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.
Monomer. Interacts with itself to form filaments; also interacts with TraQ.
Belongs to the ABC transporter superfamily. CcmA exporter (TC 3.A.1.107) family.
Part of the ABC transporter complex CcmAB involved in the biogenesis of c-type cytochromes; once thought to export heme, this seems not to be the case, but its exact role is uncertain. Responsible for energy coupling to the transport system.
The complex is composed of two ATP-binding proteins (CcmA) and two transmembrane proteins (CcmB).
Belongs to the MurCDEF family. Mpl subfamily.
Reutilizes the intact tripeptide L-alanyl-gamma-D-glutamyl-meso-diaminopimelate by linking it to UDP-N-acetylmuramate.
Belongs to the bacterial solute-binding protein 3 family.
Part of an ABC transporter involved in lysine, arginine and ornithine transport. Stimulates ATPase activity of HisP.
The complex is composed of two ATP-binding proteins (HisP), two transmembrane proteins (HisM and HisQ) and a solute-binding protein (ArgT).
Belongs to the prolyl-tRNA editing family. YbaK/EbsC subfamily.
Functions in trans to edit the amino acid from incorrectly charged Cys-tRNA(Pro) via a Cys-tRNA(Pro) deacylase activity.
Reaction mechanism involves exclusion of catalytic water from the active site and substrate-mediated catalysis: the sulfhydryl side chain of the Cys substrate acts as a nucleophile and attacks the carbonyl center of the ester bond, leading to the cleavage of the Cys-tRNA ester bond and formation of a cyclic cysteine thiolactone intermediate. In contrast, the INS editing domain of ProRS catalyzes Ala-tRNA(Pro) hydrolysis via nucleophilic attack by a catalytic water molecule (By similarity).
Belongs to the acetolactate synthase small subunit family.
S.typhimurium contains genes for 3 AHAS isozymes: ilvBN, ilvGM and ilvIH.
Belongs to the NAD(P)-dependent epimerase/dehydratase family.
The functional difference between abequose synthase and paratose synthase lies in the side of the pyranose ring from which the keto group on carbon 4 is attacked in the reduction of CDP-4-keto-3,6-dideoxy-D-glucose.
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.
Required for optimal acid stress protection, which is important for survival of enteric bacteria in the acidic environment of the host stomach. Exhibits a chaperone-like activity at acidic pH by preventing the aggregation of many different periplasmic proteins.
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 and in the biotin biosynthesis (By similarity).
The antibiotic diazaborine interferes with the activity by binding to the protein.
Not essential, it has a diminished capacity to survive in murine macrophages.
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 DNA polymerase type-A family.
In addition to polymerase activity, this DNA polymerase exhibits 3'-5' and 5'-3' exonuclease activity. It is able to utilize nicked circular duplex DNA as a template and can unwind the parental DNA strand from its template.
Single-chain monomer with multiple functions.
Essential component of the Rcs signaling system, which controls transcription of numerous genes. Plays a role in signal transduction from the cell surface to the histidine kinase RcsC. May detect outer membrane defects.
Belongs to the nucleobase:cation symporter-2 (NCS2) (TC 2.A.40) family.
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.
Induced by MurNAc 6-phosphate that releases the repressor MurR from the DNA. Repressed by MurR in the absence of MurNAc 6-phosphate.
Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D-lactate. Together with AnmK, is also required for the utilization of anhydro-N-acetylmuramic acid (anhMurNAc) either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling.
Belongs to the 5-formyltetrahydrofolate cyclo-ligase family.
Belongs to the LysR transcriptional regulatory family.
Anaerobic nitric oxide reductase; uses NADH to detoxify nitric oxide (NO), protecting several 4Fe-4S NO-sensitive enzymes. Has at least 2 reductase partners, only one of which (NorW, flavorubredoxin reductase) has been identified. NO probably binds to the di-iron center; electrons enter from the NorW at rubredoxin and are transferred sequentially to the FMN center and the di-iron center. Also able to function as an aerobic oxygen reductase.
In the N-terminal section; belongs to the zinc metallo-hydrolase group 3 family.
A mutant in which deletion of the last 50 residues in ubiA is combined with the Tyr-56 mutation in rsmG is highly resistant to streptomycin and has a small colony phenotype (which grow slowly and are resistant to aminoglycoside anitbiotics).
Belongs to the methyltransferase superfamily. RNA methyltransferase RsmG family.
Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Belongs to the polysaccharide transport (PST) (TC 2.A.66.2) family.
Mediates the transbilayer movement of Und-PP-GlcNAc-ManNAcA-Fuc4NAc (lipid III) from the inner to the outer leaflet of the cytoplasmic membrane during the assembly of enterobacterial common antigen (ECA).
Probably part of a complex composed of WzxE, WzyE and WzzE.
Belongs to the binding-protein-dependent transport system permease family. FecCD subfamily.
Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly.
Belongs to the glycosyltransferase 56 family.
Catalyzes the synthesis of Und-PP-GlcNAc-ManNAcA-Fuc4NAc (Lipid III), the third lipid-linked intermediate involved in ECA synthesis.
Belongs to the transferase hexapeptide repeat family.
Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate.
Belongs to the fimbrial export usher family.
Catalyzes the dehydration of galactarate to form 5-dehydro-4-deoxy-D-glucarate (5-KDG).
Belongs to the drug/metabolite transporter (DMT) superfamily. Small multidrug resistance (SMR) (TC 2.A.7.1) family.
Belongs to the DNA repair enzymes AP/ExoA family.
Major apurinic-apyrimidinic endonuclease of E.coli. It removes the damaged DNA at cytosines and guanines by cleaving on the 3'-side of the AP site by a beta-elimination reaction. It exhibits 3'-5'-exonuclease, 3'-phosphomonoesterase, 3'-repair diesterase and ribonuclease H activities (By similarity).
Probably binds two magnesium or manganese ions per subunit.
Belongs to the type IA topoisomerase family.
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.
Induced by L-ascorbate. Repressed by UlaR.
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.
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 UlaABC PTS system is involved in ascorbate transport.
Belongs to the lipid A palmitoyltransferase family.
Disruption of this gene increases outer membrane permeability in response to CAMP.
Regulated by the PhoP/PhoQ two-component regulatory system.
Transfers a fatty acid residue from the sn-1 position of a phospholipid to the N-linked hydroxyfatty acid chain on the proximal unit of lipid A or its precursors. Required for resistance to cationic antimicrobial peptides (CAMPs). Modifications of lipid A with an acyl chain allow to evade host immune defenses by resisting antimicrobial peptides and attenuating the inflammatory response to infection triggered by lipopolysaccharide through the Toll-like receptor 4 (TLR4) signal transduction pathway.
Belongs to the glycosyl hydrolase 13 family.
Removes maltotriose and maltotetraose chains that are attached by 1,6-alpha-linkage to the limit dextrin main chain, generating a debranched limit dextrin.
Belongs to the aconitase/IPM isomerase family.
Cells lacking this gene do not grow on propionate unless glutamate is added, and the addition of glutamate does not restore growth to the level of wild-type. Also unable to grow on acetate and citrate and only slight improvements are observed when glutamate is added. AcnB mutant also shows an impaired binding to the surface of macrophage-like cells, is less motile and possesses fewer flagella due to a level of the flagellum protein FliC lower. The acnAB double mutant does not grow on propionate even when supplemented with glutamate and is unable to respire propionate under anaerobic growth conditions.
Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. Also catalyzes the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate. The apo form of AcnB functions as a RNA-binding regulatory protein which regulates FliC synthesis via interaction with the ftsH transcript to decrease the intracellular levels of FtsH. The lower levels of FtsH protease activity then influence sigma-32, DnaK and ultimately FliC production.
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).
Controls the transcription of genes involved in arginine and lysine metabolism.
Interacts with FlhD in the FlhC(2)FlhD(4) heterohexamer, inhibiting its ability to activate transcription.
Involved in the export and assembly of FimA fimbrial subunits across the outer membrane.
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.
Belongs to the non-flavoprotein flavin reductase family. HpaC subfamily.
Catalyzes the reduction of free flavins (FMN, FAD and riboflavin) by NADH. Subsequently, the reduced flavins diffuse to the large HpaB component or to other electron acceptors such as cytochrome c and Fe(3+) ion (By similarity).
Homodimer. 4-HPA 3-monooxygenase consists of a reductase component HpaC and an oxygenase component HpaB (By similarity).
A component of the bacterial microcompartment (BMC) shell dedicated to ethanolamine degradation (PubMed:22428024, PubMed:27063436). Forms a hexagonal trimer with 3 small channels and a large central pore that has been seen in both open and closed forms and is probably used for gated transport into and out of the BMC (By similarity). Ethanolamine-binding by the small channels has been hypothesized to stabilize the EutL central pore in a closed (non-transporting) state. An open pore is thought to be large enough to transport ATP and/or cobalamin (By similarity). Expression of eutK, eutL, eutM, eutN, eutS (eutSMNLK) in E.coli leads to formation of a single BMC (PubMed:22428024, PubMed:27063436). Coexpression of eutQ with eutSMNLK permits E.coli to make cells with more than one mobile BMC, as is usual in vivo (PubMed:27063436).
Artificial BMCs can be made in E.coli by expressing eutK, eutL, eutM, eutN, eutS (eutSMNLK) or eutS alone. Cargo proteins can be targeted to them and beta-galactosidase (lacZ) was active within the BMC, showing the BMC allows passage of substrate into the interior. This can lead to the development of tailored BMCs for specific metabolic reactions (PubMed:22428024). The addition of eutQ to the eutSMNLK construct results in biogenesis of multiple BMCs (PubMed:27063436).
Expression of the eut operon allows this bacteria to use ethanolamine as a carbon, nitrogen and energy source. It relies on cobalamin (vitamin B12) both as a cofactor for the ethanolamine ammonia-lyase (EAL) activity and to induce the operon (PubMed:3045078). EA enhances bacterial survival in macrophages in a concentration-dependent manner, suggesting it is an important nutrient during infection (PubMed:29531136).
Has 2 BMC domains which can evolve independently of each other.
Not required for aerobic growth on ethanolamine (EA) supplemented with cobalamin (vitamin B12) (PubMed:10464203). A double eutL-eutK strain grows as well as wild-type on EA and cyanocobalamin, but a quadruple eutL-eutK eutM-eutN strain does not grow (PubMed:16291677). A non-polar deletion mutant grows on EA at pH 5.5 to pH 7.0 but not at pH 8.0 or pH 8.5, releases increased amounts of acetaldehyde on EA plus vitamin B12. Preventing acetaldehyde vapor loss allow growth up to pH 8.5 (PubMed:16585748).
Part of the 17-gene eut operon transcribed from a single promoter, induced by ethanolamine and adenosylcobalamin (AdoCbl, vitamin B12).
The ethanolamine (EA) catabolic bacterial microcompartment (BMC) probably concentrates low levels of ethanolamine catabolic enzymes, concentrates volatile reaction intermediates, keeps the level of toxic acetaldehyde low, generates enough acetyl-CoA to support cell growth, and maintains a pool of free coenzyme A (CoA) and NAD (Probable) (PubMed:16585748). Deletion of BMC genes (eutK, eutL, eutM) restores growth of eutD deletions, suggesting there are dedicated pools of coenzyme A (CoA) and NAD in the BMC (PubMed:23585538).
The need for a bacterial microcompartment in EA metabolism can be bypassed by increasing the levels of EAL and an acetaldehyde dehydrogenase (not necessarily EutE).
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).
Belongs to the ABC transporter superfamily. Sulfate/tungstate importer (TC 3.A.1.6) family.
Part of the ABC transporter complex CysAWTP involved in sulfate/thiosulfate import. Responsible for energy coupling to the transport system.
The complex is composed of two ATP-binding proteins (CysA), two transmembrane proteins (CysT and CysW) and a solute-binding protein (CysP).
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.
Belongs to the chloride channel (TC 2.A.49) family. ClcA subfamily.
Proton-coupled chloride transporter. Functions as antiport system and exchanges two chloride ions for 1 proton. Probably acts as an electrical shunt for an outwardly-directed proton pump that is linked to amino acid decarboxylation, as part of the extreme acid resistance (XAR) response.
Belongs to the radical SAM superfamily. Anaerobic sulfatase-maturating enzyme family.
Belongs to the bacterial ribosomal protein bL25 family.
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.
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 arabinose isomerase family.
Catalyzes the conversion of L-arabinose to L-ribulose.
Belongs to the FHIPEP (flagella/HR/invasion proteins export pore) family.
Required for formation of the rod structure of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin.
In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family.
In the N-terminal section; belongs to the aldehyde dehydrogenase family.
Component of the periplasmic nitrate reductase NapAB complex composed of NapA and NapB.
Electron transfer subunit of the periplasmic nitrate reductase complex NapAB.
Binds the cellulose synthase activator, bis-(3'-5') cyclic diguanylic acid (c-di-GMP).
