M5 (PubMed:6432797).
Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S and 23S rRNAs.
Required for correct processing of both the 5' and 3' ends of 5S rRNA precursor, which is does in conjunction with ribonuclease M5 (RNase M5, rnmV). Possibly folds the 5S rRNA precursor into the correct conformation, thus acting as a chaperone.
This is one of the proteins that bind and probably mediate the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.
Belongs to the type-II 3-dehydroquinase family.
Catalyzes a trans-dehydration via an enolate intermediate.
Phe-23 is present instead of the conserved Tyr which is expected to be an active site residue.
Autocatalytically cleaves its own C-terminus.
Digestion of cleaved signal peptides (By similarity). Required for efficient processing of precursors under conditions of hyper-secretion. Has a preference for leucine-rich substrate peptides.
Homooctamer, assembles into a ring structure with a central cavity (PubMed:22472423, PubMed:24228759). Interacts with FloT (PubMed:23651456).
Belongs to the bacterial solute-binding protein 7 family.
Part of the binding-protein-dependent transport system for uptake of C4-dicarboxylates. Responsible for growth on fumarate and succinate but not malate. Is not directly involved in C4-dicarboxylate uptake, but plays a sensory role in the DctS/DctR two-component system which regulates the expression of the dctA C4-dicarboxylate transporter.
Belongs to the monovalent cation:proton antiporter 2 (CPA2) transporter (TC 2.A.37) family.
Belongs to the major facilitator superfamily. Organophosphate:Pi antiporter (OPA) (TC 2.A.1.4) family.
Responsible for glycerol-3-phosphate uptake.
Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.
Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate.
There are 2 substrate-binding sites: the catalytic A site, and the non-catalytic B site that may play a role in the transfer of substrate or product between the active site and the solvent. Alternatively, the B site may bind allosteric effectors.
Member of a two-component regulatory system MalK/MalR. Involved in the activation of maeA, maeN and yflS in presence of malate. Probably activates MalR by phosphorylation.
Belongs to the elongation factor P family.
Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase (By similarity).
Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
No sporulation at 37 or 47 degrees Celsius.
Required for swarming motility and for maximal sigma-D activity.
Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Belongs to the DNA mismatch repair MutL/HexB family.
Cells lacking this gene have an 80-fold increased spontaneous mutation frequency. A double mutS/mutL and a triple mutS/mutL/nth disruption has a 200 to 280-fold increased spontaneous mutation frequency.
This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex (By similarity). Overexpression of mutSL partially suppresses the high spontaneous mutation frequency of a ytkD/mutM/mutY triple disruption which lacks the system required to prevent damage by oxidized guanine (8-oxo-dGTP). This suggests that MutSL also functions to repair mismatches due to oxidative stress in both growing and stationary phase cells.
This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex.
Adapter protein required for efficient degradation of Spx by ClpXP under non-stress conditions (PubMed:17908206, PubMed:19074380, PubMed:24942655). Interaction with Spx stabilizes Spx and exposes the C-terminus of Spx for recognition and proteolysis by ClpXP (PubMed:24942655, PubMed:27191337). Is specific for Spx and does not enhance proteolysis by ClpCP protease (PubMed:19074380). Probably binds 2 zinc ions (PubMed:19074380).
Adapter protein required for efficient degradation of Spx by ClpXP under non-stress conditions. Interaction with Spx stabilizes Spx and exposes the C-terminus of Spx for recognition and proteolysis by ClpXP.
Expressed throughout cell growth. Negatively influences its own expression.
Interacts with Spx (PubMed:19074380, PubMed:24942655, PubMed:27191337). Interacts with SpxO/YuzO (PubMed:21378193).
Irreversible aggregation upon several stress conditions prevents interaction with Spx and therefore leads to Spx stabilization (PubMed:25353645). Inhibited by interaction with SpxO/YuzO (PubMed:21378193).
Strains lacking this gene show poor growth, affected sporulation, complete loss of competence development and overproduce Spx under unperturbed growth. Mutants also overproduce TrxA and show reduced sensitivity to disulfide stress.
The histidine-rich N terminus is essential for interaction with Spx.
Belongs to the queuine tRNA-ribosyltransferase family.
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Homodimer. Within each dimer, one monomer is responsible for RNA recognition and catalysis, while the other monomer binds to the replacement base PreQ1.
Cells lacking this gene lose the ability to utilize proline, ornithine, or arginine as sole carbon source and grow more slowly when proline or ornithine is utilized as sole nitrogen source in the presence of glucose. A double rocG-gudB disruption has the same phenotype as a single rocG disruption.
Devoted to catabolic function of glutamate (and other amino acids of the glutamate family) utilization as sole nitrogen source. It is not involved in anabolic function of glutamate biosynthesis since B.subtilis possesses only one route of glutamate biosynthesis from ammonia, catalyzed by glutamate synthase. Wild-type cells are unable to utilize glutamate or glutamine as a sole carbon source; thus RocG does not function physiologically to synthesize glutamate, but it is involved in the utilization of arginine, and proline as carbon or nitrogen source (PubMed:9829940). The catabolic RocG is essential for controlling gltAB expression via an inhibitory interactions with the transcriptional regulator GltC in response to the availability of sugars (PubMed:17183217, PubMed:15150224).
Enzyme activity is low in early exponential phase and reached higher levels in the middle and late stages of exponential growth (at protein level). Repressed by glucose; induced by arginine, ornithine, or to a lesser extent proline (in the absence of glucose). Not induced by glutamate or glutamine (PubMed:9829940). Expression depends on the alternative sigma-L factor and the transcription factor RocR (PubMed:10468601). Subject to direct CcpA-dependent glucose repression (PubMed:15150224).
Homohexamer (PubMed:16244435, PubMed:20630473). Interacts with transcriptional regulator GltC (PubMed:17608797).
Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Belongs to the type II topoisomerase GyrB family.
Belongs to the proline dehydrogenase family.
Converts proline to delta-1-pyrroline-5-carboxylate. Important for the use of proline as a sole carbon and energy source or a sole nitrogen source.
Could catalyze the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to an acceptor substrate and release both CoA and the acetylated product.
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Homooctamer. Component of a possible RNA degradosome complex composed of rny, rnjA, rnjB, pnp, pfkA and eno (PubMed:19193632) (although rnjA and rnjB's presence is unclear).
The covalent binding to the substrate at Lys-339 of a small fraction of enolase causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein (PubMed:15003462). Citrate acts as a non-competitive inhibitor for both forward and reverse reactions, probably by chelating Mg(2+) (PubMed:22198292).
The covalent binding to the substrate causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein.
Expressed at the early stages of sporulation.
Required for the formation of axial filaments and for anchoring the origin regions at the cell poles in sporulating cells, thus ensuring proper chromosome segregation in the prespore. Binds in a dispersed manner throughout the chromosome but preferentially to sites clustered in the origin portion of the chromosome, causing condensation of the chromosome and its remodeling into an elongated, anchored structure.
Belongs to the ABC transporter superfamily. ABCF family. ARE2 subfamily.
Binds within the E-site of the 70S ribosome, where it contacts ribosomal proteins L1, L5, L33-1, S7, S11, the 16 and 23S rRNAs and the acceptor arm of the P-site tRNA.
Binds within the E-site of the 70S ribosome, where it contacts ribosomal proteins of the large and small subunit, the 16 and 23S rRNAs and the acceptor arm of the P-site tRNA.
Expressed during all growth phases; expression is higher during early log phase and decreases as growth continues. Expression is dramatically increased in the presence of antibiotics virginiamycin M and lincomycin. A monocistronic operon.
Hypersensitivity toward the antibiotics virginiamycin M and lincomycin, mildly increased sensitivity to erythromycin, clindamycin and oleandomycin (PubMed:16109936). Hypersensitivity toward the antibiotics virginiamycin M, lincomycin and tiamulin, in this study has no effect on sensitivity to erythromycin, chloramphenicol or linezolid (PubMed:30126986).
Recognizes and binds in the vacant E-site of ribosomes stalled by some peptidyltransferase center (PTC)-targeting antibiotics. Makes contact with the PTC and both ribosomal subunits. Induces conformational changes in the P-site, which allows it to dislodge the antibiotic from its PTC binding site.
Recognizes and binds in the vacant E-site of ribosomes stalled by some peptidyltransferase center (PTC)-targeting antibiotics. Makes contact with the PTC and both ribosomal subunits. Induces conformational changes in the P-site, which allows it to dislodge the antibiotic from its PTC binding site. Binds to ribosomes either directly following translation initation or subsequent to E tRNA release during elongation (PubMed:30126986). Involved in resistance to a narrow spectrum of antibiotics (the streptogramin A antibiotic virginiamycin M, the lincosamide antibiotic lincomycin and the pleuromutilin antibiotic tiamulin) (PubMed:16109936, PubMed:30126986).
The antibiotic resistance domain (ARD) is packed between the 23S rRNA and the acceptor arm of the P-site tRNA and inserts into the peptidyltransferase center (PTC). The C-terminal extension (CTE) contacts the small ribosomal subunit, positioned in the Shine-Dalgarno-anti-Shine-Dalgarno cavity.
Converts oxalate to formate and CO(2) in an O(2)-dependent reaction. Can also catalyze minor side reactions: oxalate oxidation to produce H(2)O(2), and oxalate-dependent, H(2)O(2)-independent dye oxidations.
Induced by acid pH but not by oxalate (PubMed:10960116). Positively regulated by SigO and its coactivator RsoA (PubMed:18573182).
Activity of this protein is best tested in a clpP or ssrA deletion mutant; ssrA (tmRNA) encodes the SsrA tag added to nascent proteins in stalled ribosomes by trans-translation, which targets the nascent protein for degradation.
Associates with stalled 50S ribosomal subunits.
Highly expressed during stationary phase.
Not essential in rich media; synthetic growth defects are seen in double rqcH ssrA mutants, further exacerbated by translational inhibitors spectinomycin and erythromycin or at elevated temperatures. Decreased accumulation of a stalled reporter protein. Triple rqcH clpP ssrA mutants cannot be generated.
Part of the ribosome quality control system (RQC). Recruits Ala-charged tRNA and directs the elongation of stalled nascent chains on 50S ribosomal subunits, leading to non-templated C-terminal Ala extensions (Ala tail). The Ala tail promotes nascent chain degradation. May add between 1 and at least 8 Ala residues. Binds to stalled 50S ribosomal subunits.
Part of the ribosome quality control system (RQC). Recruits Ala-charged tRNA and directs the elongation of stalled nascent chains on 50S ribosomal subunits, leading to non-templated C-terminal Ala extensions (Ala tail). The Ala tail promotes nascent chain degradation. Selectively binds tRNA(Ala)(UGC), which is presumably the sole source of tRNA(Ala) used for Ala tailing directed by this protein. May add between 1 and at least 8 Ala residues; detection of the Ala tail requires either deletion of clpP or its inhibition. Binds to 50S ribosomal subunits, at least 30% of which contain a P-site tRNA and thus are obstructed.
Up-regulated under secretion stress conditions, possibly in a CssR/CssS-dependent manner.
Belongs to the metallo-dependent hydrolases superfamily. NagA family.
Involved in the first committed step in the biosynthesis of amino-sugar-nucleotides. Catalyzes the hydrolysis of the N-acetyl group of N-acetylglucosamine-6-phosphate (GlcNAc-6-P) to yield glucosamine 6-phosphate and acetate.
Heterotetramer of two alpha and two beta chains. Directly associated with ODBA in the E1 complex.
Appears to be allosterically activated by the binding of pArg-containing polypeptides to the pArg-binding pocket localized in the C-terminal domain of McsB (By similarity). The McsB kinase is inhibited in nonstressed cells by direct interaction with ClpC; upon heat exposure, the interaction of McsB with ClpC is dramatically decreased, leading to McsB release and activation during heat stress. Its kinase activity is counteracted by the protein-arginine-phosphatase YwlE in vivo. Requires McsA for full kinase activity.
Appears to be allosterically activated by the binding of pArg-containing polypeptides to the pArg-binding pocket localized in the C-terminal domain of McsB.