Tightly associated with the cellulose synthase catalytic subunit.
Belongs to the acetyltransferase family. YpeA subfamily.
Belongs to the major facilitator superfamily. Metabolite:H+ Symporter (MHS) family (TC 2.A.1.6) family.
Uptake of citrate across the boundary membrane with the concomitant transport of protons into the cell (symport system) (Probable). Allows the utilization of citrate as a sole source of carbon and energy upon expression in E.coli (PubMed:1718953).
Component of the Rcs signaling system, which controls transcription of numerous genes. Binds, with RcsB, to the RcsAB box to regulate expression of genes.
Belongs to the prokaryotic GSH synthase family.
Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Involved in a secretory pathway responsible for the surface presentation of determinants needed for the entry of Salmonella species into mammalian cells.
Belongs to the class-I aminoacyl-tRNA synthetase family.
Catalyzes the attachment of tryptophan to tRNA(Trp).
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 ManXYZ PTS system is involved in mannose transport.
Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family.
Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the 2 position. This enzyme can utilize either acyl-CoA or acyl-acyl-carrier-protein as the fatty acyl donor.
The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Belongs to the binding-protein-dependent transport system permease family. CysTW subfamily.
Induced in response to increased extracellular osmolarity, this is the second gene of the proU operon (proV-proW-proX). Osmoregulation requires curved DNA downstream of the transcription start site in proV, which is repressed when bound by H-NS. H-NS may act indirectly to influence the local topology of the promoter (PubMed:1423593).
Part of the ProU ABC transporter complex involved in glycine betaine and proline betaine uptake. Probably responsible for the translocation of the substrate across the membrane.
The complex is composed of two ATP-binding proteins (ProV), two transmembrane proteins (ProW) and a solute-binding protein (ProX).
Belongs to the DegT/DnrJ/EryC1 family. ArnB subfamily.
Catalyzes the conversion of UDP-4-keto-arabinose (UDP-Ara4O) to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) (PubMed:12429098, PubMed:24460375). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides (By similarity).
Belongs to the D-alanine--D-alanine ligase family.
Binds 2 magnesium or manganese ions per subunit.
Belongs to the class-II aminoacyl-tRNA synthetase family.
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 GHMP kinase family. PduX subfamily.
Catalysis proceeds by a steady-state ordered bi-bi complex mechanism in which ATP is the first substrate to bind.
Growth is impaired on 1,2-PD minimal medium supplemented with cobyric acid, but is restored on similar medium supplemented with vitamin B12, cobinamide (PubMed:18308727). A double pduW-pduX deletion grows as well as wild-type on 1,2-PD (PubMed:12700259).
L-threonine kinase that catalyzes the conversion of L-threonine to L-threonine-O-3-phosphate. Involved in the de novo synthesis of adenosylcobalamin (coenzyme B12) and the assimilation of cobyric acid. Uses ATP; the activity with CTP, GTP or UTP is 6, 11, and 3% of the activity with ATP, respectively.
The 1,2-propanediol (1,2-PD)-specific bacterial microcompartment (BMC) concentrates low levels of 1,2-PD catabolic enzymes, concentrates volatile reaction intermediates thus enhancing pathway flux and keeps the level of toxic, mutagenic propionaldehyde low. This gene probably benefits from its induction via the Pdu promoter, rather than a physical interaction with the BMC.
The BMC operon and BMC production is induced by growth on 1,2-PD vitamin B12 medium.
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.
Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Belongs to the anthranilate synthase component I family.
Cooperatively feedback inhibited by tryptophan.
Homodimer. In fact, exists in a monomer-dimer equilibrium in solution, shifted spontaneously in favor of the dimer; the monomer has a reduced activity compared with the dimer. Heterotetramer consisting of two non-identical subunits: a beta subunit (TrpG) and a large alpha subunit (TrpE) (Potential).
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.
Allosterically activated by AMP and by several sugar phosphates. Belongs to type II PK.
Catalyzes the formation of pyruvate in the last step of glycolysis, it is irreversible under physiological conditions. The reaction is critical for the control of metabolic flux in the second part of glycolysis.
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.
Homodimer. Heterotetramer of two MnmE and two MnmG subunits.
Belongs to the pseudouridine synthase RluA family.
Dual specificity enzyme that catalyzes the synthesis of pseudouridine from uracil-746 in 23S ribosomal RNA and from uracil-32 in the anticodon stem and loop of transfer RNAs.
Belongs to the MSOX/MTOX family. MTOX subfamily.
Catalyzes the oxidative demethylation of N-methyl-L-tryptophan.
Belongs to the methyltransferase superfamily. RsmH family.
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Belongs to the histidine acid phosphatase family.
Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family. RlmB subfamily.
Specifically methylates the ribose of guanosine 2251 in 23S rRNA.
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. Attractants increase the level of methylation while repellents decrease the level of methylation, the methyl groups are added by the methyltransferase CheR and removed by the methylesterase CheB.
Receptor for the attractant L-aspartate and related amino and dicarboxylic acids. Tar mediates taxis away from the repellents cobalt and nickel. Unlike in E.coli tar, it does not mediates maltose taxis.
Belongs to the CcmH/CycL/Ccl2/NrfF family.
Belongs to the IS200/IS605 insertion sequence (IS) element family.
Transposase responsible for transposition of the IS200 insertion sequence (IS) element. Transposition occurs in 2 main steps, excision from the donor DNA 'top strand' into a single strand circle and its subsequent reinsertion into the DNA target. This increases the copy number of the IS.
Belongs to the thiolase-like superfamily. Thiolase family.
Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed.
Heterotetramer of two alpha chains (FadJ) and two beta chains (FadI).
Tetramer of two alpha and two beta chains.
The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Belongs to the binding-protein-dependent transport system permease family.
Belongs to the acetate uptake transporter (AceTr) (TC 2.A.96) family.
Required for flagellar hook formation. May act as a scaffolding protein.
Belongs to the iron-sulfur dependent L-serine dehydratase family.
Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation.
The PPIase activity resides only in the second parvulin domain. The N-terminal region and the C-terminal tail are necessary and sufficient for the chaperone activity of SurA. The PPIase activity is dispensable for SurA to function as a chaperone. The N-terminal region and the C-terminal tail are also required for porin recognition.
Belongs to the bacterial sugar transferase family.
Is responsible for transferring galactose-1-phosphate to the lipid precursor undecaprenol phosphate in the first steps of O-polysaccharide biosynthesis.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. CysN/NodQ subfamily.
Heterodimer composed of CysD, the smaller subunit, and CysN.
With CysD forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD.
A type III restriction enzyme that recognizes 2 inversely oriented double-stranded sequences 5'-CAGAG-3' and cleaves DNA 25-27 base pairs downstream. After binding to one recognition site undergoes random one-dimensional diffusion along DNA until it collides with a stationary enzyme bound to the second DNA site, which is when DNA cleavage occurs. DNA restriction requires both the Res and Mod subunits.
Belongs to the type III restriction-modification system Res protein family.
Contains two different subunits: Res and Mod.
Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.
Acetylation of Ser-2 converts L12 to L7.
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 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.
Belongs to the dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family.
Responsible for the transport of dicarboxylates such as succinate, fumarate, and malate from the periplasm across the inner membrane.
Belongs to the class II fructose-bisphosphate aldolase family. TagBP aldolase GatY subfamily.
Catalytic subunit of the tagatose-1,6-bisphosphate aldolase GatYZ, which catalyzes the reversible aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to produce tagatose 1,6-bisphosphate (TBP). Requires GatZ subunit for full activity and stability. Is involved in the catabolism of galactitol.
BMC production is induced by growth on 1,2-PD vitamin B12 medium.
Bacterial microcompartments (BMC) 100-200 nm in cross section are formed during aerobic growth on minimal 1,2-PD-B12 or anaerobic growth on 1,2-PD-tetrathionate medium, but not during aerobic growth on glucose, anerobic growth on glucose or pyruvate-tetrathionate (PubMed:10498708). BMCs can constitute up to 10% of total cell protein (PubMed:12923081).
Evolutionarily distinct from Pta (phosphate acetyltransferase).
Involved in 1,2-propanediol (1,2-PD) utilization in the bacterial microcompartment (BMC) dedicated to 1,2-PD degradation by catalyzing the conversion of propanoyl-CoA to propanoyl-phosphate. Also able to catalyze the reverse reaction. Also has phosphate acetyltransferase activity to a lesser extent (PubMed:17158662). Required for optimal growth on 1,2-PD when the BMC is intact. CoA is regenerated within the BMC (for use by PduP) via this enzyme, although there must also be cofactor transport across the BMC. Directly targeted to the BMC (PubMed:25962918).
Monomer, when purified in the absence of the encapsulation peptide (EP, residues 1-27). The EP may influence oligomerization.
The 1,2-PD-specific bacterial microcompartment (BMC) concentrates low levels of 1,2-PD catabolic enzymes, concentrates volatile reaction intermediates thus enhancing pathway flux and keeps the level of toxic, mutagenic propionaldehyde low.
The N-terminal 20 residues target foreign proteins (tested with eGFP) to the BMC (PubMed:25962918). Formed by 2 beta-barrels, each is capped on both ends by short alpha-helices (By similarity).
There are 2 Zn(2+) ions per monomer; Zn(2+) and CoA bind inbetween the 2 domains in each monomer.
Unable to ferment 1,2-PD, impaired for aerobic growth on this compound.
It contains a N-terminal DNA binding region and a C-terminal metal binding region.
Loss of copper-based induction of copA. Causes a mild defect in aerobic growth on CuSO(4), strongly impairs survival during anaerobic growth on CuSO(4).
Regulates the transcription of the copA and cuiD (cueO) genes. Detects cytoplasmic copper stress and activates transcription in response to increasing copper concentrations (PubMed:17768242).
Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.
Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
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.
Belongs to the Gram-negative porin family.
Forms pores that allow passive diffusion of small molecules across the outer membrane. It is also a receptor for the bacteriophage T2 (By similarity).
Belongs to the acyltransferase 3 family.
Responsible for the incorporation of O-acetyl groups into the enterobacterial common antigen (ECA) trisaccharide repeat units.
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily.
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.
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 ketopantoate reductase family.
Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid. Has a strong preference for NADPH over NADH as the electron acceptor. Pantoate, ketoisovalerate, oxaloacetate, pyruvate, 3-hydroxypyruvate, alpha-ketoglutarate, alpha-ketobutyrate, and acetaldehyde cannot serve as substrates for reduction.
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 (PubMed:235429). Acts on 6-amino and 6-oxopurines including deoxyinosine, deoxyguanosine, deoxyadenosine, adenosine, guanosine, and inosine (PubMed:235429).
Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward HscA.
Interacts with HscA and stimulates its ATPase activity. Interacts with IscU.
Curlin is the structural subunit of the curli. Curli are coiled surface structures that assemble preferentially at growth temperatures below 37 degrees Celsius. Curli can bind to fibronectin. The minor subunit is the nucleation component of curlin monomers.
DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM.
Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by oxidizing the DsbA protein (By similarity).
Contains various tandem pentapeptide repeats in the C-terminal region. The pentapeptide motif is required to efficiently recruit kinesin-1. No position is completely conserved in these repeats, whose consensus sequence is A-[DN]-[FLM]-X-X. The C-terminal 38 amino acid residues, specifically, the C-terminal motif LFNEF, are required for peripheral localization of PipB2 and redistribution of lysosomal-associated membrane protein (LAMP). The N-terminal 225 amino acid residues are sufficient for type III translocation and association with Sifs and SCVs, but not accumulation in peripheral vesicles.
Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. Involved in the reorganization of late endosome/lysosome (LE/Lys) compartments in mammalian cells. Necessary and sufficient to link kinesin-1 onto the Salmonella-containing vacuole (SCV) membrane. Required for centrifugal extension of lysosomal glycoprotein-rich membrane tubules, known as Salmonella-induced filaments (Sifs), away from the SCV and toward the cell periphery. Required for virulence, but not for intracellular survival and replication in phagocytic cells.
Expression of the gene is regulated by the two-component regulatory system SsrA/SsrB. It is also activated by SlyA and controlled by the two-component regulatory system PhoP/PhoQ.
Interacts with the host kinesin light chain (KLC), a subunit of the kinesin-1 motor complex.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family. TrmA subfamily.
Catalyzes the formation of 5-methyl-uridine at position 54 (m5U54) in all tRNAs.
Dual-specificity methyltransferase that catalyzes the formation of 5-methyluridine at position 54 (m5U54) in all tRNAs, and that of position 341 (m5U341) in tmRNA (transfer-mRNA).
Growth rate-dependent regulation of transcription. Is a novel example of a mRNA regulated through a mechanism similar to that of a stable RNA (rRNA).
Belongs to the multi antimicrobial extrusion (MATE) (TC 2.A.66.1) family. MdtK subfamily.
Multidrug efflux pump that functions probably as a Na(+)/drug antiporter.
Binds 1 K(+) per subunit. The potassium ion strongly increases the affinity for DNA.
Binds 2 Mg(2+) per subunit. Only one magnesium ion has a direct interaction with the protein, the other interactions are indirect.
Has flap endonuclease activity. During DNA replication, flap endonucleases cleave the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment.
Belongs to the DnaA family. HdA subfamily.
Mediates the interaction of DNA replication initiator protein DnaA with DNA polymerase subunit beta sliding clamp (dnaN). Stimulates hydrolysis of ATP-DnaA to ADP-DnaA, rendering DnaA inactive for reinitiation, a process called regulatory inhibition of DnaA or RIDA (By similarity).
The active form seems to be an ADP-bound monomer. Forms the RIDA complex (regulatory inactivation of DnaA) of ATP-DnaA, ADP-Hda and the DNA-loaded beta sliding clamp (dnaN).
Belongs to the transposase mutator family.
Required for the transposition of the insertion element.
Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family.
Belongs to the binding-protein-dependent transport system permease family. HisMQ subfamily.
Belongs to the peptidase S12 family. YfeW subfamily.
Belongs to the DEAD box helicase family. RhlB subfamily.
Component of the RNA degradosome, which is a multiprotein complex involved in RNA processing and mRNA degradation.
DEAD-box RNA helicase involved in RNA degradation. Has RNA-dependent ATPase activity and unwinds double-stranded RNA.
Mediates coordination of peptidoglycan synthesis and outer membrane constriction during cell division.
Belongs to the membrane fusion protein (MFP) (TC 8.A.1) family.
Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane.
Was originally (PubMed:2680969) thought to be involved in mouse virulence. It was later shown that the mutation responsible for the virulence phenotype maps to nearby genes (PubMed:8288531).
Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.
Cells lacking this gene display a strong clockwise motor bias; in combination with a yhjH disruption and overexpression of ycgR, cells switch from clockwise to a counterclockwise bias.
Homodimer. Interacts (via C-terminus) with phosphorylated CheY (CheY-P).
Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P). Acts on free CheY-P.
Activates the transcription of the eut operon, allowing utilization of ethanolamine (EA). Positively regulates its own transcription (Probable) (PubMed:1328159, PubMed:8113167). Probably binds EA and vitamin B12 as effectors (Probable). Competes with ethanolamine ammonia-lysase (EAL, the first enzyme in the EA degradation pathway) for adenosylcobalamin (PubMed:8113167). Ethanolamine-associated signaling mediated via this protein, but not EA degradation, impacts S.typhimurium survival within macrophages. Binds the promoter of ssrB and eutS in vitro; in mouse infection models binding to ssrB probably induces all 4 operons of pathogenicity island SPI-2 (PubMed:26565973).
Expression of the eut operon allows this bacteria to use ethanolamine (EA) as a carbon, nitrogen and energy source. It relies on cobalamin (vitamin B12) both as a cofactor for the ethanolamine ammonia-lyase (EAL) activity and to induce the operon (PubMed:3045078). EA enhances bacterial survival in macrophages in a concentration-dependent manner, suggesting it is an important nutrient in infection (PubMed:29531136).
Mutations prevent expression of the entire eut operon (PubMed:2656649). No phenotype during bacterial growth in vitro. About 10-fold outcompeted by wild-type in mouse intestines at 2 and 4 days following oral infection. Loss of induction of pathogenicity island SPI-2 in mouse macrophages (PubMed:26684793). About 25% reduction in survival in mouse macrophage assays. Bacteria growth is not enhanced by exogenous EA in macrophage survival assays (PubMed:29531136).
Part of the 17-gene eut operon transcribed from a single promoter, positively regulates its own expression, induced by ethanolamine and adenosylcobalamin (AdoCbl, vitamin B12). This is the last gene in the operon and has a second weaker promoter that is constitutively transcribed at a low level (PubMed:10464203, PubMed:3045078, PubMed:1328159, PubMed:26565973) (Probable). Subject to catabolite repression; expression is substantially lower during growth on glucose than during growth versus succinate. Catabolite repression is overcome by adding exogenous cAMP to the glucose growth media (PubMed:1328159). Induced after phagocytosis by mouse RAW macrophages and in spleen in mouse infection; the whole eut operon is not induced (PubMed:26565973).
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).
Belongs to the bacterial ribosomal protein bL31 family. Type A subfamily.
Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit family.
Heterodimer of a large and a small subunit.
Belongs to the universal ribosomal protein uL5 family.
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 binds and probably mediates 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.
Reduction of a variety of nitroaromatic compounds using NADH (and to lesser extent NADPH) as source of reducing equivalents; two electrons are transferred. Capable of reducing nitrofurazone (By similarity).
Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH.
Belongs to the bacterial ribosomal protein bL35 family.
By heat shock under the control of the HtpR regulatory protein.
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 (By similarity). Necessary for invasion of epithelial cells, secretion of invasion proteins and proliferation within macrophages.
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.
Belongs to the N-acylglucosamine 2-epimerase family.
Catalyzes the isomerization of sulfoquinovose (SQ) to 6-deoxy-6-sulfo-D-fructose (SF) (By similarity). In vitro, can also catalyze the interconversion of mannose, fructose and glucose, but has extremely low activity with glucose (PubMed:18328504).
Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
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.
Belongs to the carbamoyltransferase HypF family.
Involved in the maturation of [NiFe] hydrogenases. Along with HypE, it catalyzes the synthesis of the CN ligands of the active site iron of [NiFe]-hydrogenases. HypF functions as a carbamoyl transferase using carbamoylphosphate as a substrate and transferring the carboxamido moiety in an ATP-dependent reaction to the thiolate of the C-terminal cysteine of HypE yielding a protein-S-carboxamide.
Negatively controls the expression of the four operons of arginine biosynthesis in addition to the carAB operon. Predominantly interacts with A/T residues in ARG boxes.
A quadruple eutP-eutQ-eutT-eutD deletion is not impaired for aerobic growth on ethanolamine (EA) supplemented with cobalamin (vitamin B12) (PubMed:10464203). Can grow on EA as sole carbon source when AdoB12 is supplied; double cobA-eutT mutants do not grow with CN-B12 as a nitrogen source (PubMed:15516577). A non-polar deletion mutant grows on EA from pH 5.5 to pH 8.0, but does not grow at pH 8.5, no change in acetaldehyde release on EA plus vitamin B12 (PubMed:16585748).
Belongs to the Cob(I)alamin adenosyltransferase family. EutT subfamily.
Binds 1 divalent metal cation ion per homodimer with both subunits providing Cys ligands; Fe(2+) gives most activity and is possibly the physiological cofactor, followed by Zn(2+) and Co(2+) (PubMed:24336938, PubMed:28045498). Activity stimulated by Mn(2+) (PubMed:16636051).
Converts cyanocobalamin (CN-B12) to adenosylcobalamin (AdoCbl), the inducer of the eut operon (PubMed:15516577, PubMed:16636051, PubMed:24336938). Is not active on cobinamide nor other intermediates in the adenosylcobalamin synthetic pathway. Allows full induction of the eut operon (PubMed:15516577). Can use ADP, CTP and dATP in place of ATP, and cobinamide in place of cobalamin, none are as efficiently used as ATP and cobalamin (PubMed:16636051).
Expression of the eut operon allows this bacteria to use ethanolamine (EA) as a carbon, nitrogen and energy source. It relies on cobalamin (vitamin B12) both as a cofactor for the ethanolamine ammonia-lyase (EAL) activity and to induce the operon (PubMed:3045078). EA enhances bacterial survival in macrophages in a concentration-dependent manner, suggesting it is an important nutrient during infection (PubMed:29531136).
Electron transfer subunit of the terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds.
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.
Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
Belongs to the phosphoribulokinase family.
Belongs to the glucose-6-phosphate 1-epimerase family.
Probably functions as a hexose-6-phosphate 1-epimerase.
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 Nudix hydrolase family. NudC subfamily.
Divalent metal cations. Mg(2+) or Mn(2+).
mRNA decapping enzyme that specifically removes the nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by hydrolyzing the diphosphate linkage to produce nicotinamide mononucleotide (NMN) and 5' monophosphate mRNA. The NAD-cap is present at the 5'-end of some mRNAs and stabilizes RNA against 5'-processing. Has preference for mRNAs with a 5'-end purine. Catalyzes the hydrolysis of a broad range of dinucleotide pyrophosphates.
Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
Tetramer of two alpha and two beta subunits.
Positive regulator essential for the expression of allD operon. Binds to the allD promoter (By similarity).
Required for induction of expression of the formate dehydrogenase H and hydrogenase-3 structural genes.
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.
Belongs to the carbohydrate kinase pfkB family.
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.
Lacks conserved residue(s) required for the propagation of feature annotation.
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.
Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Belongs to the TonB-dependent receptor family.
Belongs to the phosphohexose mutase family.
Belongs to the glycerate kinase type-1 family.
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.
Belongs to the amino acid-polyamine-organocation (APC) superfamily. Basic amino acid/polyamine antiporter (APA) (TC 2.A.3.2) family.
Each subunit has 12 transmembrane (TM) helices; TM1 and TM6 are interrupted by short non-helical Gly-rich loops in the middle of their transmembrane spans. TM11 and TM12 provide most of the homodimerization interface. Each subunit has a central cavity which probably binds substrate.
Homodimer; each subunit has its own individual transport capacity.
Major component of the acid-resistance (AR) system allowing enteric pathogens to survive the acidic environment in the stomach (Probable). Exchanges extracellular arginine for its intracellular decarboxylation product agmatine (Agm) thereby expelling intracellular protons (PubMed:19578361). Probably undergoes several conformational states in order to translocate the substrate across the membrane; keeps the substrate accessible to only 1 side of the membrane at a time by opening and closing 3 membrane-internal gates (By similarity).
Maximum induction requires anaerobiosis, acidic conditions and tyrosine.
Belongs to the 'phage' integrase family. XerC subfamily.
Forms a cyclic heterotetrameric complex composed of two molecules of XerC and two molecules of XerD, in which XerC interacts with XerD via its C-terminal region, XerD interacts with XerC via its C-terminal region and so on.
FtsK may regulate the catalytic switch between XerC and XerD in the heterotetrameric complex during the two steps of the recombination process.
Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. Binds cooperatively to specific DNA consensus sequences that are separated from XerD binding sites by a short central region, forming the heterotetrameric XerC-XerD complex that recombines DNA substrates. The 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. In the complex XerC specifically exchanges the top DNA strands.
Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
Belongs to the major facilitator superfamily. Proton-dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family. DtpD subfamily.
Probable proton-dependent permease that transports dipeptides.
Belongs to the amino acid-polyamine-organocation (APC) superfamily.
Probable amino-acid or metabolite transport protein.
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.
Belongs to the ABC-3 integral membrane protein family.
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.
Belongs to the monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family.
Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
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).
Interacts with the TusBCD complex. Interacts with MnmA (By similarity).
Part of a sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions. Could accept sulfur from TusD (By similarity).
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 helicase family. DnaB subfamily.
Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with DnaC protein, primase, and other prepriming proteins.
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).
Belongs to the sigma-70 factor family. RpoS subfamily.
Interacts with the RNA polymerase core enzyme.
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 master transcriptional regulator of the stationary phase and the general stress response.
Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
Belongs to the SNF2/RAD54 helicase family. RapA subfamily.
Interacts with the RNAP. Has a higher affinity for the core RNAP than for the holoenzyme. Its ATPase activity is stimulated by binding to RNAP.
Transcription regulator that activates transcription by stimulating RNA polymerase (RNAP) recycling in case of stress conditions such as supercoiled DNA or high salt concentrations. Probably acts by releasing the RNAP, when it is trapped or immobilized on tightly supercoiled DNA. Does not activate transcription on linear DNA. Probably not involved in DNA repair.
Belongs to the IUNH family. RihC subfamily.
Hydrolyzes both purine and pyrimidine ribonucleosides with a broad-substrate specificity.
Catalyzes the decarboxylation of oxaloacetate coupled to Na(+) translocation.
Composed of three chains (alpha, beta, and gamma).
Belongs to the ATP phosphoribosyltransferase family. Long 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).
Equilibrium between an active dimeric form, an inactive hexameric form and higher aggregates. Interconversion between the various forms is largely reversible and is influenced by the natural substrates and inhibitors of the enzyme (Probable).
Feedback inhibited by histidine. Also inhibited by AMP and ADP.
Repressed by ppGpp in the presence of histidine.
Belongs to the porin LamB (TC 1.B.3) family.
Homotrimer formed of three 18-stranded antiparallel beta-barrels, containing three independent channels.
Involved in the transport of maltose and maltodextrins. Does not act as a receptor for phages.
Covalent carrier of the coenzyme of citrate lyase.
Oligomer with a subunit composition of (alpha,beta,gamma)6.
Belongs to the TRAP transporter large permease family.
Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
The complex comprises the extracytoplasmic solute receptor protein and the two transmembrane proteins.
Belongs to the NAD(P)H dehydrogenase (quinone) family. KefF subfamily.
Regulatory subunit of a potassium efflux system that confers protection against electrophiles. Required for full activity of KefC. Shows redox enzymatic activity, but this enzymatic activity is not required for activation of KefC.
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.
Binds between the large and small subunits.
Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds (Probable). It is spontaneously inactivated by its substrate and reactivated by EutA (By similarity). May play a role in BMC assembly or maintenance (Probable).
Expression of the eut operon allows this bacteria to use ethanolamine (EA) as a carbon, nitrogen and energy source. It relies on cobalamin (vitamin B12) both as a cofactor for the ethanolamine ammonia-lyase activity and to induce the operon. EA enhances bacterial survival in macrophages in a concentration-dependent manner, suggesting it is an important nutrient during infection (PubMed:29531136).
No aerobic growth on ethanolamine (EA) supplemented with cobalamin (vitamin B12) (PubMed:10464203, PubMed:2656649). No phenotype during growth in vitro. Decreased expression of eutR during bacterial growth in vitro. About 10-fold outcompeted by wild-type in mouse intestine at 2 and 4 days following oral infection, but no effect seen during growth in peritoneal exudate macrophages (PubMed:26565973). A non-polar deletion mutant does not grow on EA between pH 5.5 and pH 8.5, stops acetaldehyde release on EA plus vitamin B12 (PubMed:16585748). A deletion allows growth on acetate, suggesting BMC assembly or maintenance is impaired (PubMed:23585538).
The basic unit is a heterodimer which dimerizes to form tetramers. The heterotetramers trimerize; 6 large subunits form a core ring with 6 small subunits projecting outwards.
Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
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.
Belongs to the organic radical-activating enzymes family.
Member of the two-component regulatory system PgtB/PgtA that regulates the inducible phosphoglycerate transport system. When activated by PgtB it acts in conjunction with sigma-54 as a transcriptional activator.
Belongs to the nucleoside-specific channel-forming outer membrane porin (Tsx) (TC 1.B.10) family.
Heterotrimer of an alpha, a beta and a gamma subunit.
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 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.
Belongs to the drug/metabolite transporter (DMT) superfamily. 10 TMS drug/metabolite exporter (DME) (TC 2.A.7.3) family.
Belongs to the globin family. Two-domain flavohemoproteins subfamily.
Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
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.
Belongs to the transcriptional regulatory CopG/NikR family.
Transcriptional repressor of the nikABCDE operon. Is active in the presence of excessive concentrations of intracellular nickel.
Bifunctional enzyme that catalyzes two sequential steps of tryptophan biosynthetic pathway. The first reaction is catalyzed by the isomerase, coded by the TrpF domain; the second reaction is catalyzed by the synthase, coded by the TrpC domain (By similarity).
In the C-terminal section; belongs to the TrpF family.
In the N-terminal section; belongs to the TrpC family.
Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein.
Was originally thought to be involved in delta-aminolevulinic acid biosynthesis.
Represses ulaG and the ulaABCDEF operon.
Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family. MdtB subfamily.
Part of a tripartite efflux system composed of MdtA, MdtB and MdtC. MdtB forms a heteromultimer with MdtC.
Binds 1 nickel ion per subunit. In the homodimer, two nickel ions are bound between subunits.
Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
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).
Part of the 30S ribosomal subunit. Contacts proteins S8 and S17. May interact with IF1 in the 30S initiation complex (By similarity).
With S4 and S5 plays an important role in translational accuracy.
Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.
Decarboxylates L-threonine-O-3-phosphate to yield (R)-1-amino-2-propanol O-2-phosphate, the precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin.
Belongs to the thioredoxin family. DsbA subfamily.
Belongs to the thioredoxin family. DsbL subfamily.
Involved in disulfide-bond formation. Acts by transferring its disulfide bond to other proteins. Part of a redox system composed of DsbI and DsbL that mediates formation of an essential disulfide bond in AssT.
An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Probably interacts with S19. 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 S19.
Belongs to the transglycosylase MltG family.
Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
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.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family.
Specifically methylates the cytosine at position 1407 (m5C1407) of 16S rRNA.
Belongs to the acyl-CoA dehydrogenase family.
Catalyzes the dehydrogenation of acyl-coenzymes A (acyl-CoAs) to 2-enoyl-CoAs, the first step of the beta-oxidation cycle of fatty acid degradation. Is required for S.typhimurium to utilize medium- and long-chain fatty acids as sole carbon sources for growth. Is needed for bacterial survival during carbone-source starvation.
Cells lacking this gene show undetectable in vivo beta-oxidation levels, and are unable to grow on oleate or decanoate as a sole carbon and energy source, in contrast to the wild-type parent strain.
Is under the negative control of the global regulator FadR and the positive control of the cAMP:cAMP receptor protein (cAMP:CRP) as well as the alarmone ppGpp. Is induced under carbon-source starvation and in the presence of the long-chain fatty acid oleate. Induction during carbon starvation is cAMP:CRP-dependent and sigma(S)-independent.
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 pyrimidines, such as thymine glycol, 5,6-dihydrouracil and 5,6-dihydrothymine. 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.
Belongs to the TRAFAC class YlqF/YawG GTPase family. RsgA subfamily.
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.
Belongs to the monovalent cation:proton antiporter 2 (CPA2) transporter (TC 2.A.37) family.
Belongs to the ABC transporter superfamily. AI-2 autoinducer porter (TC 3.A.1.2.8) family.
In the absence of AI-2, repressed by LsrR. Induced by AI-2, via release of the LsrR repressor.
Part of the ABC transporter complex LsrABCD involved in autoinducer 2 (AI-2) import. Responsible for energy coupling to the transport system.
The complex is composed of two ATP-binding proteins (LsrA), two transmembrane proteins (LsrC and LsrD) and a solute-binding protein (LsrB).
Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding.
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
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-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Inhibited by EDTA, mercuric salts and by leucine. Inhibition by leucine is non-competitive with respect to 3-methyl-2-oxobutanoate and competitive with respect to acetyl-CoA, and is more sensitive at pH 6.5 than pH 8.5.
Exonuclease involved in the 3' processing of various precursor tRNAs. Initiates hydrolysis at the 3'-terminus of an RNA molecule and releases 5'-mononucleotides.
May form homooligomers. Probably interacts with the periplasmic domain of PhoQ.
PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing. MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway. Represses PhoP/PhoQ signaling, possibly by binding to the periplasmic domain of PhoQ, altering its activity and that of downstream effector PhoP.
Member of the two-component regulatory system BasS/BasR. Autophosphorylates and activates BasR by phosphorylation. Plays a role in the adaptation of the organism to the host environment, in particular to neutrophils, and therefore it plays a role in virulence as well.
The eptA-basRS operon is positively autoregulated by BasR under high iron or aluminum concentration conditions.
Belongs to the oligogalacturonate-specific porin KdgM (TC 1.B.35) family. OmpL subfamily.
Outer membrane channel protein that allows an efficient diffusion of low-molecular-weight solutes such as small sugars and tetraglycine. However, the specific substrate recognized by the OmpL channel is unknown (By similarity).
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 binding-protein-dependent transport system permease family. AraH/RbsC subfamily.
Part of the ABC transporter complex MglABC involved in galactose/methyl galactoside import. Probably responsible for the translocation of the substrate across the membrane.
The complex is composed of one ATP-binding protein (MglA), two transmembrane proteins (MglC) and a solute-binding protein (MglB).
May be involved in cell division. May play a role in bacterial septation or regulation of cell wall degradation during cell division (By similarity).
Belongs to the DEAD box helicase family. DeaD/CsdA subfamily.
DEAD-box RNA helicase involved in various cellular processes at low temperature, including ribosome biogenesis, mRNA degradation and translation initiation.
Belongs to the tRNA methyltransferase O family.
Belongs to the ner transcriptional regulatory family.
Belongs to the GHMP kinase family. Homoserine kinase subfamily.
Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Involved in copper resistance. Appears to be involved in copper uptake.
Belongs to the phosphopentomutase family.
Phosphotransfer between the C1 and C5 carbon atoms of pentose.
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. Contacts proteins S5 and S12 (By similarity).
Belongs to the glycosyl hydrolase 37 family.
Hydrolyzes trehalose to glucose. Could be involved, in cells returning to low osmolarity conditions, in the utilization of the accumulated cytoplasmic trehalose, which was synthesized in response to high osmolarity.
Belongs to the SAICAR synthetase family.
Belongs to the shikimate dehydrogenase family.
The actual biological function of YdiB remains unclear, nor is it known whether 3-dehydroshikimate or quinate represents the natural substrate. Catalyzes the reversible NAD-dependent reduction of both 3-dehydroshikimate (DHSA) and 3-dehydroquinate to yield shikimate (SA) and quinate, respectively. It can use both NAD or NADP for catalysis, however it has higher catalytic efficiency with NAD.
Belongs to the complex I subunit 4 family.
Composed of 13 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex.
The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB.
Belongs to the bacterial ribosomal protein bL17 family.
Part of the 50S ribosomal subunit. Contacts protein L32.
Belongs to the Mrp/NBP35 ATP-binding proteins family.
Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins (PubMed:18616280, PubMed:19001370). Can hydrolyze ATP (PubMed:12486045, PubMed:19001370). Both activities are required for function in vivo, but the ability to hydrolyze ATP is not necessary for Fe-S cluster transfer (PubMed:19001370).
Homodimer. Holo-ApbC forms a mixture of homodimers and homotetramers.
Mutants are impaired in Fe-S cluster metabolism. They are conditional thiamine auxotrophs and have lower aconitase and succinate dehydrogenase activities.
Belongs to the gluconokinase GntK/GntV family.
Belongs to the pyridoxamine 5'-phosphate oxidase family.
Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Belongs to the binding-protein-dependent transport system permease family. UgpAE subfamily.
Part of the ABC transporter complex UgpBAEC involved in sn-glycerol-3-phosphate (G3P) import. Probably responsible for the translocation of the substrate across the membrane.
The complex is composed of two ATP-binding proteins (UgpC), two transmembrane proteins (UgpA and UgpE) and a solute-binding protein (UgpB).
Activated under anaerobic conditions by NrdG, a tightly associated activase. Activation involves the formation of a glycyl radical at Gly-681.
Belongs to the anaerobic ribonucleoside-triphosphate reductase family.
Catalyzes the conversion of ribonucleotides into deoxyribonucleotides, which are required for DNA synthesis and repair.
Forms a tetramer composed of two NrdD and two NrdG subunits.
Citrate synthase is found in nearly all cells capable of oxidative metabolism.
Belongs to the succinate/malate CoA ligase alpha subunit family.
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 alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.
Belongs to the CoA-transferase III family. CaiB subfamily.
Catalyzes the reversible transfer of the CoA moiety from gamma-butyrobetainyl-CoA to L-carnitine to generate L-carnitinyl-CoA and gamma-butyrobetaine. Is also able to catalyze the reversible transfer of the CoA moiety from gamma-butyrobetainyl-CoA or L-carnitinyl-CoA to crotonobetaine to generate crotonobetainyl-CoA (By similarity).
Binds 2 Mn(2+) ions per subunit in a binuclear metal center.
Hydrolyzes the pyrophosphate bond of UDP-2,3-diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Involved in DNA repair and RecF pathway recombination.
Belongs to the major facilitator superfamily. Bcr/CmlA family.
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.
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 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.
Produces ATP from ADP in the presence of a proton gradient across the membrane.
May be involved in the biosynthesis of molybdopterin.
Belongs to the myoviridae tail sheath protein family.
Belongs to the NAD(P)-dependent epimerase/dehydratase family. GDP-mannose 4,6-dehydratase subfamily.
Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6-deoxy-D-mannose.
Controls the length of the flagellar hook.
Two-domain protein with the central portion of the sequence acting as a hinge or connector between the two.
Interacts with PduU, probably via the PduU beta-barrel which is predicted by modeling to be on the exterior of the BMC.
May play a role in the spatial distribution of the bacterial microcompartment (BMC) dedicated to 1,2-PD degradation, perhaps being involved in cytoskeleton dynamics. This subunit is directly targeted to the BMC (By similarity). Might bind GTP (Probable).
The 1,2-propanediol (1,2-PD) degradation bacterial microcompartment (BMC) concentrates low levels of 1,2-PD catabolic enzymes, concentrates volatile reaction intermediates thus enhancing pathway flux and keeps the level of toxic, mutagenic propionaldehyde low.
Transcriptional repressor for the pyruvate dehydrogenase complex genes aceEF and lpd.
Belongs to the PEP-utilizing enzyme family.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
During stationary phase, binds the chromosome non-specifically, forming a highly ordered and stable dps-DNA co-crystal within which chromosomal DNA is condensed and protected from diverse damages. It protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral, which can be released after reduction. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton reaction.