Autophosphorylated on Arg residues. Phosphorylation on Arg-40 and Arg-86 are up-regulated upon stress conditions.
Belongs to the ATP:guanido phosphotransferase family.
Catalyzes the specific phosphorylation of arginine residues in a large number of proteins. Is part of the bacterial stress response system, where it is involved in regulating the global heat shock repressor CtsR; phosphorylates arginine residues in the winged helix-turn-helix domain of CtsR, thereby preventing its binding to DNA and consequently inducing the expression of repressed genes. The transcriptional repressor HrcA, the chaperone GroEL, the unfoldase ClpC, together with several ribosomal subunits, represent other physiological targets of McsB under stress conditions. Protein arginine phosphorylation has a physiologically important role and is involved in the regulation of many critical cellular processes, such as protein homeostasis, motility, competence, and stringent and stress responses, by regulating gene expression and protein activity. Functions as an adapter whose kinase activity is required for ClpCP-mediated degradation of CtsR during heat stress. Is required for the delocalization of competence proteins from the cell poles, probably via a role in the degradation of anchor proteins.
Catalyzes the specific phosphorylation of arginine residues in a large number of proteins. Is part of the bacterial stress response system. Protein arginine phosphorylation has a physiologically important role and is involved in the regulation of many critical cellular processes, such as protein homeostasis, motility, competence, and stringent and stress responses, by regulating gene expression and protein activity.
Cells lacking this gene show a defect in the delocalization of competence proteins that is not related to altered expression of the com genes on the levels of either transcription or translation. Inactivation of mcsB also decreases transformability (PubMed:19226326). CtsR is no more degraded (PubMed:30962626).
Interacts with CtsR in its autophosphorylated form. Interacts with McsA in nonstressed as well as in heat-stressed cells, whereas strongly interacts with ClpC only in nonstressed cells.
Is repressed by the transcriptional regulator CtsR. Forms part of an operon with ctsR, mcsA and clpC.
Activity is improved in the presence of Mn(2+), Mg(2+) and Ca(2+), and inhibited by Ni(2+), Zn(2+) and Cu(2+).
Adopts the classical GT-B fold containing the N-terminal and C-terminal domains that accommodate the sugar acceptor and UDP-glucose, respectively (PubMed:33310191, PubMed:33152360). The spacious sugar-acceptor binding pocket might be responsible for the broad substrate spectrum (PubMed:33310191).
Glycosyltransferase that can glycosylate a wide range of substrates, including various flavonoids, phenyl ketones, curcuminoid, lignins, zingerone, triterpenes, stilbene and anthraquinone, using UDP-glucose or ADP-glucose as sugar donor (PubMed:28315700, PubMed:33152360). It also exhibits O-, N- and S-glycosylation activities towards simple aromatics (PubMed:28315700). In vivo, the broad acceptor tolerance of YjiC might function as a detoxification agent against exogenous xenobiotics to make the strain adaptable to the changeable environment (Probable).
Controls the length of the flagellar hook.
Belongs to the ferredoxin--NADP reductase type 2 family.
Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme (By similarity).
Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA (By similarity). Has a role in growth and sporulation on acetate.
Disruption of this gene induces a loss of the ability to utilize acetate as a carbon source for growth or sporulation.
Cells lacking this gene show a lack of cardiolipin.
Involved in the biosynthesis of cardiolipin.
Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another.
An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism (By similarity). Binds both GDP and GTP. Complements an E.coli era disruption mutant.
An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Era GTPase family.
Constitutively expressed, two-fold induced at the end of the exponential phase; this is under control of Spo0A, suggesting it may have a role in sporulation.
Essential in some but not all strains; in 168 / BR151 the null mutation grows slowly and forms irregularly shaped colonies after several days. In liquid culture forms chains of elongated cells with diffuse nucleoids that occupy most of the cell. Sporulation in this disruption strain is severely impaired. Essential in strains CRK6000 and IS75, where it cannot be disrupted. In CRK600 in depletion experiments cells become 1.5 to 2-fold longer and nucleoid distribution is dispersed. The number of replication origins increases, suggesting an increase in chromosome replication.
Estimated to be present at 3000 copies per cell.
Was originally thought to be the spo0F protein.
In the C-terminal section; belongs to the PhoH family.
Belongs to the PNP/MTAP phosphorylase family.
The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.
The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. Cleaves guanosine, inosine, 2'-deoxyguanosine and 2'-deoxyinosine.
Constitutively expressed during exponential growth. Encoded in an operon with ydiO and in a second with groES, groEL, ydiM and ydiN. This second operon is heat-inducible.
An unidentified mutation in this gene gives rise to thiostrepton resistance.
Belongs to the universal ribosomal protein uL11 family.
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
One or more lysine residues are methylated.
Part of the ribosomal stalk of the 50S ribosomal subunit. Interacts with L10 and the large rRNA to form the base of the stalk. L10 forms an elongated spine to which 2 L12 dimers bind in a sequential fashion forming a pentameric L10(L12)2(L12)2 complex.
Part of the ribosomal stalk of the 50S ribosomal subunit. Interacts with L10 and the large rRNA to form the base of the stalk. L10 forms an elongated spine to which L12 dimers bind in a sequential fashion forming a multimeric L10(L12)X complex.
Forms a complex with BofA and SpoIVFB localized in the mother-cell membrane surrounding the forespore.
Implicated in the coupling of mother cell to forespore gene expression. Required for spore formation at 37 degrees Celsius, but not at 30 degrees Celsius. SpoIVFA plays a central role in both maintaining the SpoIVFA/BofA/SpoIVFB complex and anchoring it to the outer forespore membrane. SpoIVFA brings BofA into close proximity to SpoIVFB, allowing BofA to inhibit SpoIVFB. Increased accumulation of SpoIVFA seems to inhibit the activity of SpoIVFB and thus regulates the activation of sigma-K.
May be degraded by FtsH. It is stabilized by an ftsH disruption mutant, and in a probably independent fashion, by overexpression of BofA.
Transcriptionally regulated by the forespore-specific sigma factor, SigG, and the general stress response regulator, SigB.
Expressed only in the forespore compartment of sporulating cells. Expression is sigma F and sigma G-dependent.
Couples proton uptake and Na(+) efflux to the substrate-product malate/lactate antiport, in an electroneutral malate-2H(+)/Na(+)-lactate exchange. Plays a role in supporting growth to high density on malate at reduced protonmotive force.
Can suppress growth and secretion defects in E.coli secA and secB mutants (PubMed:1435734). Probably a molecular chaperone for exported proteins or may act by stabilizing the SecA protein (PubMed:1435734, PubMed:10816431).
Grows normally, reduced secretion of SdpC (formerly YvaY) and another 36 kDa protein.
Homodimer (PubMed:17372352). Probably binds SecA and prePhoB (PubMed:10816431). Probably interacts with proSdpC (PubMed:13129613).
Present in exponentially growing cells (at protein level).
Relieves catabolite repression of gapB and pckA transcription. Disruption is epistatic over a yqfL deletion.
Transcription repressor that binds to the promoter of gapB and pckA genes, preventing their expression. Acts as a regulator for catabolite repression of gluconeogenic genes.
Oxidizes hypoxanthine and xanthine to uric acid. PucA subunit could exert a molybdenum cofactor recruiting function.
Main asparagine synthetase in vegetative cells.
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Belongs to the arginase family. Agmatinase subfamily.
Catalyzes the formation of putrescine from agmatine.
Cells lacking this gene have a greatly increased sensitivity to DNA damaging agents, 25-fold decreased plasmid transformation and only slightly reduced chromosomal DNA transformation (PubMed:10692371). They form anucleate cells 100-times more frequently than wild-type cells during normal growth (PubMed:18684995). DNA damaging agent sensitivity is partially suppressed by disruption of radA and fin (also called sms and subA respectively) (PubMed:11810266).
Endonuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves mobile four-strand junctions by introducing symmetrical nicks in paired strands. Promotes annealing of linear ssDNA with homologous dsDNA. Required for DNA repair, homologous recombination and chromosome segregation.
Has at least 2 separable functions; Holliday junction resolution with generation of monomeric chromosomes, and modulation of RecA activity. Endonuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves mobile four-strand junctions by introducing symmetrical nicks in paired strands. Promotes annealing of linear ssDNA with homologous dsDNA. Required for DNA repair, homologous recombination and chromosome segregation. Partially inhibits the hydrolysis of dATP or rATP by RecA. Holliday junction resolution is stimulated by RuvB.
Recombination protein U, a short form proposed to initiate from Met-33, which is equivalent to RecU-delta1-32, is not detected in vivo, and would not be functional. The name is misleading and should no longer be used.
Was originally named prfA (Penicillin-binding protein-related factor A, PBP-related factor A) due to its proximity to the ponA gene; this name is misleading and should no longer be used.
Belongs to the bacterial ribosomal protein bL20 family.
Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit (By similarity).
Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit.
Belongs to the galactose-1-phosphate uridylyltransferase type 2 family.
Member of the two-component regulatory system DctS/DctR. Essential for expression of dctP.
Up-regulated in response to depletion of tryptophan, phenylalanine, tyrosine, or availability of charged tRNATrp.
Binding to DNA is inhibited by L-arabinose.
Transcriptional repressor of the arabinose utilization genes. Also regulates its own expression. Binds to two sequences within the promoters of the araABDLMNPQ-abfA operon and the araE gene, and to one sequence in the araR promoter.
Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol (By similarity). May have a role in the heat shock response since the level of the transcript of ywiE increases after a heat shock.
Belongs to the PNP/UDP phosphorylase family. MtnN subfamily.
Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively (PubMed:10574451). Also cleaves 5'-deoxyadenosine, a toxic by-product of radical S-adenosylmethionine (SAM) enzymes, into 5-deoxyribose and adenine (By similarity).
Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. Also cleaves 5'-deoxyadenosine, a toxic by-product of radical S-adenosylmethionine (SAM) enzymes, into 5-deoxyribose and adenine.
Binds 1 Ca(2+) ion per subunit. Can also use Co(2+) or Mn(2+).
Catalyzes the hydrolysis of supercoiled double and single strand DNA and RNA. Involved in chromosomal DNA degradation and cell death caused by thermal stress.
Cells lacking this gene are more sensitive to mitomycin C, show an increased ability of competence and are not able to metabolize extracellular DNA.
Inhibited by aurintricalboxylic acid but not by Zn(2+), Mn(2+), Hg(2+), 2-mercaptoethanol and sodium citrate. Neither inhibited nor activated by ATP.
Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes.
Belongs to the HAD-like hydrolase superfamily. YjjG family.
Belongs to the anthranilate phosphoribosyltransferase family.
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Probably part of the ABC transporter complex YxeMNO that could be involved in amino-acid import. May transport S-methylcysteine.
Couples transcription and DNA repair by recognizing RNA polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent release of RNAP and its truncated transcript from the DNA, and recruitment of nucleotide excision repair machinery to the damaged site.
In the C-terminal section; belongs to the helicase family. RecG subfamily.
In the N-terminal section; belongs to the UvrB family.
Belongs to the antibiotic N-acetyltransferase family.
May contribute to antibiotic resistance.
Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.
Positively regulated by the two-component system YycFG. Expression is maximal during exponential growth.
Forms a complex with cognate toxin YopC.
May be the antitoxin component of a type II toxin-antitoxin (TA) system. Neutralizes the activity of cognate toxin YopC.
Homodimer under conditions of nitrogen excess (PubMed:1677938, PubMed:18331450, PubMed:25691471). Monomer under conditions of nitrogen-limited (PubMed:25691471). Interacts with feedback-inhibited GlnA in order to stabilizes GlnR-DNA complex (PubMed:1677938, PubMed:18331450, PubMed:25691471).
In vivo, this mutant constitutively represses glnR expression. In vitro, this mutant binds DNA more tightly than wild-type and this binding is not activated by feedback-inhibited GlnA.