Homododecamer. The 12 subunits form a hollow sphere into which the mineral iron core of up to 500 Fe(3+) can be deposited.
Belongs to the DcuA/DcuB transporter (TC 2.A.13.1) family.
Responsible for the transport of C4-dicarboxylates.
Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family.
Artificial BMCs can be made in E.coli by expressing eutK, eutL, eutM, eutN, eutS (eutSMNLK) or eutS alone. Cargo proteins can be targeted to them and beta-galactosidase (lacZ) was active within the BMC, showing the BMC allows passage of substrate into the interior. This can lead to the development of tailored BMCs for specific metabolic reactions (PubMed:22428024, PubMed:27063436). The addition of eutQ to the eutSMNLK construct results in biogenesis of multiple BMCs (PubMed:27063436). Can incorporate into the pdu BMC where it alters growth, suggesting fine-tuning metabolite flux by using different BMC components is possible (PubMed:28585808).
Belongs to the bacterial microcompartments protein family.
Can be used as a self-assembling protein scaffold for synthetic biology. Overexpressed, purified protein with a SpyCatcher tag added to the C-terminus yields self-assembling fibrils that are stable at pH 5-9 and up to 50 degrees Celsius. Addition of SpyTagged cargo proteins leads to isopeptide bond formation between the scaffold and cargo proteins, colocalizing and stabilizing the cargo proteins and reducing the time for the reaction to make maximimal product.
Essential, it cannot be deleted when the 17-gene operon is otherwise intact, possibly due to polar effects on downstream genes (PubMed:7868611). Not required for cobalamin-dependent degradation of ethanolamine (EA) when polar effects are removed. A double eutD-eutM deletion is also not required for growth in the above conditions (PubMed:10464203). A double eutM-eutN strain grows as well as wild-type on EA and cyanocobalamin, but a quadruple eutL-eutK eutM-eutN strain does not grow (PubMed:16291677). A non-polar deletion mutant grows on EA at pH 5.5 to pH 7.0 but not at pH 8.0 or pH 8.5, releases increased amounts of acetaldehyde on EA plus vitamin B12. Preventing acetaldehyde vapor loss allows growth up to pH 8.5 (PubMed:16585748).
Homohexamer with a central pore of up to 8.6 Angstroms diameter. The hexamers pack into a two-dimensional array (By similarity). Interacts with EutQ; a probably cytoplasm-facing helix (Val-49 to Gln-64) interacts with N-terminus of EutQ (PubMed:27063436).
Probably a major component of the bacterial microcompartment (BMC) shell dedicated to ethanolamine degradation (PubMed:22428024, PubMed:27063436). Each homohexamer has a central pore with an opening of up to 8.6 Angstroms. A positively-charged funnel leads to the pore from each side of the hexamer. The pore probably allows metabolite passage into and out of the BMC (By similarity). Expression of eutK, eutL, eutM, eutN, eutS (eutSMNLK) in E.coli leads to formation of a single BMC. Expression alone leads to thick filaments that interfere with cell separation (PubMed:22428024, PubMed:27063436). Coexpression of eutQ with eutSMNLK permits E.coli to make cells with more than one mobile BMC, as is usual in vivo. May play a role in BMC shell biogenesis (PubMed:27063436). Can replace homolog pduA in the pdu operon, cells grow better than wild-type on 1,2-propanediol and vitamin B12. Protein is incorporated into the pdu BMC microcompartment (PubMed:28585808).
Belongs to the dTDP-4-dehydrorhamnose 3,5-epimerase family.
Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.
Belongs to the N(4)-acetylcytidine amidohydrolase family.
Catalyzes the hydrolysis of N(4)-acetylcytidine (ac4C).
A CoA-acylating aldehyde dehydrogenase required for optimal 1,2-propanediol (1,2-PD) degradation (PubMed:14504694, PubMed:20308536). Optimizes growth in the bacterial microcompartment (BMC) dedicated to 1,2-PD degradation by minimizing propionaldehyde toxicity (Probable). Directly targeted to the BMC (PubMed:20308536, PubMed:22927404, PubMed:26283792). NAD(+) and NADH are regenerated internally within the Pdu BMC by the PduP and PduQ enzymes, which reduce NAD(+) and oxidize NADH respectively, although there must also be cofactor transport across the BMC (PubMed:23077559).
A short N-terminal, probably helical sequence targets this enzyme and foreign proteins (tested with GST, MBP and eGFP) to the BMC. 10 residues give poor localization while 14 is better and 18 is better yet. The cargo is only detected by Western blot in broken shells, strongly suggesting this protein is normally found inside the BMC and not on its exterior (PubMed:20308536, PubMed:22927404, PubMed:26283792). This N-terminal sequence interacts with the C-terminus of PduA, and possibly also with PduJ, to encapsulate PduP into BMCs (PubMed:22927404). PduD and PduP compete for encapsulation in BMCs (PubMed:26283792).
Interacts with BMC shell proteins PduA and PduJ, which target this protein to BMC (PubMed:22927404). Interacts with PduQ, probably via the N-terminus of PduQ (PubMed:23077559). Interacts with PduK, probably with its BMC-containing N-terminus (By similarity).
Significantly impaired for growth on 1,2-PD/CN-B12, loss of propionaldehyde dehydrogenase activity (PubMed:14504694). Releases decreased amounts of acetaldehyde when grown on propanediol (PubMed:16585748).
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.
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).
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).
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.
Belongs to the beta-class carbonic anhydrase family.
Belongs to the UDP-galactopyranose/dTDP-fucopyranose mutase family.
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 class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.
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.
Belongs to the type-B carboxylesterase/lipase 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).
Belongs to the alkylbase DNA glycosidase AlkA family.
Major determinant of cell surface composition. Negatively regulates motility, adhesion and synthesis of biofilm exopolysaccharides.
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 periplasmic pilus chaperone family.
Belongs to the major facilitator superfamily. Organophosphate:Pi antiporter (OPA) (TC 2.A.1.4) family.
Part of the UhpABC signaling cascade that controls the expression of the hexose phosphate transporter UhpT. UhpC senses external glucose-6-phosphate and interacts with the histidine kinase UhpB, leading to the stimulation of the autokinase activity of UhpB.
Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family.
Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA.
Catalyzes the ferrous insertion into protoporphyrin IX.
Composed of a rhodanese domain and a P-loop domain, which probably binds geranyl diphosphate. The two activities are mechanistically different, but the rhodanese domain is important for both.
Involved in the post-transcriptional modification of the uridine at the wobble position (U34) of tRNA(Lys), tRNA(Glu) and tRNA(Gln) (PubMed:27073879, PubMed:7520175). Catalyzes the conversion of 2-thiouridine (S2U-RNA) to 2-selenouridine (Se2U-RNA) (PubMed:7520175, PubMed:27073879). Acts in a two-step process involving geranylation of 2-thiouridine (S2U) to S-geranyl-2-thiouridine (geS2U) and subsequent selenation of the latter derivative to 2-selenouridine (Se2U) in the tRNA chain (Probable).
It was also suggested that 2-thiourine geranylation and 2-thiouridine selenation in the tRNA chain may occur independently, in two distinc metabolic processes.
Belongs to the aspartate/glutamate racemases family.
Provides the (R)-glutamate required for cell wall biosynthesis.
Belongs to the LRR-containing bacterial E3 ligase family.
Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway.
Exists in an autoinhibited state in the absence of substrate protein, due to interactions of the leucine-rich repeat domain with the catalytic domain. Is activated upon binding to a substrate protein.
The LRR (leucine-rich repeat) domain is involved in autoinhibition of the enzyme activity by interacting with the catalytic domain.
Ubiquitinated in the presence of host E1 ubiquitin-activating enzyme UBA1, E2 ubiquitin-conjugating enzyme UBE2D2 and ubiquitin.
Belongs to the helicase family. UvrD subfamily.
Rep helicase is a single-stranded DNA-dependent ATPase involved in DNA replication; it can initiate unwinding at a nick in the DNA. It binds to the single-stranded DNA and acts in a progressive fashion along the DNA in the 3' to 5' direction.
Part of the Bam complex, which is composed of the outer membrane protein BamA, and four lipoproteins BamB, BamC, BamD and BamE.
Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
Belongs to the trans-sulfuration enzymes family.
Catalyzes the cleavage of cystathionine to homocysteine, pyruvate and ammonia during methionine biosynthesis.
Electron transfer protein for anaerobic sulfite reductase subunit A.
The anaerobic sulfite reductase seems to consist of three subunits.
Belongs to the major facilitator superfamily. Nitrate/nitrite porter (TC 2.A.1.8) family.
Belongs to the acetyl-CoA hydrolase/transferase family.
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 (By similarity).
Binds 1 [4Fe-4S] cluster per subunit. The cluster is presumably bound at the interface of two monomers.
Involved in iron-sulfur cluster biogenesis. Binds a 4Fe-4S cluster, can transfer this cluster to apoproteins, and thereby intervenes in the maturation of Fe/S proteins. Could also act as a scaffold/chaperone for damaged Fe/S proteins.
Belongs to the precorrin methyltransferase family.
Methylates cobalt-precorrin-2 at the C-20 position to produce cobalt-precorrin-3A in the anaerobic cobalamin biosynthesis pathway.
Belongs to the sodium:galactoside symporter (TC 2.A.2) family.
Could be involved in the export of 2,3-dihydroxypropane-1-sulfonate (DHPS).
Belongs to the threonine aldolase family.
Belongs to the GppA/Ppx family. GppA subfamily.
Catalyzes the conversion of pppGpp to ppGpp. Guanosine pentaphosphate (pppGpp) is a cytoplasmic signaling molecule which together with ppGpp controls the 'stringent response', an adaptive process that allows bacteria to respond to amino acid starvation, resulting in the coordinated regulation of numerous cellular activities.
Belongs to the glutathione peroxidase family. BtuE subfamily.
Non-specific peroxidase that can use thioredoxin or glutathione as a reducing agent.
Belongs to the GST superfamily. HSP26 family.
Belongs to the cytochrome c oxidase bacterial subunit 4 family.
Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron.
Heterooctamer of two A chains, two B chains, two C chains and two D chains.
Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis. Essential for lipoprotein maturation under conditions where membrane fluidity may be altered.
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 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. Interacts with proteins S7 and S18. Binds to IF-3.
Belongs to the glycosyltransferase 2 family. OpgH subfamily.
Involved in the biosynthesis of osmoregulated periplasmic glucans (OPGs).
Belongs to the binding-protein-dependent transport system permease family. LivHM subfamily.
Part of the binding-protein-dependent transport system for branched-chain amino acids. Probably responsible for the translocation of the substrates across the membrane.
Activates expression of the rhaBAD and rhaT operons.
Belongs to the universal stress protein A family.
Belongs to the iron-containing alcohol dehydrogenase family.
In the C-terminal section; belongs to the transposase 35 family.
In the N-terminal section; belongs to the transposase 2 family.
Curlin is the structural subunit of the curli. Curli are coiled surface structures that assemble preferentially at growth temperatures below 37 degrees Celsius. Curli can bind to fibronectin.
Belongs to the SIMIBI class G3E GTPase family. HypB/HupM subfamily.
In minimal medium, cells lacking this gene grow normally with MSO, but growth is inhibited by MSX. In rich medium, growth of cells lacking this gene are partially inhibited by MSX, only when its concentration is at least 50 uM.
Plays a role in the resistance against the toxic effects of L-methionine sulfoximine (MSX), a rare amino acid which inhibits glutamine synthetase (GlnA). Catalyzes the acetylation of MSX. It can also use L-methionine sulfone (MSO) (PubMed:25368301). Also catalyzes the acylation of free L-amino acids using an acyl-CoA as acyl donor (By similarity).
Required for the assembly of the rivet at the earliest stage of flagellar biosynthesis.
Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
Cell-wall hydrolase involved in septum cleavage during cell division.
Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Belongs to the cytochrome ubiquinol oxidase subunit 2 family.
Belongs to the type III secretion exporter family.
Belongs to the major facilitator superfamily. DHA1 family. MdtG (TC 2.A.1.2.20) subfamily.
Metalloprotease involved in CcdA degradation. Suppresses the inhibitory activity of the carbon storage regulator (CsrA).
Participates in cysteine desulfuration mediated by SufS. Cysteine desulfuration mobilizes sulfur from L-cysteine to yield L-alanine and constitutes an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Functions as a sulfur acceptor for SufS, by mediating the direct transfer of the sulfur atom from the S-sulfanylcysteine of SufS, an intermediate product of cysteine desulfuration process.
Belongs to the dienelactone hydrolase family.
May be involved in the biogenesis of curli organelles.
Belongs to the flagella basal body rod proteins family.
The basal body constitutes a major portion of the flagellar organelle and consists of five rings (E,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.
May play a role in stationary phase survival.
Belongs to the ABC transporter superfamily. Macrolide exporter (TC 3.A.1.122) family.
Homodimer. Part of the tripartite efflux system MacAB-TolC, which is composed of an inner membrane transporter, MacB, a periplasmic membrane fusion protein, MacA, and an outer membrane component, TolC. The complex forms a large protein conduit and can translocate molecules across both the inner and outer membranes. Interacts with MacA.
Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides.
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.
Belongs to the mannose-6-phosphate isomerase type 2 family.
Involved in GDP-mannose biosynthesis which serves as the activated sugar nucleotide precursor for mannose residues in cell surface polysaccharides. This enzyme participates in synthesis of the LPS group B O antigen.
May nick specific sequences that contain T:G mispairs resulting from m5C-deamination.
Belongs to the binding-protein-dependent transport system permease family. OppBC subfamily.
Involved in a peptide intake transport system that plays a role in the resistance to antimicrobial peptides.
Part of the sapA-sapB-sapC-sapD-sapF operon, RNA detected in mid-log phase cells.
Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Increases acid tolerance in rpoS mutants, defective in glucose metabolism.
Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.
This enzyme catalyzes the hydrogen sulfide production from sulfite. It is strictly anaerobic. It is regulated by electron acceptors rather than by cysteine.
Belongs to the thioredoxin family. DsbE subfamily.
Involved in disulfide bond formation. Catalyzes a late, reductive step in the assembly of periplasmic c-type cytochromes, probably the reduction of disulfide bonds of the apocytochrome c to allow covalent linkage with the heme. Possible subunit of a heme lyase (By similarity).
Not yet known. Might function in the uptake of a still unidentified substrate.
Component of Salmonella pathogenicity island 2 (SPI-2) type III secretion system, required for secretion of some type III-secreted effectors including the SpvB toxin.
Disruption prevents SpvB-induced F-actin depolymerization in human macrophages without affecting intra-bacterial SpvB protein levels.
Belongs to the glycosyl hydrolase 24 family.
Component of a transport pathway that contributes to membrane integrity.
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.
Binds 1 pyridoxal phosphate per subunit.
Involved in both the arginine and lysine biosynthetic pathways.
The reaction catalyzed by ACOAT is highly reversible. This enzyme may also transaminate ornithine.
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 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. Contacts protein S5. The interaction surface between S4 and S5 is involved in control of translational fidelity.
With S5 and S12 plays an important role in translational accuracy.
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, and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings (PubMed:16267301). Replenishes negative supercoiling downstream of highly transcribed genes to help control overall chromosomal supercoiling density (PubMed:22916023). E.coli makes 15% more negative supercoils in pBR322 plasmid DNA than S.typhimurium; the S.typhimurium GyrB subunit is toxic in E.coli, while the E.coli copy can be expressed in S.typhimurium even though the 2 subunits have 777/804 residues identical (PubMed:17400739).
Belongs to the type II topoisomerase GyrB family.
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+).
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.
Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
Belongs to the bacterial ribosomal protein bL34 family.
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.
Belongs to the transglycosylase Slt family.
Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division. Preferentially cleaves at a distance of more than two disaccharide units from the ends of the glycan chain.
Belongs to the cysteine synthase/cystathionine beta-synthase family.
Two cysteine synthase enzymes are found. Both catalyze the same reaction. Cysteine synthase B can also use thiosulfate in place of sulfide to give cysteine thiosulfonate as a product.
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.
Belongs to the AspA/AstE family. Succinylglutamate desuccinylase subfamily.
By nitrogen and carbon starvation, and arginine, via the ArgR and Crp transcriptional regulators.
Transforms N(2)-succinylglutamate into succinate and glutamate.
Catalyzes the hydrolysis of the N-glycosidic bond of AMP to form adenine and ribose 5-phosphate. Involved in regulation of AMP concentrations.
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.
Belongs to the aromatic acid exporter ArAE (TC 2.A.85) family.
Belongs to the ferritin family. Prokaryotic subfamily.
Component of the lipopolysaccharide transport and assembly complex. Interacts with LptA and the LptBFG transporter complex.
Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. Facilitates the transfer of LPS from the inner membrane to the periplasmic protein LptA. Could be a docking site for LptA.
Required for the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane.
Belongs to the DODA-type extradiol aromatic ring-opening dioxygenase family.
Belongs to the ABC-4 integral membrane protein family. LolC/E subfamily.
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.
Belongs to the ABC transporter superfamily.
Called LivG in S.typhimurium, but we renamed it to LivF for the sake of consistency with the E.coli protein.
Component of the high-affinity branched-chain amino acid transport system.
Member of a two-component regulatory system.
Belongs to the sulfur carrier protein TusA family.
Sulfur carrier protein involved in sulfur trafficking in the cell. Part of a sulfur-relay system required for 2-thiolation during synthesis of 2-thiouridine of the modified wobble base 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) in tRNA. Interacts with IscS and stimulates its cysteine desulfurase activity. Accepts an activated sulfur from IscS, which is then transferred to TusD, and thus determines the direction of sulfur flow from IscS to 2-thiouridine formation. Also appears to be involved in sulfur transfer for the biosynthesis of molybdopterin.
Belongs to the glycosyl hydrolase 31 family.
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
The covalent binding to the substrate causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein.
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.
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 (By similarity).
Belongs to the cytochrome ubiquinol oxidase subunit 1 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.
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.
Phosphorylates 6-deoxy-6-sulfo-D-fructose (SF) to 6-deoxy-6-sulfo-D-fructose 1-phosphate (SFP).
Belongs to the sigma-70 factor family. FliA subfamily.
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor controls the expression of flagella-related genes. May regulate the expression of genes involved in virulence.
Belongs to the TonB-dependent receptor family. BtuB (TC 1.B.14.3.1) subfamily.
Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans-periplasmic membrane protein TonB.
A global transcription regulator. Complexes with cyclic AMP (cAMP) which allosterically activates DNA binding to regulate transcription. It can act as an activator, repressor, coactivator or corepressor. Induces a severe bend in DNA. Acts as a negative regulator of its own synthesis as well as for adenylate cyclase (cyaA), which generates cAMP. Plays a major role in carbon catabolite repression (CCR) (By similarity).
Homodimer, which upon binding cAMP is able to bind DNA. Binds the N- and C-terminus of RNA polymerase subunit RpoA and sigma-70 (RpoD) (By similarity).
The N-terminal domain binds cAMP and is responsible for homodimerization, while the C-terminal domain binds DNA when cAMP is bound.
Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.
Binding to TXN is inhibited by hydrogen peroxide in vitro.
Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway. Can ubiquitinate both ubiquitin and host TXN (thioredoxin). Leads to significant decrease of thioredoxin activity and increase of host cell death.
The LRR (leucine-rich repeat) domain forms a slightly curved solenoid and may mediate interaction with target proteins.
Ubiquitinated in the presence of host E1 ubiquitin-activating enzyme, E2 ubiquitin-conjugating enzyme and ubiquitin.
Enhances distal genes transcription elongation in a specialized subset of operons that encode extracytoplasmic components. RfaH is recruited into a multi-component RNA polymerase complex by the ops element, which is a short conserved DNA sequence located downstream of the main promoter of these operons. Once bound, RfaH suppresses pausing and inhibits Rho-dependent and intrinsic termination at a subset of sites. Termination signals are bypassed, which allows complete synthesis of long RNA chains.
Interacts with both the nontemplate DNA and the RNA polymerase (RNAP).
Allosterically activated by GTP. Probably inhibited by UTP.
Catalyzes the reversible phosphorylation of UMP to UDP.
Acetylation of prosthetic group (2-(5''-phosphoribosyl)-3'-dephosphocoenzyme-A) of the gamma subunit of citrate lyase.
Catalyzes the conversion of N-formimidoyl-L-glutamate to L-glutamate and formamide.
Belongs to the rhamnose isomerase family.
Catalyzes the interconversion of L-rhamnose and L-rhamnulose.
Allosterically activated by N-acetylglucosamine 6-phosphate (GlcNAc6P).
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.
Belongs to the serine/threonine dehydratase family. DsdA subfamily.
Belongs to the PAPS reductase family. CysH subfamily.
Catalyzes the formation of sulfite from phosphoadenosine 5'-phosphosulfate (PAPS) using thioredoxin as an electron donor.
Belongs to the cation diffusion facilitator (CDF) transporter (TC 2.A.4) family. FieF subfamily.
Divalent metal cation transporter which exports Zn(2+), Cd(2+) and possibly Fe(2+). May be involved in zinc and iron detoxification by efflux.
Belongs to the methylenetetrahydrofolate reductase family.
Catalyzes the NADH-dependent reduction of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate. Is required to provide the methyl group necessary for methionine synthetase to convert homocysteine to methionine; the methyl group is given by 5-methyltetrahydrofolate.
Belongs to the ABC transporter superfamily. ABCF family. Uup subfamily.
Probably plays a role in ribosome assembly or function. May be involved in resolution of branched DNA intermediates that result from template switching in postreplication gaps. Binds DNA and has ATPase activity.
Belongs to the major facilitator superfamily. YfcJ family.
Cleaves 6-deoxy-6-sulfo-D-fructose 1-phosphate (SFP) to form dihydroxyacetone phosphate (DHAP) and 3-sulfolactaldehyde (SLA).
An iron-dependent alcohol dehydrogenase required for optimal 1,2-propanediol (1,2-PD) degradation. NAD(+) and NADH are regenerated internally within the bacterial microcompartment (BMC) dedicated to 1,2-PD degradation by the PduP and PduQ enzymes, which reduce NAD(+) and oxidize NADH respectively, although there must also be cofactor transport across the BMC.
Interacts with PduP, probably via the N-terminus of PduQ.
Loss of NADH-dependent reduction of propionaldehyde in BMCs. BMCs appear to be normal, cells grow more slowly on 1,2-PD with limiting or saturating CN-B12.
Binds zinc. Could be an important component of the zinc-balancing mechanism (By similarity).
Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O.
No change observed, indicating that it could be not necessary for the Ara4N addition to lipid A and polymyxin resistance.
Translocates 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol (alpha-L-Ara4N-phosphoundecaprenol) from the cytoplasmic to the periplasmic side of the inner membrane.
Membrane protein involved in F pilin formation.
Catalyzes the synthesis of dTDP-4-amino-4,6-dideoxy-D-galactose (dTDP-Fuc4N) from dTDP-4-keto-6-deoxy-D-glucose (dTDP-D-Glc4O) and L-glutamate.
Binding of tRNA to MiaE induces a protein conformational change that influences the electronic structure of the diiron site.
Contains a nonheme dinuclear iron cluster (PubMed:17679698, PubMed:23906247, PubMed:25453905). Contains three different forms of the dinuclear site: an hydroxo-bridged FeIII-OH-FeIII center, an oxo-bridged FeIII-O-FeIII center and an hydroxo-bridged FeII-OH-FeIII mixed-valent center (PubMed:17679698).
Disruption mutant shows normal growth characteristics after being shifted from anaerobic to aerobic conditions (PubMed:8253666). Mutant shows slower growth on citrate and acetate, and is unable to grow on the citric acid cycle intermediates succinate, fumarate and malate (PubMed:8253666, PubMed:9620964).
Involved in specific tRNA modification. Catalyzes the oxygen-dependent hydroxylation of 2-methylthio-N-6-isopentenyl adenosine (ms2i6A) to produce 2-methylthio-N-6-(cis-hydroxy)isopentenyl adenosine (ms2io6A) at position 37 in tRNAs (PubMed:8253666, PubMed:17679698, PubMed:23906247). Can also use N6-(dimethylallyl)adenosine (i6A) as substrate, with lower efficiency (PubMed:23906247, PubMed:25453905). The presence of the hydroxyl group on the tRNA may regulate the ability of S.typhimurium to grow on the citric acid cycle (CAC) intermediates succinate, fumarate and malate (PubMed:9620964).
It is uncertain whether Met-1 or Met-17 is the initiator.
Belongs to the bacterial ribosomal protein bL27 family.
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).
In the C-terminal section; belongs to the transpeptidase family.
In the N-terminal section; belongs to the glycosyltransferase 51 family.
Belongs to the PINc/VapC protein family.
Toxic component of a toxin-antitoxin (TA) system. A site-specific tRNA-(fMet) endonuclease, it cleaves both charged and uncharged tRNA-(fMet) between positions 38 and 39 at the anticodon stem-loop boundary. Its toxic effects are neutralized by expression of cognate antitoxin VapB.
Belongs to the LpxL/LpxM/LpxP family. LpxP subfamily.
Catalyzes the transfer of palmitoleate from palmitoleoyl-acyl carrier protein (ACP) to Kdo(2)-lipid IV(A) to form Kdo(2)-(palmitoleoyl)-lipid IV(A).
Belongs to the methyltransferase superfamily. RlmI family.
Specifically methylates the cytosine at position 1962 (m5C1962) of 23S rRNA.