Transcription repressor that represses many genes including ureABC and tnrA, during nitrogen excess (PubMed:2573733, PubMed:1677938, PubMed:10231480, PubMed:18331450). On the contrary of the MerR members, which require longer DNA sites for high-affinity binding, GlnR requires a DNA sequence of 17 nucleotides as minimal binding site (PubMed:10231480, PubMed:25691471).
Under conditions of nitrogen excess, the DNA binding activity of GlnR is activated by a transient interaction with feedback-inhibited GlnA (PubMed:18331450). Under conditions of nitrogen-limited, GlnR is autoinhibited by its C-terminal region (PubMed:25691471).
Under conditions of nitrogen-limited growth, repressed by TnrA.
Controls the rotational direction of flagella during chemotaxis.
Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin.
Inhibits DNA replication in growing cells, thus reducing chromosome copy number and playing a significant role during the onset of sporulation.
Belongs to the BPG-independent phosphoglycerate mutase family.
Essential for rapid growth and for sporulation. Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Inhibited during sporulation by acidification of the forespore, thus allowing accumulation of the spore's large depot of 3-phosphoglyceric acid.
Catalyzes two steps in the degradation of uric acid, i.e. the oxidation of uric acid to 5-hydroxyisourate (HIU) and the stereoselective decarboxylation of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) to (S)-allantoin.
Expression is very low in excess nitrogen (glutamate plus ammonia) and is induced by TnrA during imiting-nitrogen conditions (glutamate). Expression is further induced when allantoin or uric acid are added during limiting-nitrogen conditions.
HIU and OHCU are unstable, they spontaneously decompose to form a racemic mixture of allantoin.
In the C-terminal section; belongs to the uricase family.
In the N-terminal section; belongs to the OHCU decarboxylase family.
Belongs to the universal ribosomal protein uS9 family.
Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'-phosphopantotheine.
Catalyzes two steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine, in the latter compound is decarboxylated to form 4'-phosphopantotheine.
In the C-terminal section; belongs to the PPC synthetase family.
In the N-terminal section; belongs to the HFCD (homo-oligomeric flavin containing Cys decarboxylase) superfamily.
Regulates the expression of the alsSD operon for acetoin biosynthesis.
May play some important role in either sporulation or the dormant spore.
Binds 1 iron-chlorin (heme d or cytochrome d) per heterodimer, in conjunction with CydB.
Binds 1 protoheme IX center (heme b558) per subunit.
Binds 1 protoheme IX center (heme b595) per heterodimer, in conjunction with CydB.
Catalysis proceeds by a classical ping-pong bi-bi reaction mechanism. The reduction of nitro-organic compounds and inorganic chromate occur in the absence of external FMN and are therefore believed to require binding of these substrates in the active site. In contrast to these reduction processes, azo dyes are reduced only in the presence of external FMN, indicating that azo dye reduction occurs outside the active site of the enzyme.
FMN is a competitive inhibitor of NADH, and therefore leads to the preferential utilization of NADPH.
Reduces FMNH(2) to FMN, with NADH or NADPH as reductant. It also reduces nitroaromatic compounds, quinones, chromates and azo dyes. It could supply the reduced form of FMN to luciferase-like protein and contribute to the degradation of aromatic compounds.
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in fructose transport.
Belongs to the LysE/ArgO transporter (TC 2.A.75) family.
Induced by salt addition via sigma-B dependent promoter.
One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation.
Histone-like DNA-binding protein which is capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions.
An unknown mutation in this protein gives rise to thiostrepton resistance.
Is involved in the adaptive response to alkylation damage in DNA caused by alkylating agents. Repairs the methylphosphotriester lesions in DNA by a direct and irreversible transfer of the methyl group to one of its own cysteine residues.
The methylation of AdaA by methylphosphotriesters in DNA leads to its activation as a transcriptional regulator that activates the transcription of the ada operon which consists of adaA and adaB, and of the adjacent gene alkA.
Up-regulated by methylated AdaA itself in response to the exposure to alkylating agents such as MNNG.
Antiterminator that binds to cis-acting regulatory sequences on the mRNA in the presence of histidine, thereby suppressing transcription termination and activating the hut operon for histidine utilization.
IF-3 binds to the 30S ribosomal subunit and shifts the equilibrum between 70S ribosomes and their 50S and 30S subunits in favor of the free subunits, thus enhancing the availability of 30S subunits on which protein synthesis initiation begins.
Acts as an antagonist to SinR. SinI prevents SinR from binding to its target sequence on the gene for AprE.
Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19) family.
Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19) family. Cation/proton exchanger (CAX) subfamily.
Ca(+)/H(+) antiporter that extrudes calcium in exchange for external protons.
Ca(+)/H(+) antiporter that extrudes calcium in exchange for external protons. Does not transport sodium or potassium.
Calcium efflux is tightly regulated by intracellular pH.
Glycerophosphodiester phosphodiesterase hydrolyzes glycerophosphodiesters into glycerol-3-phosphate (G3P) and the corresponding alcohol.
Catalyzes the reversible NADPH-dependent reduction of scyllo-inosose (SIS) to scyllo-inositol (SI). Cannot use NADH instead of NADPH. May be involved in reduction of not only SIS but also various oxidized compounds manifested upon stressful conditions.
Cells lacking this gene show normal growth on SI as well as on glucose or myo-inositol (MI) as the sole carbon source.
Is constitutively expressed, even in the absence of both myo-inositol and scillo-inositol (PubMed:20133360). Is up-regulated under certain stressful conditions (PubMed:22383849).
May be important for peptidoglycan remodeling.
A probable RNA chaperone. Forms a complex with KhpB which binds to cellular RNA and controls its expression. Plays a role in peptidoglycan (PG) homeostasis and cell length regulation.
Belongs to the KhpA RNA-binding protein family.
Involved in a cysteine salvage pathway from S-alkylcysteine. Catalyzes the oxidation of N-acetyl-S-benzyl-L-cysteine and N-acetyl-S-methyl-L-cysteine to (R)-N-acetyl-S-benzyl-L-cysteine sulfoxide and (R)-N-acetyl-S-methyl-L-cysteine sulfoxide, respectively. This pathway is likely important in the catabolism of alkylated cysteine generated by proteolysis of alkylated glutathione formed in the detoxification of a wide range of electrophiles.
Homodimer, probably forms a complex with cognate toxin YutE.
Probable antitoxin component of a putative type VII toxin-antitoxin (TA) system. Probably neutralizes cognate toxin YutE.
Associated with cell lysis upon induction of PbsX.
Belongs to the aconitase/IPM isomerase family. LeuC type 1 subfamily.
In the C-terminal section; belongs to the bacterial solute-binding protein 5 family.
Expression requires the sigma-E factor SigE.
Probable member of the two-component regulatory system YxjM/YxjL. May activate YxjL by phosphorylation.
Belongs to the glucose-6-phosphate dehydrogenase family.
Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone.
Cells partially restore cytochrome c oxidase activity in a CcdA-deficient mutant, possibly because the bacteria can no longer oxidize the two heme-binding thiol groups in apocytochrome c.
Required for the stabilization, possibly via formation of a disulfide bond, of the obligatory competence protein ComGC. Not normally required for production of the secreted lantibiotic sublancin 168, although it can partially substitute for BdbB when the latter is absent. It may also be required for the stability of other secreted proteins. Not required for sporulation.
Belongs to the mannitol dehydrogenase family.
The IMP cyclohydrolase activity resides in the N-terminal region.
By the antimicrobial streptomycin, produced by the Gram-positive bacterium S.griseus.
Probable hydrolase that is able to inhibit the signaling pathway required for the streptomycin production and development of aerial mycelium in S.griseus. Thus, serves as a defensive strategy against competing bacteria. The putative target for YtnP may be a gamma-butyrolactone termed A factor, which is the quorum-sensing signaling molecule that positively regulates streptomycin production and development of aerial hyphae in S.griseus.
This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
Belongs to the pseudomonas-type ThrB family.
Knockout mutant is susceptible to amicoumacin A.
Phosphorylates the antibiotic amicoumacin A (Ami), leading to its inactivation. Mediates natural B.subtilis resistance to the drug.
Involved in protein export. Participates in an early event of protein translocation (By similarity).
Involved in protein export. Participates in an early event of protein translocation.
Catalyzes the oxidation of dihydrolipoamide to lipoamide.
Homodimer. Component of two multienzyme complexes: pyruvate dehydrogenase complex and oxoglutarate dehydrogenase complex.
Belongs to the arylamine N-acetyltransferase family.
Transcribed at a constant level in all growth phases. Part of the mraZ-rsmH-ftsL-pbpB operon.
Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+).
Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.
To M.jannaschii MJ0043 N-terminal region.
Because it hydrolyzes 6-phospho-alpha-glucopyranosides without activated leaving groups (such as maltose-6'-phosphate) but not glycosidic linkage of naturally occurring phospho-beta-glucosides such as cellobiose-6'-phosphate nor methyl 6-phospho-beta-D-glucopyranoside, GlvA is certainly more appropriately classified as a 6-phospho-alpha-glucosidase than as a 6-phospho-beta-glucosidase. The ability to hydrolyze beta-glycosidic linkages is exceptional and applies only to activated 6-phospho-beta-D-glucopyranosides.
Binds 1 NAD(+) per subunit. Is only active with NAD(+), not NADH.
Binds 1 divalent metal cation per subunit. Manganese, iron, cobalt or nickel enhance activity.
Cellobiose-6'-phosphate and 6-phospho-beta-D-glucopyranoside are not substrates but competitive inhibitors of GlvA.
Hydrolyzes maltose-6'-phosphate and trehalose-6'-phosphate. Is involved in the catabolism of alpha-glycosides accumulated via a phosphoenolpyruvate-dependent maltose phosphotransferase system (PEP-PTS). Is also able to significantly catalyze the hydrolysis of both 6-phospho-alpha- and 6-phospho-beta-glucosides containing activated leaving groups such as p-nitrophenol and does so with retention and inversion, respectively, of the substrate anomeric configuration.
Reaction proceeds via a redox-elimination-addition mechanism consistent with an E1cb-type mechanism. This includes redox steps involving NAD(+) and stabilization of intermediates by Mn(2+).
Belongs to the glycosyl hydrolase 30 family.
Catalyzes the depolymerization of methylglucuronoxylan (MeGAXn) from different sources. It cleaves the beta-1,4-xylosidic bond penultimate to that linking carbon one of the xylose residue substituted with alpha-1,2-linked 4-O-methyl-D-glucuronate (MeGA).
Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to CheB, CheY or CheV.
Belongs to the aconitase/IPM isomerase family.
By citrate via CcpC. When citrate is absent, CcpC binds to the sites near the citB promoter and blocks expression. When citrate is present, it causes a change in the interaction of CcpC with its binding sites, resulting in derepression of citB. When citrate is very abundant, CcpC activates citB expression, presumably reflecting a change in the interaction of CcpC with RNA polymerase. Also induced by decoyinine and nutrient depletion.
Catalyzes the isomerization of citrate to isocitrate via cis-aconitate.
Cells lacking this gene show a dramatic increase in the concentration of citrate. This accumulation of citrate prevents sporulation due to chelation by citrate of divalent cations required for proper functioning of the Spo0A-initiated phosphorelay.
Involved in both the tricarboxylic acid (TCA) and methylcitric acid cycles (PubMed:28956599). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate (PubMed:3110133, PubMed:23354745). Also catalyzes the rehydration of 2-methyl-cis-aconitate to produce 2-methylisocitrate (PubMed:28956599). The apo form of AcnA functions as a RNA-binding regulatory protein which plays a role in the regulation of citrate concentration and in the sporulation. To prevent the accumulation of excessive levels of citrate, it binds near the 5' end of the citZ mRNA, decreasing its stability and thereby limiting the concentration of citrate synthase in the cell. Aconitase also binds to the gerE transcript late in sporulation and stabilizes it for translation, thereby increasing the rate and level of GerE protein accumulation (PubMed:10468622, PubMed:16923907, PubMed:23354745, PubMed:9393699).