Binds to H-NS and modified the range of genes it silences; H-NS alonge silences core gene while the H-NS-Hha complex (and presumably also H-NS-YdgT) silences genes acquired by horizontal gene transfer. Plays a role silencing virulence factors in the absence of factors that induce pathogenicity (By similarity). The complex formed with H-NS binds to the specific 26-bp cnb site in the origin of replication oriC (By similarity).
Forms complexes with both H-NS (PubMed:23515315) and StpA (By similarity).
Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily.
The MetNIQ system is also to be able to transport the toxic methionine analog alpha-methyl-methionine.
This protein is a component of a D-methionine permease, a binding protein-dependent, ATP-driven transport system.
Belongs to the outer membrane OOP (TC 1.B.6) superfamily. OmpX family.
Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage.
Belongs to the Nudix hydrolase family. RppH subfamily.
Belongs to the carbon-nitrogen hydrolase superfamily. NIT1/NIT2 family.
Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins.
Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1B (PBP1b).
Belongs to the bacterial solute-binding protein 9 family.
Involved in the high-affinity zinc uptake transport system.
Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
Involved in cell wall peptidoglycan recycling. Specifically cleaves the amide bond between the lactyl group of N-acetylmuramic acid and the alpha-amino group of the L-alanine in degradation products containing an anhydro N-acetylmuramyl moiety.
Zn(2+) is required for amidase activity.
Belongs to the bacterial secretin family. T3SS SctC subfamily.
Component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells. Forms a ring-shaped multimeric structure with an apparent central pore in the outer membrane.
The core secretion machinery of the T3SS is composed of approximately 20 different proteins, including cytoplasmic components, a base, an export apparatus and a needle. This subunit is part of the base, which anchors the injectisome in the bacterial cell envelope. Forms a stable homooligomeric complex.
Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
Belongs to the pseudouridine synthase RsuA family.
Dual specificity enzyme that catalyzes the synthesis of pseudouridine from uracil-2604 in 23S ribosomal RNA and from uracil-35 in the anticodon of tRNA(Tyr).
Null mutant gains the ability to efficiently use exogenous aminoimidazole riboside (AIRs) as a source of thiamine.
Represses the expression of the STM4065-STM4067 operon.
Belongs to the class-I DAHP synthase family.
Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP).
Responsible for synthesis of pseudouridine from uracil-2605 in 23S ribosomal RNA.
Artificial BMCs can be made in E.coli by expressing pduA-pduB/B'-pduT-pduU-pduN-pduJ-pduK (in this order). Enzymes can be targeted to the BMC, and appear to be encapsulated within it.
Forms BMCs with a variety of morphologies, including elongated, enlarged, and aggregated MCPs and some with rounded cross-sections. Grows in an interrupted manner on 1,2-PD and vitamin B12; grows for a while then stops, then restarts as if a toxic compound was accumulating and then decreases.
Homopentamer (By similarity). Interacts with shell protein PduA (By similarity).
Probably forms vertices in the shell of the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation. Required for structural integrity of BMCs and to mitigate propionaldehyde toxicity.
Belongs to the prokaryotic AdoMetDC family. Type 2 subfamily.
Binds 1 pyruvoyl group covalently per subunit.
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.
Heterooctamer of four alpha and four beta chains arranged as a tetramer 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.
Belongs to the cytochrome c oxidase subunit 2 family.
Belongs to the Nudix hydrolase family. PCD1 subfamily.
Probably mediates the hydrolysis of some nucleoside diphosphate derivatives.
3'-5' exonuclease that prefers single-stranded DNA and RNA. May play a role in the H(2)O(2)-induced DNA damage repair.
Belongs to the metallo-dependent hydrolases superfamily. TatD-type hydrolase family. TatD subfamily.
Belongs to the ABC transporter superfamily. Molybdate importer (TC 3.A.1.8) family.
Part of the ABC transporter complex ModABC involved in molybdenum import. Responsible for energy coupling to the transport system.
The complex is composed of two ATP-binding proteins (ModC), two transmembrane proteins (ModB) and a solute-binding protein (ModA).
Needed for flagellar regrowth and assembly.
Belongs to the universal ribosomal protein uL15 family.
Belongs to the Nudix hydrolase family. NudK subfamily.
In the dimer, the N-terminal domains are swapped between the two monomers, such that residues of both chains contribute to the active site.
Nucleoside diphosphate sugar hydrolase that hydrolyzes GDP-mannose as its preferred substrate, yielding GMP and mannose-1-phosphate.
Belongs to the PTPS family. QueD subfamily.
Conducts the efflux of homoserine and homoserine lactone.
Belongs to the bacterial glucokinase family.
Belongs to the SOS response-associated peptidase family.
Belongs to the peptidase M48 family. BepA subfamily.
Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state.
Belongs to the triosephosphate isomerase family.
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates.
The accessory proteins ExbB and ExbD seem to form a complex with TonB.
Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
Belongs to the glucose-1-phosphate thymidylyltransferase family.
Belongs to the methyltransferase superfamily. Bacterial-type CbiT family.
Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.
Was originally thought to be a precorrin-8w decarboxylase.
Belongs to the fructosamine kinase family.
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.
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 glycosyltransferase 2 family.
Catalyzes the transfer of 4-deoxy-4-formamido-L-arabinose from UDP to undecaprenyl phosphate. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. Plays an important role in pathogenesis by providing resistance to antimicrobial peptides within macrophages or at other anatomic sites encountered during infection.
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 Glu/Leu/Phe/Val dehydrogenases family.
Catalyzes the reversible oxidative deamination of glutamate to alpha-ketoglutarate and ammonia.
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.
The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane.
Cys-106 is easily oxidized to sulfinic acid.
Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Is able to repair glycated serum albumin, collagen, glyceraldehyde-3-phosphate dehydrogenase, and fructose biphosphate aldolase. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE) that cause irreversible damage. Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. However, is less efficient than Hsp31 and YhbO, suggesting that YajL might be preferentially dedicated to protein repair. Displays a covalent chaperone activity with sulfenylated thiol proteins by forming mixed disulfides with members of the thiol proteome, and preferentially with sulfenylated cellular proteins, upon oxidative stress; these mixed disulfides can be subsequently reduced by low-molecular-weight thiols to regenerate YajL and reduced proteins. Involved in biogenesis of ribosomal proteins, probably as a ribosomal protein-folding chaperone. Confers resistance to oxidative stress. Plays an important role in protection against electrophile/carbonyl stress. The chaperone activity reported for YajL is probably recruited to execute its deglycase activity, to interact with non-native glycated proteins and gain access to partially buried glycated sites. Also displays an apparent glyoxalase activity that in fact reflects its deglycase activity.
Belongs to the thioredoxin family. DsbC subfamily.
Required for disulfide bond formation in some periplasmic proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process.
Belongs to the drug/metabolite transporter (DMT) superfamily. Small multidrug resistance (SMR) (TC 2.A.7.1) family. MdtI subfamily.
Part of the ABC transporter complex FhuCDB involved in iron(3+)-hydroxamate import. Responsible for the translocation of the substrate across the membrane (By similarity). Involved in ferrioxamine-mediated iron(III) utilization (PubMed:10103258).
The complex is composed of two ATP-binding proteins (FhuC), two transmembrane proteins (FhuB) and a solute-binding protein (FhuD).
Belongs to the arginine N-succinyltransferase family.
Catalyzes the transfer of succinyl-CoA to arginine to produce N(2)-succinylarginine.
Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate.
Belongs to the L-fucose isomerase family.
Converts the aldose L-fucose into the corresponding ketose L-fuculose.
Belongs to the 'GDXG' lipolytic enzyme family.
Displays esterase activity towards short chain fatty esters (acyl chain length of up to 8 carbons). Able to hydrolyze triacetylglycerol (triacetin) and tributyrylglycerol (tributyrin), but not trioleylglycerol (triolein) or cholesterol oleate. Negatively regulates MalT activity by antagonizing maltotriose binding. Inhibits MelA galactosidase activity.
Homodimer. Interacts with MalT and MelA.
Apoprotein is apparently conformationally labile and readily converts to different states, including inward-facing conformations for substrate access (PubMed:34110360). Contains a conserved cation-binding pocket, which directly connects to the sugar specificity pocket (PubMed:34341464).
Binding of Na(+) and melibiose is cooperative, the binding affinity for one substrate is increased by the presence of the other (PubMed:29054867, PubMed:34110360). With binding of one substrate (either Na(+) or melibiose), MelB favors open conformations (likely outward facing), whereas the cooperative binding of both substrates induces cavity closure. Thus, cooperative binding is the key that regulates the alternating-access process and ensures the obligatory cotransport as the core mechanism for symport (PubMed:34110360). Melibiose uptake is inhibited by valinomycin (PubMed:21148559).
Mediates the transport of melibiose and other galactosides by a symport mechanism (PubMed:21148559, PubMed:24389923, PubMed:29054867, PubMed:34110360). Can use sodium, lithium and protons as coupling cations, with a preference for sodium and lithium (PubMed:21148559, PubMed:24389923, PubMed:29054867). The use of Na(+) as coupling ion for sugar transport is based not on ion selectivity but on competitive binding under physiological conditions, because of a much higher Na(+) concentration under physiological conditions (PubMed:29054867).
Belongs to the monovalent cation:proton antiporter 2 (CPA2) transporter (TC 2.A.37) family. KefC subfamily.
Homodimer. Interacts with the regulatory subunit KefF.
Pore-forming subunit of a potassium efflux system that confers protection against electrophiles. Catalyzes K(+)/H(+) antiport.
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.
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 metallo-beta-lactamase superfamily. Glyoxalase II family.
Binds 2 metal ions per subunit; upon overexpression in E.coli the enzyme purifies with various amounts of iron, zinc and manganese. The endogenous metal is unknown.
Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
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.
Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Part of an enzyme complex containing four subunits: a flavoprotein, an iron-sulfur protein, plus two membrane-anchoring proteins, SdhC and SdhD.
The heme is bound between the two transmembrane subunits.
Belongs to the prokaryotic/mitochondrial release factor family.
Methylated by PrmC. Methylation increases the termination efficiency of RF1 (By similarity).
Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
Belongs to the bacterial secretin family. PilQ subfamily.
Acetylates and inactivates the acetyl-CoA synthase (Acs). Can also acetylate other central metabolic enzymes in response to environmental changes.
Exhibits positive cooperativity. It may be the result of acetyl-CoA binding to two distinct sites, or the result of subunit interactions.
In the N-terminal section; belongs to the acetate CoA ligase alpha subunit family.
In the central section; belongs to the acetate CoA ligase beta subunit family.
Monomer in the absence of acetyl-CoA. Oligomerizes to a tetrameric form in the presence of acetyl-CoA.
May function as a transcriptional regulator that controls feoABC expression.
A low activity DNA endonuclease probably yielding 3'-hydroxyl ends. Involved in RecA-independent recombination and horizontal gene transfer (By similarity).
Belongs to the Rpn/YhgA-like nuclease family.
Belongs to the complex I 75 kDa subunit family.
Composed of 13 different subunits. Subunits NuoCD, E, F, and G constitute the peripheral sector of the complex.
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).
Belongs to the autotransporter-2 (AT-2) (TC 1.B.40) family.
Immunization of mice with folded, full-length, purified SadA elicits an IgG response which provides limited protection against bacterial challenge.
In vitro, loss of sadA does not affect cell aggregation, biofilm formation and adhesion to epithelial cells. Disruption does not affect the course of infection.
Involved in cell aggregation, biofilm formation, and adhesion to human intestinal epithelial cells.
The signal peptide, cleaved at the inner membrane, guides the autotransporter protein to the periplasmic space. Then, insertion of the C-terminal translocator domain in the outer membrane forms a hydrophilic pore for the translocation of the passenger domain to the bacterial cell surface (By similarity). The surface exposed region contains four YadA-like head domains and extended stalk regions, multiply segmented by FGG, HANS, DALL and neck motifs (PubMed:23213248).
Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. Probably responsible for the translocation of the substrate across the membrane.
The complex is composed of two ATP-binding proteins (MlaF), two transmembrane proteins (MlaE), two cytoplasmic solute-binding proteins (MlaB) and six periplasmic solute-binding proteins (MlaD).
Protease that can cleave T7 RNA polymerase. Specific for paired basic residues.
Belongs to the ABC transporter superfamily. sn-glycerol-3-phosphate importer (TC 3.A.1.1.3) family.
Part of the ABC transporter complex UgpBAEC involved in sn-glycerol-3-phosphate (G3P) import. Responsible for energy coupling to the transport system.
A DNA fragment of approximately 900 base pairs, adjacent to the fljB (H2) gene, which specifies the synthesis of phase-2 flagellin, can exist in either orientation with respect to fljB. The orientation of the inversion region controls expression of fljB. The hin gene occupies about two-thirds of the inversion region; it is required for the inversion of the fljB controlling region.
Belongs to the site-specific recombinase resolvase family.
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.
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.
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.
Could be involved in sulfoquinovose import.
Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P).