Mutagenesis of different positions (F662L, R741F, Q745E, I810T and V853A) on the C-terminal region of citB gene product shows that even B.subtilis mutant has high aconitase catalytic activity, it is defective in sporulation. The defect is at a late stage of sporulation, specifically affecting expression of sigma-K-dependent genes, many of which are important for spore coat assembly and require transcriptional activation by GerE. It strongly suggests that aconitase RNA binding activity may stabilize gerE mRNA in order to allow efficient GerE synthesis and proper timing of spore coat assembly.
Whether aconitase is active as an enzyme or an RNA-binding protein is determined by the status of an iron-sulfur (4Fe-4S) cluster that is essential for the catalytic activity of all aconitases. Citrate is both cotransported with iron and a chelator of divalent cations, including iron. If the intracellular citrate level becomes excessive, iron will be sequestered away from iron-containing proteins, including aconitase. Since excess citrate greatly stimulates aconitase synthesis via the positive regulatory effect of CcpC, the cell will gain the ability to metabolize citrate at a higher rate. If so much iron has been sequestered that aconitase loses enzymatic activity, the cell will acquire a high concentration of enzymatically inactive but RNA-binding-competent aconitase molecules. These aconitase proteins can bind to the citZ mRNA and reduce the rate of citrate accumulation by restricting the synthesis of citrate synthase protein.
Deletion of the gene affects the levels of over 800 mRNAs (PubMed:24163345). Deletion mutant overexpresses flagellin and other genes of the sigma-D-dependent motility regulon. In contrast, the two major operons for biofilm formation are not expressed and the mutant is unable to form biofilms. All cells are short and motile (PubMed:21856853). Deletion also results in a significant decrease in intercellular molecular exchange (PubMed:26906740). Mutant displays aberrant developmental patterns and forms smaller colonies (PubMed:26904951).
Plays a central, regulatory role in the late adaptive responses and affects the levels of many genes (PubMed:24163345). May act via regulation of cAMP levels (PubMed:26904951). Decreases the expression of motility genes and induces genes involved in biofilm formation, by controlling the expression of SlrR (PubMed:21856853). Required for formation of intercellular nanotubes that bridge neighboring cells to allow molecular exchange (PubMed:26906740). Plays a key role in directing the early stages of colony development (PubMed:26904951). In vitro, has a metal-dependent phosphodiesterase activity against 2',3'-cAMP and 2',3'-cGMP. Has also 3',5'-cyclic-nucleotide phosphodiesterase activity, but cannot use cyclic di-AMP or cyclic di-GMP, and does not have phosphatase activity (PubMed:24163345).
Involved in the assembly of several proteins in the inner and outer layer of the spore coat.
Was originally (Ref.1) thought to be two genes, ydcI and ydcJ.
Plays a role in carbon catabolite repression (CCR). Specifically required for transcriptional repression of the levanase operon by glucose but not by other sugars.
Belongs to the AB hydrolase superfamily. AB hydrolase 2 family.
Putative hydrolase that may contribute to the degradation of aromatic compounds.
Converts proline to delta-1-pyrroline-5-carboxylate.
Cleaves the N-terminal amino acid of tripeptides.
Necessary to maintain spores after the late stage of sporulation. Might be involved in cortex formation.
Member of the two-component regulatory system YvfT/YvfU. Probably activates YvfU by phosphorylation.
Belongs to the universal ribosomal protein uL24 family.
Has also been isolated as a basic, heat-shock stable DNA-binding protein from the B.subtilis nucleoid. It binds cooperatively to double-stranded supercoiled DNA which it further compacts into complexes 15-17 nm in diameter. Overexpression of the protein disrupts nucleoid segregation and positioning.
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
Belongs to the methyltransferase superfamily. MnmM family.
Involved in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA (PubMed:36762482). Catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34 to form mnm(5)s(2)U34 (PubMed:36762482).
Mutant accumulates nm(5)s(2)U34 and cannot form mnm(5)s(2)U34.
Cells lacking this gene are moderately sensitive to DNA-damaging agents. Sensitivity increases in the presence of mutated AddAB nuclease.
Probable DNA helicase. Required for DNA repair and intramolecular recombination; probably has overlapping function with RecS (AC P50729). It probably acts to help generate ss-DNA from ds-DNA breaks.
Catalyzes the attachment of tryptophan to tRNA(Trp).
General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr then transfers it to the PTS EIIA domain.
P-Ser-HPr interacts with the catabolite control protein A (CcpA), forming a complex that binds to DNA at the catabolite response elements cre, operator sites preceding a large number of catabolite-regulated genes. Thus, P-Ser-HPr is a corepressor in carbon catabolite repression (CCR), a mechanism that allows bacteria to coordinate and optimize the utilization of available carbon sources. P-Ser-HPr also plays a role in inducer exclusion, in which it probably interacts with several non-PTS permeases and inhibits their transport activity.
Phosphorylation on Ser-46 inhibits the phosphoryl transfer from enzyme I to HPr.
Belongs to the NAD(P)-dependent epimerase/dehydratase family. dTDP-glucose dehydratase subfamily.
Catalyzes the dehydration of dTDP-D-glucose to form dTDP-6-deoxy-D-xylo-4-hexulose via a three-step process involving oxidation, dehydration and reduction.
Acts as repressor of the lincomycin-resistance (lmrAB) and yxaGH operons.
Homodimer. In stressed cells, forms a complex with RsbV. The predominant form of this complex has a stoichiometry of 2:2 (one dimer of RsbW is bound by two monomers of RsbV). In unstressed cells, forms a 2:1 complex with sigma-B.
Negative regulator of sigma-B activity. Phosphorylates and inactivates its specific antagonist protein, RsbV. Upon phosphorylation of RsbV, RsbW is released and binds to sigma-B, thereby blocking its ability to form an RNA polymerase holoenzyme (E-sigma-B).
The higher affinity of RsbW for RsbV than for sigma-B, rather than a difference in the concentrations of RsbV and sigma-B, is the driving force that is responsible for the switch of RsbW to non-phosphorylated RsbV. The kinase activity of RsbW is directly regulated by changes in the ATP/ADP ratio.
Belongs to the urease gamma subunit family.
Expression is sigma F and sigma G-dependent.
Seems to improve the efficiency of sporulation by fine-tuning the expression of genes in the sigma F regulon, particularly the timing of their expression. Negatively regulates spoIIR and its own synthesis.
Belongs to the glycosyl hydrolase 53 family.
Involved in galactan degradation (PubMed:17056685, PubMed:27501980). Degrades arabinose-free galactan to galactooligosaccharides, producing galactotetraose as the main product along with galactotriose, galactobiose, and galactose (PubMed:27501980). Is also able to degrade galactotetraose, galactotriose and galactobiose, suggesting an additional exo-mode of activity (PubMed:27501980). May hydrolyze the beta-1,4-galactan linkages of the galactan portion of arabinogalactan type I, a pectic plant polysaccharide from which most of the arabinose has been removed (Probable).
A number of substitutions and deletions can promote streptomycin resistance, dependence or pseudodependence; all but one of these (K55R) are associated with hyperaccurate translation.
Belongs to the universal ribosomal protein uS12 family.
Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit (By similarity).
Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.
Many streptomycin resistant B.subtilis with mutations in this protein produce increased quantities of a natural (but uncharacterized) antibiotic.
Part of the 30S ribosomal subunit (PubMed:30126986). Contacts proteins S8 and S17. May interact with IF1 in the 30S initiation complex (By similarity). Interacts with BrxC (PubMed:33722570).
Part of the 30S ribosomal subunit. Contacts proteins S8 and S17. May interact with IF1 in the 30S initiation complex.
The enzyme that would modify Asp-102 to 3-methylthioaspartic acid has not been found in the proteome of this organism, and that modification does not occur.
With S4 and S5 plays an important role in translational accuracy.
Catalyzes the conversion of UDP-2,4,6-trideoxy-2-acetamido-4-amino glucose to UDP-2,4,6-trideoxy-2,4-diacetamido glucose, commonly known as UDP-N,N'-diacetylbacillosamine (UDP-diNAcBac).
Insertion mutant shows decreased efficiency of biofilm formation. Disruption affects swarming motility.
Belongs to the GcvP family. C-terminal subunit subfamily.
Belongs to the glycosyl hydrolase 13 family. GlgB subfamily.
Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
Involved in the maturation of iron-sulfur (Fe-S) proteins. May function as a Fe-S cluster carrier.
Belongs to the bacterial ribosomal protein bL31 family. Type B subfamily.
Only found in ribosomes after the end of exponential growth. In PubMed:12904577 its expression was predicted to be repressed by the zinc-specific metallo-regulatory protein zur; in PubMed:15049826 it was shown that its expression is indeed repressed by zur.
Part of the 50S ribosomal subunit after the end of exponential growth.
While neither of the L31 paralogs is essential, this protein does not seem to function as the main L31 protein. Has a higher affinity for 70S ribosomes than the zinc-containing L31 paralog; is able to displace it to varying extents, even under zinc-replete conditions.
Involved in the resistance to tunicamycin. Binds ATP.
Belongs to the transcriptional regulatory Rex family.
Modulates transcription in response to changes in cellular NADH/NAD(+) redox state.
Expressed at the end of the exponential growth phase.
Belongs to the chaperonin (HSP60) family.
Forms a cylinder of 14 subunits composed of two heptameric rings stacked back-to-back. Interacts with the co-chaperonin GroES.
Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
Partially reduces sensitivity to the toxic niacin analog 6-amino-nicotinamide.
Probably involved in the uptake of amidated and deamidated forms of niacin. Increases the growth rate of E.coli that is unable to make niacin de novo; confers increased sensitivity to the toxic niacin analog 6-amino-nicotinamide to wild-type E.coli. There is probably another mechanism for niacin uptake.
A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids.
A non-functional D-aminoacyl-tRNA deacylase (PubMed:4292198, PubMed:24097941, PubMed:25441601).
An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality.
Could be the product of a pseudogene. The lack of an initiation codon prevents translation of this gene, in agreement with the observation that D-Tyr-tRNA(Tyr) deacylase activity cannot be detected in some strains of B.subtilis (PubMed:4292198, PubMed:24097941, PubMed:25441601). Mutagenesis to restore the start codon (in strain NCIB 3610, the parent of the fully sequenced 168) confers resistance to D-Tyr (PubMed:24097941).
Culture in the presence of D-Leu, D-Met, D-Trp or D-Tyr leads to growth inhibition due to their incorporation into protein, as well as inhibition of biofilm formation (PubMed:24097941). Partially contradictory results are seen in another study where growth occurs in the presence of 20 and 500 mg/ml D-Trp but not in 500 mg/ml D-Asp or D-Ser; whether these are the exact same strains is unknown (PubMed:25441601). Strains in which this gene is restored by mutagenesis are resistant to D-Leu, D-Met, D-Trp and D-Tyr and form biofilm even in the presence of D-amino acids, while maintaining the ability to incorporate at least D-Trp into peptidoglycan (PubMed:24097941).
The dtd gene from B.amyloliquefaciens strain A50 confers the ability to grow in the presence of 20 mg/ml D-Tyr and 500 mg/ml D-Asp to B.subtilis, showing it can be used as a selective marker in bacteria that do not have a functional copy of this gene. Spontaneous resistance to D-Tyr is very rare, on the order of 10(-9) (PubMed:25441601).
Catalyzes the decarboxylation of malate to pyruvate. Can use NAD and NADP, but with a strong preference for NAD. Can also catalyze the decarboxylation of oxaloacetate (PubMed:16788182). Involved in keeping the ATP levels high (PubMed:23136871).
Mutant can use either a gluconeogenic carbon source or glucose as efficiently as the wild-type strain (PubMed:16788182). The ATP concentrations in the mutant grown in minimal medium with glucose are similar to the wild-type level. ATP concentrations decrease by about 10% in malate minimal medium. The mleA-maeA-malS triple mutant shows a decrease in ATP concentrations by about 20% and a moderate growth defect (PubMed:23136871). NADPH overproduction is roughly halved in the deletion mutant (PubMed:33824210).
This protein undergoes protein self-splicing that involves post-translational excision of the intervening region (intein) followed by peptide ligation.
Belongs to the plasmid replication initiation factor family.
Probable DNA relaxase involved in the transfer of the integrative and conjugative element ICEBs1. Required for the transfer of ICEBs1. Probably mediates conjugation of ICEBs1 by nicking at oriT on the conjugative element and facilitates the translocation of a single strand of ICEBs1 DNA through a transmembrane conjugation pore into the recipient cell.
The oriT nick site is located within the nicK open reading frame.
In double copy it causes aberrant cell morphology, filamentation and inhibits sporulation. Hydrolyzes 5-bromo-4-chloroindolyl phosphate.
Belongs to the thymidylate kinase family.
Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Belongs to the peptide transporter carbon starvation (CstA) (TC 2.A.114) family.
Activates ICEBs1 gene expression, excision and transfer by inactivating the ICEBs1 repressor protein ImmR (PubMed:16105942, PubMed:21036995). RapI-mediated induction likely results from an increase in the specific activity of the protease ImmA, which mediates proteolysis of ImmR (PubMed:21036995). In addition, is involved in regulation of sporulation (PubMed:23526881). Acts as a phosphatase that specifically dephosphorylates the sporulation initiation phosphotransferase Spo0F and inhibits its activity (PubMed:23526881).
Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
Mg(2+)-activated ribonuclease which hydrolyzes RNA apparently nonspecifically into oligonucleotides with 5'-terminal phosphate.
Belongs to the glycoside hydrolase 171 family.
Catalyzes the exo-lytic cleavage of beta-1,4-N-acetylmuramate (beta-1,4-MurNAc) from the non-reducing ends of peptidoglycan chains (PubMed:33684445). Specifically hydrolyzes the natural, peptidoglycan-derived disaccharide MurNAc-GlcNAc and the artificial substrate para-nitrophenyl beta-N-acetylmuramic acid (pNP-MurNAc) (PubMed:33684445). Requires a MurNAc entity at the non-reducing end, and cannot cleave GlcNAc-MurNAc (PubMed:33684445). Probably plays a role in cell wall turnover and recycling (PubMed:33684445).
Contains an N-terminal catalytic domain and a C-terminal auxiliary domain (PubMed:33684445). A putative active site is located in a cleft within the interface of two subdomains (PubMed:33684445).
Deletion mutant accumulates specific cell wall fragments and shows growth defects under starvation conditions.
Oligomer of 11 identical subunits arranged in doughnut-like structure.
Required for transcription attenuation control in the Trp operon. This trans-acting factor seems to recognize a 10 bases nucleotide sequence in the Trp leader transcript causing transcription termination. Binds the leader RNA only in presence of L-tryptophan.
Required for transcription attenuation control in the trp operon. This trans-acting factor binds to trinucleotide repeats (GAG or UAG) located in the trp leader transcript causing transcription termination. Binds the leader RNA only in presence of L-tryptophan.
Belongs to the fatty acid desaturase type 1 family.
Catalyzes the introduction of a cis-double bond at the delta(5) position of existing saturated fatty acids attached to membrane phospholipids. It is not strictly specific for palmitic acid (C16) but can also accept C14 as well as C18 species to yield unsaturated fatty acids.
Transcriptionally regulated by DesR/DesK in response to cold shock.
Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
Involved in bacillithiol (BSH) biosynthesis. May catalyze the last step of the pathway, the addition of cysteine to glucosamine malate (GlcN-Mal) to generate BSH.
Mutant accumulates GlcN-Mal and does not produce BSH.
Belongs to the RNA methyltransferase RlmH family.
Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Belongs to the sigma-70 factor family. SigI subfamily.
Cells lacking this gene exhibit normal cell morphology and growth rate at 37 degrees Celsius, but cannot grow at high temperature.
Negatively regulated by the anti-sigma-I factor RsgI.
Negatively regulated by the anti-sigma-I factor RsgI. Upon exposure to heat, SigI is released from RsgI and activated. Transient heat activation of SigI may depend upon DnaK chaperone.
Part of the sigI-rsgI operon, which is transiently induced by heat stress. Expression is positively autoregulated via the sigma-I promoter (PubMed:11157964, PubMed:17185538). In exponentially growing cells, expression is regulated by the WalRK two-component system, which represses the sigma-I promoter and activates the sigma-A promoter, leading to the formation of a basal level of SigI (PubMed:23199363). WalRK can also positively and directly regulate transcription of the operon under heat stress through a binding site located upstream of the sigma-I promoter (PubMed:24125693). Repressed by glucose (PubMed:17185538).
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is involved in regulation of cell wall metabolism in response to heat stress. Acts by regulating the expression of genes such as bcrC, mreBH and lytE (PubMed:18156261, PubMed:21541672, PubMed:23199363). Also plays a role in survival at low temperatures (PubMed:19114499).
Cells lacking this gene show DNase activity when exposed to thermal stress. Also shows an increased ability of competence.
Shows DNase activity on double strand DNA.
Monomer. Heterodimer consisting of two non-identical subunits: a glutamine amidotransferase subunit (PabA) and a aminodeoxychorismate synthase subunit (PabB).
Part of a heterodimeric complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p-aminobenzoate (PABA) and tetrahydrofolate. In the first step, a glutamine amidotransferase (PabA) generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by aminodeoxychorismate synthase (PabB) to produce ADC.
Requires p-aminobenzoic acid but not tryptophan for growth.
The catalytically active amino acid residue K274 of E.coli enzyme is missing and corresponds to A283 in B.subtilis. It is postulated that the enzymatic mechanism for the PABA biosynthesis in B.subtilis proceeds without covalent intermediate. First, ammonia is added at C2 of chorismate with concomitant loss of the C4 hydroxy group, yielding 2-amino-2-deoxyisochorismate (ADIC). The second step is the addition of a second molecule ammonia to C4 of ADIC with concomitant loss of the C2 amino group, yielding ADC. Both steps are catalyzed by ADCS (PubMed:19275258).
Belongs to the PNP/UDP phosphorylase family.
Catalyzes the reversible phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.
According to PubMed:16233211, SerC is not involved in pyridoxine biosynthesis in B.subtilis. In this organism, pyridoxal phosphate biosynthesis is achieved via an alternative pathway involving PdxS and PdxT.
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.
Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
Impaired ability to form spores when associated with a ytrI deletion. In combination with a ybaN deletion, cells show a severe sporulation defect.
Involved in sporulation. May contribute to cortex formation or stability.
Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Homodimer (By similarity). Probably interacts with PlsY.
Homodimer. Probably interacts with PlsY.
Probably part of an ABC transporter complex. Probably responsible for the translocation of the substrate across the membrane (By similarity).
Belongs to the methyltransferase superfamily. RlmI family.
Belongs to the transcriptional antiterminator BglG family. GlcT subfamily.
Composed of 3 domains: an N-terminal RNA-binding domain that prevents transcriptional termination, and two PTS regulation domains, PRD 1 and PRD 2. PRD 1 is the target of negative control exerted by EII-Glc and PRD 2 is the target of HPr.
Homodimer (By similarity). The monomeric form probably also exists but it would be inactive in RNA binding and antitermination.
Mediates the positive regulation of the glucose PTS operon (ptsGHI) by functioning as an antiterminator factor of transcription via its interaction with the RNA-antiterminator (RAT) sequence located upstream of the ptsG gene. The RNA-binding domain of GlcT directly binds to the RNA antiterminator (RAT) sequence and prevents transcriptional termination. GlcT binding requires two identical and nearly symmetrical triple base pairings in the RAT sequence.
Phosphorylated by HPr (PtsH) and EII-Glc (PtsG). HPr phosphorylates the PRD 2 domain which has a slight stimulatory effect on GlcT activity, while EII-Glc phosphorylates the PRD 1 domain which inactivates GlcT. The phosphorylation is dependent on the presence or absence of glucose which acts as an inducer of the ptsGHI operon expression. In the presence of glucose the phosphoryl group is transferred from phosphorylated HPr to the sugar via EII-Glc. Under these conditions GlcT is not phosphorylated and binds to the RAT sequence, thus allowing transcription of the ptsGHI operon. In the absence of glucose, phosphorylated EII-Glc accumulates in the cell and phosphorylates the PRD 1 domain of GlcT, leading to its inactivation; this phosphorylation may prevent dimerization of GlcT.
Interacts with RsbRA, RsbRB in the stressosome. The stressosome probably also contains RsbRC and RsbRD.
Phosphorylated by RsbT. Dephosphorylated by RsbX.
Belongs to the carbon-nitrogen hydrolase superfamily. NIT1/NIT2 family.
Impaired growth on methylthioribose (MTR) as sole sulfur source.
Involved in the methylthioribose (MTR) recycling pathway (PubMed:12022921, PubMed:24837359). Probably catalyzes the conversion of 2-oxoglutaramate to 2-oxoglutarate (PubMed:24837359).
Involved in bacillithiol (BSH) biosynthesis. Catalyzes the first step of the pathway, the formation of N-acetylglucosaminylmalate (GlcNAc-Mal) from UDP-N-acetylglucosamine (UDP-GlcNAc) and L-malate.
Member of the two-component regulatory system CssS/CssR required to control the cellular response to secretion stress.
Chaperone that serves for the intracellular sequestration and transport of Cu(+). Delivers Cu(+) to the copper-transporting ATPase CopA. Functions in E.coli to transfer Cu(+) to CopA missing its first metal-binding domain (PubMed:25899340).
Cu(+) ion is always at least three-coordinated. Physiological thiol may be needed to complete the Cu(+) coordination sphere in order to prevent homodimer (dead-end products) formation between 2 CopZ.
Monomer in the absence of copper. Homodimer in the presence of copper ions. Forms a heterodimer (electrostatic interactions) with CopA during the transfer of Cu(+).
Belongs to the RbsD / FucU family. RbsD subfamily.
Catalyzes the interconversion of beta-pyran and beta-furan forms of D-ribose.
Was originally thought (PubMed:7921236, PubMed:9353933) to be a high affinity ribose transport protein.
A farnesyl diphosphate (FPP) phosphatase. Involved in biofilm formation, its disruption blocks biofilm synthesis which is restored by exogenous farnesol (PubMed:25308276). Releases diphosphate from FPP, was initally suggested to be a squalene synthase. Diphosphate release is higher from FPP than geranyl pyrophosphate (GPP) or geranylgeranyl pyrophosphate (GGPP). Biofilm synthesis is partially restored by exogenous squalene, beta-carotene or retinol. Required for integrity of cell membrane lipid rafts (PubMed:20713508). Involved in spatial organization of membranes, required for the flotillin-like proteins FloT and FloA to function correctly (PubMed:23651456).
Belongs to the phytoene/squalene synthase family.
Diphosphate release from FPP is inhibited by zaragozic acid.
Loss of biofilm formation (PubMed:20713508, PubMed:25308276). Loss of a dark-orange pigment from cells, alteration of cellular lipid profile. Significant reduction of proteins found in detergent-resistant membrane (DRM) fractions (PubMed:20713508). Decrease in membrane fluidity, about 30% decrease in protein secretion (PubMed:23651456).
Was originally thought to be a squalene synthase (PubMed:20713508). Further characterization suggests it is actually a farnesyl diphosphate phosphatase (PubMed:25308276).
Belongs to the HAD-like hydrolase superfamily. PpaX family.
Hydrolyzes pyrophosphate formed during P-Ser-HPr dephosphorylation by HPrK/P. Might play a role in controlling the intracellular pyrophosphate pool.
Was originally (PubMed:9465101) called P-Ser-HPr phosphatase as it has been shown to stimulate P-Ser-HPr dephosphorylation, but actually (PubMed:12359880) it has pyrophosphatase activity.
Part of the ABC transporter complex TagGH (TC 3.A.1.34.1) involved in exporting the two types of intracellularly synthesized teichoic acids. Probably responsible for the translocation of the substrate across the membrane.
The complex is composed of two ATP-binding proteins (TagH) and two transmembrane proteins (TagG).
Belongs to the universal ribosomal protein uL15 family.
Belongs to the ABC transporter superfamily. Teichoic acids exporter (TC 3.A.1.104.1) family.
Part of the ABC transporter complex TagGH involved in teichoic acids export. Responsible for energy coupling to the transport system.
Disruption of the gene leads to almost full resistance to trifluoromethylthioribose (3FMTR), a toxic analog of MTR.
Involved in import of methylthioribose (MTR) into the cell.
Involved in a high affinity multicomponent binding-protein-dependent transport system for choline. Probably responsible for energy coupling to the transport system.
LH45 is not a natural strain. It has been constructed by transformation of strain 168 with linear DNA from B.subtilis ATCC 6633. It is a subtilin-producing mutant of B.subtilis 168 (PubMed:7592481).
An anti-sigma-G factor, prevents premature activation of sigma-G factor in the forespore; overexpression leads to 1000-fold reduction in spore formation, spore formation stops after engulfment (PubMed:17921305, PubMed:19497328). Overexpression also inhibits sigma-G transcription activation activity (PubMed:18208527). When both Gin and sigma-G are expressed in E.coli Gin inhibits sigma-G, strongly suggesting Gin inhibits by direct physical interaction (PubMed:19497328).
Binds 0.5 mol of zinc/mol protein, probably 1 zinc per dimer.
During sporulation under control of sigma-F factor.
Expressed starting 2 hours after sporulation onset for at least 7 hours.
Premature expression of sigma-G factor (sigG or spoIIIG) activity during the early stages of forespore development (PubMed:17921305, PubMed:18208527). Spore formation continues normally (PubMed:17921305, PubMed:8759874). However its absence has deleterious effects on strain robustness and is strongly selected against in competitions experiments (PubMed:18208527).
Probably functions as a homodimer (PubMed:19497328). Interacts with sigma-G factor, recognition occurs via the first 71 residues of sigma-G (PubMed:18208527, PubMed:19497328).
Belongs to the NrnA oligoribonuclease family.
Bifunctional enzyme which has both oligoribonuclease and pAp-phosphatase activities. Degrades RNA and DNA oligonucleotides with a length of 5 nucleotides and shorter, with a preference for 3-mers. Directionality is controversial; shown to degrade 5-mers and less in a 3' to 5' direction (PubMed:17586819), and 11-mers in a 5' to 3' direction (PubMed:21087930). Converts 3'(2')-phosphoadenosine 5'-phosphate (PAP) to AMP.
In accordance with its dual activities, is able to complement both orn and cysQ mutants in E.coli.
Belongs to the DAO family. ThiO subfamily.
Catalyzes the FAD-dependent oxidative deamination of various amines and D-amino acids to yield the corresponding alpha-keto acids, ammonia/amine, and hydrogen peroxide. Oxidizes sarcosine (N-methylglycine), N-ethylglycine and glycine (PubMed:9827558, PubMed:11744710, PubMed:19864430). Can also oxidize the herbicide glyphosate (N-phosphonomethylglycine) (PubMed:19864430). Displays lower activities on D-alanine, D-valine, D-proline and D-methionine (PubMed:9827558, PubMed:11744710). Does not act on L-amino acids and other D-amino acids (PubMed:9827558). Is essential for thiamine biosynthesis since the oxidation of glycine catalyzed by ThiO generates the glycine imine intermediate (dehydroglycine) required for the biosynthesis of the thiazole ring of thiamine pyrophosphate (PubMed:12627963).
Cells lacking this gene have an absolute requirement for the thiazole alcohol for growth.
Introducing the gene coding for the glycine oxidase mutant Ser-51/Arg-54/Ala-244 in plants may be an effective alternative mechanism for glyphosate tolerance in transgenic crops. In addition, transgenic plants that are able to oxidize glyphosate may represent an innovative bioremediation system for the soil treated with this herbicide.
Is competitively inhibited by glycolate.
Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family.
Has 2 similar domains, D1 (approximately residues 1-600) and D2 (approximately residues 601-1193). D1 is able to bind membranes, tether liposomes and cause membrane fusion in the absence of D2; both regions are required for GTPase activity. Possibly the fusion of 2 dynamin-like genes (PubMed:21205012). D1 alone promotes membrane tethering but requires D2 for stable tethering and content mixing (PubMed:31361971).
Has intrinsic affinity for membranes and membrane distortion capability; causes tubulation and membrane distortion when expressed in a Drosophila cell line.
Homodimer in solution (Probable). Both D1 and D2 domains interact with YwpG, YneK interacts only with D1 while RNase Y (rny) only interacts with whole protein (PubMed:23060960). Probably oligomerizes at damaged membrane sites (Probable).
Mediates lipid mixing of vesicles and full mixing of their contents in the absence and presence of GTP. Tethers and mixes small vesicles better than larger ones, indicating a curvature preference. GTP slows down DynA-mediated lipid fusion, perhaps controlling its activity. Prefers phospholipid composition close to the B.subtilis membrane; requires phosphatidylglycerol for fusion has no activity on pure phosphatidylethanolamine vesicles (PubMed:31361971). Regulates membrane lipid diffusion. Required to prevent membrane damage when exposed to low levels of membrane-damaging antibiotics or to bacteriophage. Probably surveys the cell membrane for stress; localizes to sites of membrane damage (treatment with nisin) and forms foci in cells treated with pore-forming compounds (CCCP). May assist membrane repair, possibly by membrane tethering and fusion (PubMed:26530236). Probably functions both in early and late cell division, affects the proper formation of the FtsZ ring. Plays a non-redundant role with flottilin (floT) in membrane dynamics and cell shape. Probably able to bend membranes (PubMed:23249255). Tethers liposomes and mediates their fusion; this does not require GTPase activity or the presence of GTP. Both GTPase domains (dynamin-type G) are required for GTPase activity (PubMed:21205012).
No visible phenotype (PubMed:21205012). 5% of cells have a double septa, 2% of cells are very long. Double dynA-ezrA mutants have longer cells with more double septa than either deletion alone. Double dynA-floT deletions are highly elongated, filamentous and have strong defects in cell shape; cells grow very slowly with an extended lag phase. Double dynA-mreB deletions have strong cell shape defects (PubMed:23249255). Double dynA-floT deletions are less motile than single floT deletions (PubMed:26842743). Increased lipid mobility in the cell membrane. Severe decrease in growth on nisin (causes membrane pore formation) with significant membrane deformation and damage, intermediate decrease in growth on antibiotics acting on lipid II or the membrane (bacitracin and daptomycin). No effect on growth on vancomycin (blocks peptidoglycan cross-links) or gramicidin D (makes small pores). 20-50% increased susceptibility to phage phi29 and SPbeta (PubMed:26530236).
Strain PSB025 / 25152 does not have the SP-beta prophage.
Alpha(8)-beta(8). The alpha component is a flavoprotein, the beta component is a hemoprotein.
Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate (Probable).
Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate.
Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides (By similarity).
Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides.
Catalyzes the formation of 5-methyl-uridine at positions 747 (m5U747) and 1939 (m5U1939) in 23S rRNA.
Belongs to the bacterial ribosomal protein bL36 family.
Allosterically activated by fructose 1,6-bisphosphate (FBP).
Catalyzes the conversion of lactate to pyruvate.
Involved in the metabolism of galactose. Catalyzes the conversion of UDP-galactose (UDP-Gal) to UDP-glucose (UDP-Glc) through a mechanism involving the transient reduction of NAD (By similarity).
Belongs to the phosphoglycerate mutase family. GpmB subfamily.
In contrast to other members of the family, has no phosphoglycerate mutase activity.
Phosphatase with broad substrate specificity. Does not have phosphoglycerate mutase activity.
Catalyzes the transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), a major component of the bacterial membrane with a positive net charge. LPG synthesis contributes to bacterial virulence as it is involved in the resistance mechanism against cationic antimicrobial peptides (CAMP) produces by the host's immune system (defensins, cathelicidins) and by the competing microorganisms.
Catalyzes the transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), one of the components of the bacterial membrane with a positive net charge. LPG synthesis contributes to the resistance to cationic antimicrobial peptides (CAMPs) and likely protects B.subtilis against its own CAMPs and against those produced by competiting microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with positively charged L-lysine results in repulsion of the peptides.
Cells lacking this gene lack lysyl-phosphatidylglycerol in their membranes. They also display an increased sensitivity to the antibiotics nisin and daptomycin (PubMed:18820022, PubMed:19164152). Cells appear normal, no effect on flotillin cluster numbers or size (PubMed:27362352).
A single active site specifically recognizes both ATP and CTP and is responsible for their addition.
Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Bacterial CCA-adding enzyme type 3 subfamily.
Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Has no poly(A) polymerase activity.
Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition is required both for tRNA processing and repair. Also involved in tRNA surveillance by mediating tandem CCA addition to generate a CCACCA at the 3' terminus of unstable tRNAs. While stable tRNAs receive only 3'-terminal CCA, unstable tRNAs are marked with CCACCA and rapidly degraded.
Was originally predicted to have poly(A) polymerase activity (EC 2.7.7.19), and its gene was named papS.
Functions as a fatty acid monooxygenase.
Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of a range of long-chain fatty acids, with a preference for long-chain unsaturated and branched-chain fatty acids over saturated fatty acids. Hydroxylation of myristic acid occurs mainly at the omega-2 position. Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain (PubMed:15375636, PubMed:15122913). Is also able to catalyze efficient oxidation of sodium dodecyl sulfate (SDS) (PubMed:21048857).
In the N-terminal section; belongs to the cytochrome P450 family.
May be involved in the formation or repair of [Fe-S] clusters present in iron-sulfur proteins.
Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
By Spo0A during nutrient starvation (PubMed:12817086). Repressed by AbrB during regular growth when nutrients are plentiful, in association with the transcriptional repressor Abh (PubMed:17720793).
This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA (By similarity). Binds biotin (PubMed:7592499).
Part of the ABC transporter complex YclNOPQ involved in uptake of ferric-petrobactin. Petrobactin is a photoreactive 3,4-catecholate siderophore produced by many members of the B.cereus group, including B.anthracis. Binds selectively iron-free and ferric petrobactin and the petrobactin precursor 3,4-dihydroxybenzoic acid (3,4-DHB).
The complex is composed of two ATP-binding proteins (YclP), two transmembrane proteins (YclN and YclO) and a solute-binding protein (YclQ) (Probable). Interacts with FloT (PubMed:23651456).
Belongs to the peptidase S14 family. TepA subfamily.
Required for efficient translocation of pre-proteins across the membrane.
Member of the two-component regulatory system YrkQ/YrkP.
Belongs to the xanthine dehydrogenase family.
Assembly of CotH requires CotE and GerE.
Expression is negatively regulated by the transcriptional regulator GerE.
Involved in the assembly of several proteins in the inner and outer layer of the spore coat. Stabilizes CotC and CotU in the mother cell compartment of sporulating cells and promotes the assembly of both early and late forms of CotC-related polypeptides on the spore surface.
Belongs to the pseudouridine synthase TruB family. Type 1 subfamily.
Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Acetylates both spermidine and spermine at primary propyl amine moieties, with spermine being the preferred substrate.
Putrescine and N(8)-acetylspermidine are competitive inhibitors of spermidine acetylation.
Expressed in sporulating cells. Disappears after 90 minutes of spore germination.
Stationary-phase cells lacking this gene are more sensitive to ionizing radiation. Growth rate, ultraviolet light and methyl-methanesulfonate sensitivities are unaffected. The spores formed are significantly more sensitive to dry heat, high vacuum-induced desiccation, X-rays and UV radiation, but no difference in hydrogen peroxide resistance exists.
With LigD forms a non-homologous end joining (NHEJ) DNA repair enzyme, which repairs dsDNA breaks with reduced fidelity. Binds linear dsDNA with 5'- and 3'- overhangs but not closed circular dsDNA nor ssDNA. Recruits and stimulates the ligase activity of LigD (By similarity). Probably involved in DNA repair during spore germination.
With LigD forms a non-homologous end joining (NHEJ) DNA repair enzyme, which repairs dsDNA breaks with reduced fidelity. Binds linear dsDNA with 5'- and 3'- overhangs but not closed circular dsDNA nor ssDNA. Recruits and stimulates the ligase activity of LigD.
To L.lactis phage infection protein (PIP).
Belongs to the thiolase-like superfamily. Chalcone/stilbene synthases family.
Involved in arginine degradative pathway.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. IF-2 subfamily.
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
The alternative initiation site Met-94 is uncertain.
Cells activate alkaline phosphatase during sporulation; the same phenotype is seen in the sapB2 and sapB10 mutants.
Induced during late exponential phase, and maximum expression is reached during the first hour of stationary phase, both under sporulation and non-sporulation conditions.
Deletion of the gene induces both differentiation pathways and interferes with their temporal separation.
Dual specificity regulatory protein that can control both sporulation and competence by acting on two distinct response regulators: Spo0F and ComA, respectively (PubMed:17581123, PubMed:21346797). Is involved in the temporal separation of competence and sporulation (PubMed:17581123). Acts as a phosphatase that specifically dephosphorylates the sporulation initiation phosphotransferase Spo0F and inhibits its activity (PubMed:17581123, PubMed:21346797). RapH can also antagonize sporulation by sterically blocking phosphoryl transfer to and from Spo0F (PubMed:21346797). In addition, inhibits the activity of ComA, a transcriptional factor that regulates the development of genetic competence (PubMed:17581123). Acts by binding to ComA, leading to the inhibition of its DNA-binding activity (PubMed:17581123).
Homodimer (PubMed:21346797). Interacts with phosphorylated Spo0F (PubMed:21346797). Each RapH protomer is bound to a monomer of Spo0F, forming an heterotetrameric complex (PubMed:21346797). May also interact with non-phosphorylated Spo0F to inhibit the sporulation phosphorelay (PubMed:21346797). Interacts with the C-terminal DNA-binding region of ComA (PubMed:17581123). Does not interact with DegU (PubMed:17581123).
Part of the rapH-phrH operon, which is transcribed from the SigA-driven rapH promoter (PubMed:21908671). Activated by the late competence transcription factor ComK (PubMed:17581123). Repressed by RghR (PubMed:16553878, PubMed:17581123).
Belongs to the acetyltransferase family. PAT/BAR subfamily.
This enzyme is an effector of phosphinothricin tripeptide (PTT or bialaphos) resistance. Inactivates PTT by transfer of an acetyl group (By similarity).
Belongs to the CidA/LrgA family. LrgA subfamily.
Inhibits the expression or activity of extracellular murein hydrolases by interacting, possibly with LrgB, with the holin-like protein CidA. The LrgAB and CidA proteins may affect the proton motive force of the membrane. May be involved in programmed cell death (PCD), possibly triggering PCD in response to antibiotics and environmental stresses.
Acts as a positive regulator of sigma-B activity in response to salt and heat stress by stimulating the activity of the RsbT kinase toward RsbS in vitro.
Cells lacking this gene have a decreased response to salt stress, indicating that RsbRA is a positive regulator of sigma-B activity. Its activity is dependent on RsbRB.
Interacts with RsbRB and RsbS in the stressosome. The stressosome probably also contains RsbRC and RsbRD.
Phosphorylated by RsbT. This threonine phosphorylation abrogates the ability of RsbRA to stimulate RsbT in vitro.
Belongs to the glycosyl hydrolase 18 family.
Cells lacking this gene display no visible phenotype during vegetative growth or sporulation.
Expressed during vegetative growth and sporulation.
Up-regulated by sigma-X and sigma-W factors.
Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of a range of medium to long-chain fatty acids, with a preference for long-chain unsaturated and branched-chain fatty acids over saturated fatty acids. Hydroxylation of myristic acid occurs mainly at the omega-2 and omega-3 positions, in approximately equal proportions. Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain.
Negatively regulated by the transcriptional repressor FatR (PubMed:11574077, PubMed:11734890). Is induced by fatty acids such as oleate, linoleate and phytanate, that bind and displace the FatR repressor (PubMed:11734890). Is also induced by palmitate, likely via another mechanism (PubMed:11574077). Transcribed under partial control of SigM ECF sigma factor (PubMed:17434969).
Belongs to the SEDS family. SpoVE subfamily.
May play an essential role not only during sporulation, but also during vegetative growth.
Belongs to the amino acid-polyamine-organocation (APC) superfamily. Basic amino acid/polyamine antiporter (APA) (TC 2.A.3.2) family.
Catalyzes electroneutral exchange between L-arginine and L-ornithine.
Has been described as a LysP lysine permease, due in part to the presence of LYS elements in the regulatory region.
Is also involved in protein lipoylation via its role as an octanoyl/lipoyl carrier protein intermediate.
Strains are lipoate auxotrophs. The requirement for lipoic acid can be bypassed by addition of both acetate and branched-chain fatty acid (BCFA) precursors.
The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
Involved in the degradation of anti-sigma-W factor RsiW. Responsible for Site-1 cleavage of the RsiW anti-sigma factor. This results, after two other proteolytic steps catalyzed by the RasP and ClpXP proteases, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Seems to be responsible for sensing antimicrobial peptides that damage the cell membrane and other agents that cause cell envelope stress. Therefore it is a protease governing regulated intramembrane proteolysis and resistance to antimicrobial peptides in B.subtilis.
Loss of expression of the SigW regulon (PubMed:17020587).
Catalyzes the transformation of pimelate into pimeloyl-CoA with concomitant hydrolysis of ATP to AMP.
Proton-dependent transporter. May mediate the efflux of lincomycin.
Key element in the phosphorelay regulating sporulation initiation. Phosphorylation of spo0B during sporulation initiation.
Phosphorylated by KinA and KinB. Dephosphorylated by RapA and RapB.
Catalyzes the oxidative cleavage of the C-S bond of N-acetyl-S-(2-succino)cysteine, forming oxaloacetate and N-acetylcysteine (NAC) (PubMed:34510734). Is involved in a S-(2-succino)cysteine (2SC) degradation pathway that allows B.subtilis to grow on 2SC as a sole sulfur source, via its metabolization to cysteine (PubMed:29626092). Shows almost no activity on S-succinylglutathione and 2SC (PubMed:34510734).
Cells lacking this gene almost lose the ability to grow on 2SC as the sulfur source but are still able to grow on sulfate. Moreover, they show a massive accumulation of N-acetyl-S-(2-succino)cysteine when S2C is added to the medium.
The substrate N-acetyl-S-(2-succino)-L-cysteine arises from the spontaneous Michael addition of cysteine to the citric acid cycle intermediate fumarate.
Required for formate dehydrogenase (FDH) activity (PubMed:7860592). Acts as a sulfur carrier protein that transfers sulfur from IscS to the molybdenum cofactor prior to its insertion into FDH (By similarity).
Required for formate dehydrogenase (FDH) activity. Acts as a sulfur carrier protein that transfers sulfur from IscS to the molybdenum cofactor prior to its insertion into FDH.
Entirely encoded within the dnaG gene, on the opposite strand.
In the central section; belongs to the PINc/VapC protein family.
Belongs to the Cob(I)alamin adenosyltransferase family.
Catalyzes the CoA-dependent transfer of an acetyl group to maltose and other sugars. Acetylates glucose exclusively at the C6 position and maltose at the C6 position of the non-reducing end glucosyl moiety. Is able to acetylate maltooligosaccharides.
Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrE subfamily.
Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Belongs to the KAE1 / TsaD family. TsaB subfamily.
Cells lacking this gene display a slow growth phenotype. Cell size, shape and nucleoid morphology remain unchanged.
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaE; this reaction does not require ATP in vitro. TsaB seems to play an indirect role in the t(6)A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD.
Belongs to the PAPS reductase family. CysH subfamily.
Catalyzes the formation of sulfite from adenosine 5'-phosphosulfate (APS) using thioredoxin as an electron donor.
No change in localization of FloA or FloT.
Exo-fructosidase that can hydrolyze both levan and inulin, leading to the production of free fructose. Is also able to hydrolyze sucrose and to a small extent raffinose, but not melezitose, stachylose, cellobiose, maltose, and lactose.
Induced by low concentrations of fructose, but not by sucrose. Repressed by glucose or high concentrations of fructose.
Is completely inhibited by Ag(+) and Hg(2+) ions.
Levanase cannot be detected in the wild-type B.subtilis but is mostly secreted into the culture medium by SacL mutants, especially at the end of the exponential growth phase.
To C.plantagineum desiccation-related protein clone PCC3-06.
Forms a complex with TatCy. Two types of complexes exist: one composed of TatAy and TatCy, and another composed only of TatAy. Cytosolic TatA forms large complexes or aggregates.
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system. Required for YwbN secretion.
Putative oxidoreductase that may contribute to the degradation of aromatic compounds.
Repressor of PBSX. Binds to four sites close to its own gene. Necessary for the maintenance of the lysogenic state.
The defective prophage of Bacillus subtilis 168, PBSX, is a chromosomally based element which encodes a non-infectious phage-like particle with bactericidal activity. PBSX is induced by agents which elicit the SOS response (PubMed:2125016).
Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
Belongs to the GTP-binding SRP family. FtsY subfamily.
Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC).
Removes 5-oxoproline from various penultimate amino acid residues except L-proline.
Catalyzes the removal of elemental sulfur from cysteine to produce alanine (By similarity). Seems to be required for NAD biosynthesis (PubMed:8444804).
Cells lacking this gene require nicotinic acid for growth.
Repressed in the presence of nicotinic acid.
May be involved in cell division and sporulation.
Cells lacking this gene show a derepression of lutABC expression. They are also defective in bacilysin production.
Negatively regulates the transcription of the lutABC operon, which is required for L-lactate utilization. LutR activity is regulated by lactate, since presence of L-lactate, that probably binds to LutR, leads to derepression of the operon. Also appears to be essential for bacilysin biosynthesis.
Belongs to the GHMP kinase family. IspE subfamily.
Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Probably part of the ABC transporter complex YxeMNO that could be involved in amino-acid import. May transport S-methylcysteine. Probably responsible for the translocation of the substrate across the membrane (Probable).
Mutation impairs pellicle formation, complex colony architecture and motility inhibition in a sinR mutant background (PubMed:19363116). Mutant is defective in biofilm formation and also shows a delay in spore formation during biofilm formation (PubMed:23396918).
Regulates the biosynthesis of the extracellular matrix and the biofilm formation (PubMed:19363116, PubMed:23646920). Activates the transcription of the matrix biosynthesis operons eps and tapA-sipW-tasA. Also activates expression of the opuA operon, involved in osmoprotection. Acts by binding specifically to the promoter region of the target genes (PubMed:23646920). Acts in parallel to the pathway that governs SinR derepression (PubMed:19363116, PubMed:23646920). Required for endosporulation (PubMed:23396918).
Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis acid cofactor.
Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
Belongs to the metallo-dependent hydrolases superfamily. CpsB/CapC family.
Dephosphorylates the phosphotyrosine-containing proteins YwqD, YwqF and Ssb.
Inhibited by vanadate and sodium pyrophosphate. Not inhibited by sodium fluoride.
Contains two domains, a large N-terminal domain encoding a serine protease homologous to subtilisin and a smaller C-terminal domain that possesses unusual sequence features (PubMed:2116590, PubMed:3142851, PubMed:16553828). The C-terminal third of the protein is not required for protease activity but is required for swarming (PubMed:2116590, PubMed:3142851, PubMed:16553828).
Disruption of the gene abolishes swarming (PubMed:11751842, PubMed:19416356). Mutant lacking this gene does not show significant decrease in CSF production, but the triple deletion mutant aprE-epr-vpr is defective in the cleavage event to release mature CSF (PubMed:17666034).
Expression is sigma D-dependent (PubMed:11751842). Expression is positively regulated by DegU, and very low levels of DegU-P are required for epr maximal expression (PubMed:19416356). Negatively regulated jointly by ScoC (Hpr) and SinR, which bind to their respective target sites 62 bp apart (PubMed:16923912). Spo0A positively regulates epr expression by negating the repressive effect of corepressors, SinR and ScoC (Hpr) (PubMed:23660663). Spo0A binds to the upstream region of epr promoter and in turn occludes the binding site of one of the corepressor, SinR (PubMed:23660663).
May undergo two steps of processing in its passage through the cell membrane: removal of the N-terminal signal sequence and cleavage of the C-terminal domain (PubMed:16553828). Several active forms of Epr with molecular masses between 40 and 34 kDa were found in the medium of B.subtilis cultures (PubMed:2116590). The size variation of the active forms expressed by the complete epr gene appears to be the result of partial removal of the C-terminus either by processing or degradation (PubMed:2116590).
Requires Ca(2+) for stability (PubMed:2116590). Activity is inhibited by phenylmethylsulfonyl fluoride (PMSF) and EDTA (PubMed:2116590, PubMed:3142851).
Serine protease (PubMed:3142851, PubMed:2116590, PubMed:17666034). Involved in the production of the competence and sporulation stimulating factor CSF (PubMed:17666034). In addition, is essential for swarming motility (PubMed:11751842, PubMed:16553828, PubMed:19416356). Plays a key role in DegU-mediated swarming motility (PubMed:19416356). The protease activity is dispensable for swarming (PubMed:16553828). Not essential for growth or sporulation (PubMed:3142851).
Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NAD to NADH. Does not contribute to oxidative pentose phosphate (PP) pathway fluxes during growth on glucose. The functional role of GntZ remains obscure.
Cells lacking this gene exhibit no detectable phenotype on glucose as the sole carbon source, and they grow normally on gluconate.
Belongs to the DNA polymerase type-A family.
In addition to polymerase activity, this DNA polymerase exhibits 3'-5' and 5'-3' exonuclease activity.
In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
Single-chain monomer with multiple functions.
A lyase-type mechanism (elimination/hydration) is suggested for the cleavage of the lactyl ether bond of MurNAc 6-phosphate, with the formation of an alpha,beta-unsaturated aldehyde intermediate with (E)-stereochemistry, followed by the syn addition of water to give product.
Belongs to the GCKR-like family. MurNAc-6-P etherase subfamily.
Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D-lactate.
Probable member of the two-component regulatory system YkoH/YkoG. Potentially phosphorylates YkoG.
General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr).
Homodimer (By similarity). Interacts with FloT (PubMed:23651456).
The N-terminal domain contains the HPr binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site.
The reaction takes place in three steps, mediated by a phosphocarrier histidine residue located on the surface of the central domain. The two first partial reactions are catalyzed at an active site located on the N-terminal domain, and the third partial reaction is catalyzed at an active site located on the C-terminal domain. For catalytic turnover, the central domain swivels from the concave surface of the N-terminal domain to that of the C-terminal domain.
Not essential for cell viability, but required for efficient secretion of many proteins.
Involved in the biosynthesis of galactosamine-containing minor teichoic acid, a non-essential cell wall polymer in B.subtilis 168.
Monomer. Binds directly to the core enzyme of the DNA-dependent RNA polymerase and to nascent RNA.
Participates in both transcription termination and antitermination.
Catalyzes the alpha- and beta-hydroxylation of myristic acid in the presence of hydrogen peroxide.
According to PubMed:11011148, cells show no effect vegetative growth, spore resistance to heat, chloroform and lysozyme, or spore germination in the presence of L-alanine. According to PubMed:12177332, cells have no detectable alteration in either dormant or germinating spore peptidoglycan, and germinate normally.
Cells producing excessive ydhD do not show impaired spore resistance, but their germination properties change: spores show reduced response to L-alanine and some of them germinate even without germinants.
Transcription of ydhD is dependent on SigE.
Along with the bacABCDEF operon, BacG is involved in the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin, composed of L-alanine and L-anticapsin. Bacilysin is an irreversible inactivator of the glutaminase domain of glucosamine synthetase (PubMed:20052993). BacG catalyzes the stereoselective reduction of exocyclic-delta(3),delta(5)-dihydro-hydroxyphenylpyruvate (ex-H2HPP), adding a pro-S hydride equivalent to C4 position to yield tetrahydro-hydroxyphenylpyruvate (H4HPP) (PubMed:22765234, PubMed:23519407). Although the 3Z,7R-ex-H2HPP isomer is kinetically disfavored by BacB and produced in a smaller quantity than 3E,7R-ex-H2HPP, it is the preferred substrate for the conjugate reduction reaction of BacG (PubMed:22765234, PubMed:23519407).
Induced at the onset of sporulation, shuts off at T3. May be under the control of Spo0A.
No observable effect on sporulation (PubMed:8002615). Forms a weak or no biofilm, wild-type sporulation (PubMed:22882210, PubMed:26297017).
Oligomerizes, probably forms homodimers; oligomerization is assisted by FloT. Interacts with FloT (PubMed:26297017). Another study shows only rare colocalization with FloT or FloA membrane assemblies. KinC membrane assemblies are more mobile than FloT membrane assemblies (PubMed:27362352).
Phosphorylates the sporulation-regulatory protein Spo0A a transcription factor that also controls biofilm formation (Probable). Requires FloT and FloA for localization to DRMs and for activity (PubMed:20713508).
Member of the two-component regulatory system YvfT/YvfU.
May be directly involved in the regulation of the rib genes. C-terminal part of RibR specifically binds to RFN of the rib leader of the riboflavin biosynthetic operon. The RFN element is a sequence within the rib-leader mRNA reported to serve as a receptor for an FMN-dependent riboswitch. Possibly, RibR produces the comodulator FMN through its own N-terminal flavokinase activity. FMN-activated RibR may stabilize the anti-anti terminator structure of RFN mRNA, causing transcription termination of the rib genes in trans.
Mutants lacking this gene are deregulated with respect to flavin (riboflavin, FMN and FAD) biosynthesis.
Overexpression of RibR suppresses the riboflavin-overproducing ribC-defective phenotype, which is the major riboflavin kinase responsible of FMN biosynthesis by riboflavin phosphorylation (PubMed:17590224, PubMed:15668000).
Repressed by the HTH-type transcriptional regulator CymR.
Part of the ABC transporter complex MetNPQ involved in methionine import. Binds the methionine and transfers it to the membrane-bound permease. It has also been shown to be involved in methionine sulfoxide transport (Probable).
Binds long-chain fatty acids, such as palmitate, and may play a role in lipid transport or fatty acid metabolism.
Catalyzes the formation of UDP-glucose from glucose-1-phosphate and UTP (PubMed:33556370). This is an intermediate step in the biosynthesis of diglucosyl-diacylglycerol (Glc2-DAG), i.e. the predominant glycolipid found in B.subtilis membrane, which is also used as a membrane anchor for lipoteichoic acid (LTA) (PubMed:33556370). YngB contributes to wall teichoic acid (WTA) glucosylation and glycolipid formation under anaerobic fermentative growth conditions (PubMed:33556370). Might also enter other glycosylation pathways, leading to the decorating of other cell envelope components with glucose residues under anaerobic or other growth conditions (PubMed:33556370).
In response to ammonium, tryptophan, glucose, and phosphate starvation.
Cells lacking this gene show no apparent growth, sporulation, or germination defect. Also shows no defect in the synthesis of the membrane-bound CccB cytochrome or any other cytochrome with covalently bound heme.
Belongs to the DadA oxidoreductase family.
Deletion mutant is more sensitive to methylglyoxal than wild-type.
Potassium antiport activity requires the presence of KhtT. Activity is also modulated by KhtS. Has higher activity at alkaline pH.
Potassium/proton antiporter that mediates the efflux of potassium ions from the cell (PubMed:17679694). Can also mediate rubidium/proton antiport, but has no permeability for sodium or lithium ions. In the absence of KhtT, does not have antiport activity, but can catalyze potassium efflux (PubMed:14987767, PubMed:17679694). Involved in protection of the cell from methylglyoxal, a toxic by-product of glycolysis, via activation by S-lactoyl-BSH of the antiporter activity, leading to cytoplasmic acidification and methylglyoxal resistance (PubMed:24330391).
Disruption of glnL by Tn917 insertion leads to protonophore-resistance.
Member of the two-component regulatory system GlnL/GlnK that positively regulates the expression of the glsA-glnT operon in response to glutamine. GlnL binds the promoter region of glsA-glnT in vitro.
Required for resistance to linearmycins, a family of antibiotic-specialized metabolites produced by some streptomycetes (PubMed:26647299, PubMed:28461449). Member of the two-component regulatory system LnrJ/LnrK, which induces expression of the LnrLMN ABC transporter in response to linearmycins and other polyenes (PubMed:11717295, PubMed:26647299, PubMed:28461449). Acts as a specific sensor for linearmycin, either directly through binding or indirectly through membrane perturbation. Probably activates LnrK by phosphorylation (PubMed:28461449). May also promote biofilm formation (PubMed:28461449).
The N-terminus share sequence similarity with the dihydrodipicolinate reductase family. It however lacks the conserved C-terminal part, suggesting it has no dihydrodipicolinate reductase activity.
Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Belongs to the ABC transporter superfamily. Aliphatic sulfonates importer (TC 3.A.1.17.2) family.
Part of the ABC transporter complex SsuABC involved in aliphatic sulfonates import. Responsible for energy coupling to the transport system (Probable). Is also involved in taurine transport.
The complex is composed of two ATP-binding proteins (SsuB), two transmembrane proteins (SsuC) and a solute-binding protein (SsuA).
Belongs to the class I-like SAM-binding methyltransferase superfamily. MenG/UbiE family.
Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2).
Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR).
Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)- to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR).
By competence, expression activated by ComK (PubMed:11948146). By DNA damage.
Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.
Cells lacking this gene are extremely sensitive to DNA-damaging agents. They show 4-fold impaired growth in their absence.
Induced during competence (PubMed:11948146).
Monomer; forms higher-order oligomers (PubMed:16061691). Interacts with RecU (PubMed:18684995). Interacts with DprA (smf) (PubMed:17803906).
Multifunctional protein involved in homologous recombination, DNA repair and competence (PubMed:16061691, PubMed:16385024, PubMed:17803906, PubMed:18684995, PubMed:25138221). Can catalyze the hydrolysis of (d)ATP in the presence of single-stranded DNA; prefers dATP at least in vitro, catalyzes the dATP-dependent uptake of single-stranded DNA by duplex DNA, and the dATP-dependent hybridization of homologous single-stranded DNAs (strand exchange) (PubMed:25138221). RecA-ATP cannot catalyze homologous DNA strand exchange; SsbA and DprA activate strand exchange by RecA-ATP (PubMed:25138221). It interacts with LexA causing its activation and leading to its autocatalytic cleavage. Hydrolysis of ATP in the presence of single-stranded DNA is partially inhibited by RecU (PubMed:18684995). Required for DNA transformation; protects transforming DNA from degradation, possibly in combination with DprA (PubMed:17803906).
Recruited to repair centers (RCs), foci that are the site of double-stranded DNA break(s), after RecN (PubMed:16061691). Concomitant with the appearance of RecO at the RCs, RecA forms threads that extend from RCs toward the opposite cell half, possibly searching for sequence homology along the sister chromosome. The threads disappear after about 2 hours (PubMed:16061691). Thread formation is absolutely dependent on RecJ or AadAB (PubMed:16385024).
Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration.
Belongs to the CidB/LrgB family. LrgB subfamily.
Inhibits the expression or activity of extracellular murein hydrolases by interacting, possibly with LrgA, with the holin-like protein CidA. The LrgAB and CidA proteins may affect the proton motive force of the membrane. May be involved in programmed cell death (PCD), possibly triggering PCD in response to antibiotics and environmental stresses.
Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane.
Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane. May serve as a defense mechanism against naturally occurring MurJ antagonists.
Mutants lacking both murJ and amj have a lethal defect in cell wall synthesis.
Transcribed under partial control of SigM ECF sigma factor (PubMed:17434969, PubMed:25918422). Expression is up-regulated in the absence of MurJ (PubMed:25918422).