Belongs to the metallo-dependent hydrolases superfamily. DHOase family. Class II DHOase subfamily.
Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Belongs to the flavin oxidoreductase frp family.
Catalyzes the reduction of nitroaromatic compounds using NADPH. Has a broad electron acceptor specificity. Reduces nitrofurazone by a ping-pong bi-bi mechanism possibly to generate a two-electron transfer product.
Allosteric enzyme. Activity is modulated by K(+), divalent cations, UTP, and tetrahydrobiopterin. Tetrahydrobiopterin is an inhibitor of this enzyme (By similarity).
Belongs to the GTP cyclohydrolase I family.
Toroid-shaped homodecamer, composed of two pentamers of five dimers.
Belongs to the acetyltransferase family.
Belongs to the bacterial ribosomal protein bL33 family.
Part of the 50S ribosomal subunit. Cross-links to the P and E site tRNAs (By similarity).
Belongs to the phosphatase IpgD/SopB family.
Contains the consensus sequence Cys-X(5)-Arg characteristic of Mg-independent phosphatases.
Converts phosphatidylinositol 3,4,5-trisphosphate (PtdIns 3,4,5-P3) to PtdIns 3-P and prevents the transition of PtdIns 3-P to PtdIns 3,5-P2. It is one of the known effectors injected by Salmonella into the host cell and is required for invasion and for an efficient generation and maintenance of Salmonella-containing vacuole (SVC). Alteration of the phosphoinositide composition of the plasma membrane causes membrane ruffling and actin cytoskeleton rearrangements. The persistence of PtdIns 3-P diverts the SCV from the endocytic pathway resulting in enlarged vesicles, which are essential to create a favorable environment where Salmonella can replicate and avoid immune defenses of the host cell.
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.
Part of the binding-protein-dependent transport system for D-methionine and the toxic methionine analog alpha-methyl-methionine. Probably responsible for the translocation of the substrate across the membrane (By similarity).
Involved in the assembly process of the P-ring formation. It may associate with FlgF on the rod constituting a structure essential for the P-ring assembly or may act as a modulator protein for the P-ring assembly.
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.
Belongs to the NADH dehydrogenase family.
Activated by bis-(3'-5') cyclic diguanylic acid (c-di-GMP).
Catalytic subunit of cellulose synthase. It polymerizes uridine 5'-diphosphate glucose to cellulose, which is produced as an extracellular component for mechanical and chemical protection at the onset of the stationary phase, when the cells exhibit multicellular behavior (rdar morphotype). Coexpression of cellulose and thin aggregative fimbriae leads to a hydrophobic network with tightly packed cells embedded in a highly inert matrix.
There are two conserved domains in the globular part of the protein: the N-terminal domain (domain A) contains the conserved DXD motif and is possibly involved in catalysis and substrate binding. The C-terminal domain (domain B) contains the QXXRW motif and is present only in processive glycosyl transferases. It could be involved in the processivity function of the enzyme, possibly required for holding the growing glycan chain in the active site.
Belongs to the HAD-like hydrolase superfamily. Cof family.
Catalyzes the hydrolysis of 4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate (HMP-PP) to 4-amino-2-methyl-5-hydroxymethylpyrimidine phosphate (HMP-P).
Binds 2 divalent metal cations per subunit.
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.
An alpha subtype methylase, recognizes the double-stranded sequence 5'-GATC-3' and methylates A-2 (PubMed:12654995) (By similarity). May be involved in methyl-directed DNA mismatch repair, initiation of chromosome replication and gene expression (By similarity).
Belongs to the N(4)/N(6)-methyltransferase family.
Heterodimer of an alpha and a beta chain.
Probably induced by trehalose-6-phosphate.
Repressor of the treBC operon. It is able to bind trehalose-6-phosphate.
Belongs to the type II topoisomerase GyrA/ParC subunit family. ParC type 1 subfamily.
Heterotetramer composed of ParC and ParE.
Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA (PubMed:22916023). Performs the decatenation events required during the replication of a circular DNA molecule.
Cytoskeletal protein that is involved in cell-shape control through regulation of the length of the long axis.
The helix-turn-helix (HTH) motif in the cytoplasmic domain of the N-terminus is involved in the formation of spirals to maintain the rigid rod shape. As this protein is anchored in the cytoplasmic membrane, the HTH motif may contribute to protein-protein interactions to form the RodZ helix, which is localized beneath the cytoplasmic membrane. The C-terminal domain may be critical for determination of the rod shape by probably interacting with enzymes required for synthesis of the peptidoglycan layer, including PBPs in the periplasm.
Belongs to the zinc-containing alcohol dehydrogenase family.
A beta subtype methylase that binds the system-specific DNA recognition site 5'-CAGAG-3' and methylates A-4 (of only 1 strand as the other does not have an A residue). DNA restriction requires both the Res and Mod subunits.
Homodimer, also forms a functional restriction-competent complex with Res.
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. R2F contains the tyrosyl radical required for catalysis.
Part of the histidine permease ABC transporter. Also part of a lysine/arginine/ornithine transporter. Probably responsible for the translocation of the substrate across the membrane. Required to relay the ATPase-inducing signal from the solute-binding protein to HisP.
The complex is composed of two ATP-binding proteins (HisP), two transmembrane proteins (HisM and HisQ) and a solute-binding protein (HisJ or ArgT).
Belongs to the major facilitator superfamily.
Belongs to the DadA oxidoreductase family.
Interacts with the mammalian NIPSNAP3A and HOOK3 proteins in infected cells.
PubMed:12174087 and PubMed:12193612 report that SpiC is not translocated into the infected cell, and is localized in the bacterial cytoplasm. They show it is required for secretion of SseB and SseC virulence proteins into infected cells.
Virulence protein that plays a central role in mammalian macrophage infection, by inhibiting phagosome-lysosome fusion and cellular trafficking. May act by disrupting the function of the mammalian HOOK3 protein, a protein involved in the cellular traffic.
Belongs to the quinone-dependent D-lactate dehydrogenase family.
Catalyzes the oxidation of D-lactate to pyruvate.
Belongs to the peroxidase family. Peroxidase/catalase subfamily.
Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.
Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme.
Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Required to maintain the reduced state of SoxR.
The complex is composed of six subunits: RsxA, RsxB, RsxC, RsxD, RsxE and RsxG.
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.
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. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
The Tat system comprises two distinct complexes: a TatABC complex, containing multiple copies of TatA, TatB and TatC subunits, and a separate TatA complex, containing only TatA subunits. Substrates initially bind to the TatABC complex, which probably triggers association of the separate TatA complex to form the active translocon.
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. Together with TatB, TatC is part of a receptor directly interacting with Tat signal peptides.
May be involved in recombinational repair of damaged DNA.
ChiQ appears dispensable for growth on either chitobiose or chitotriose.
In the absence of chitobiose, expression of chiPQ is silenced by the ChiX small regulatory RNA (sRNA), which sequesters the ribosome binding site of the chiPQ mRNA by an antisense mechanism. In the presence of chitosugars, the chbBCARFG chitobiose operon is induced and acts as an RNA trap to degrade the constitutively expressed ChiX, leading to the translation of chiPQ. Chitobiose and chitotriose also induce chiP mRNA synthesis.
Belongs to the glycosyltransferase 28 family.
Could be involved in gluconate metabolism.
Belongs to the bacterial flagellin family.
Required for invasion of epithelial cells.
Member of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. Phosphorylated NtrC binds directly to DNA and stimulates the formation of open promoter-sigma54-RNA polymerase complexes.
Phosphorylated and dephosphorylated by NtrB.
Catalyzes the phosphorylation of guanosine and inosine to GMP and IMP, respectively.
Probably involved in the polymerization of enterobacterial common antigen (ECA) trisaccharide repeat units.
Was originally thought to be WecF, the 4-alpha-L-fucosyltransferase.
Belongs to the ABC transporter superfamily. Ycf16 family.
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.
Required for the biogenesis of long polar fimbria; binds and interact with LpfA.
Belongs to the universal ribosomal protein uL13 family.
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.
Belongs to the bile acid:sodium symporter (BASS) (TC 2.A.28) family.
Transports ketopantoate, pantoate and, to a lesser extent, pantothenate into the cell. Can also transport a product of coenzyme A (CoA) degradation that serves as a precursor to CoA and enters the biosynthetic pathway between PanC and CoaBC.
Belongs to type I PK; fructose 1,6-bisphosphate-activated.
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.
Member of the two-component regulatory system ZraS/ZraR. May function as a membrane-associated protein kinase that phosphorylates ZraR in response to high concentrations of zinc or lead in the medium (By similarity).
Was originally thought to be involved in the regulation of the labile hydrogenase activity.
Modulates the polysaccharide chain length of enterobacterial common antigen (ECA).
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.
Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transduction protein PII (GlnB) which indicates the nitrogen status of the cell.
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).
Catalyzes the Claisen rearrangement of chorismate to prephenate.
Belongs to the UPF0073 (Hly-III) family.
Belongs to the branched chain amino acid transporter family.
Liv-II branched chain amino acid transport system, which transports leucine, valine and isoleucine.
Belongs to the Cob(I)alamin adenosyltransferase family. PduO subfamily.
Converts cob(I)alamin to adenosylcobalamin (adenosylcob(III)alamin), the cofactor for propanediol dehydratase. Found in the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation (PubMed:11160088, PubMed:15547259, PubMed:27446048, PubMed:15817784, PubMed:20656910). For adenosylcobalamin synthesis dATP can replace ATP, but no other nucleotides will substitute (PubMed:15547259). PduS and PduO allow regeneration of the adenosylcobalamin cofactor within the BMC (Probable).
Decreased growth on 1,2-PD cyanocobalamin medium; no growth is seen in a double cobA-pduO deletion.
Inhibited by ADP but not significantly by other nucleotides, inhibited by diphosphate and less well by triphosphate.
Mn(2+) and Co(2+) are almost as active as Mg(2+) for adenosylcobalamin synthesis.
Stoichiometry of heme binding is 2 PduOC:1 heme; the binding pocket is formed by a PduOC dimer. Full-length PduO also binds heme.
The C-terminal domain (PduOC) forms stable octomers and also crystallizes as an octomer (PubMed:27446048). Forms a complex with PduS (PubMed:15817784, PubMed:20656910).
The N-terminus (PduON, residues 1-185) has adenosyltransferase activity in vivo and in vitro; it partially complements a deletion mutant for growth on 1,2-PD (PubMed:15547259, PubMed:27446048). The C-terminal domain (PduOC, residues 194-336) is required for full complemention of a pduO deletion (PubMed:27446048).
Belongs to the bacterial solute-binding protein 1 family.
Insertions in thiBPQ cause a defect in the transport of both thiamine and TPP.
Part of the ABC transporter complex ThiBPQ involved in thiamine import (PubMed:9535878). Is also involved in thiamine pyrophosphate transport (PubMed:9535878).
The complex is composed of two ATP-binding proteins (ThiQ), two transmembrane proteins (ThiP) and a solute-binding protein (ThiB).
Trans-acting protein required for termination of DNA replication. Binds to DNA replication terminator sequences (terA to terF) to prevent the passage of replication forks. The termination efficiency will be affected by the affinity of this protein for the terminator sequence.
Belongs to the four-carbon acid sugar kinase family.
Catalyzes the ATP-dependent phosphorylation of 3-oxo-tetronate to 3-oxo-tetronate 4-phosphate.
Deletion mutant is unable to use L-threonate or D-erythronate as a carbon source.
Belongs to the glycosyl hydrolase 43 family.
Belongs to the prokaryotic pantothenate kinase family.
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. Contacts proteins S9 and S11 (By similarity). Binds EngA (AC Q9XCI8).
May be an export pump for several amino acids and their metabolites, including cysteine.
Belongs to the invasin protein B family.
Required for entry into the host cell through presentation or delivery of SipC at the host cell plasma membrane. Along with SipC, is necessary for the transfer of other effector proteins into the host cell. Induces macrophage apoptosis either by binding and activating the proapoptotic enzyme caspase-1 (caspase-1 dependent), resulting in the release of interleukin-1 beta active form, or by disrupting mitochondria and inducing autophagy (caspase-1 independent). The former is dependent of its membrane-fusion activity. The SipBC complex, in association with its chaperone SicA, is regulated by binding of InvE.
SipB membrane integration requires both hydrophobic domains and the helical C-terminal region.
Part of the ABC transporter complex ThiBPQ involved in thiamine import (PubMed:9535878). Probably responsible for the translocation of the substrate across the membrane (Probable). Is also involved in thiamine pyrophosphate transport (PubMed:9535878).
Belongs to the peptidase U32 family. UbiU subfamily.
Required for O(2)-independent ubiquinone (coenzyme Q) biosynthesis. Together with UbiV, is essential for the C6-hydroxylation reaction in the oxygen-independent ubiquinone biosynthesis pathway.
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. NifS/IscS subfamily.
Homodimer. Forms a heterotetramer with IscU, interacts with other sulfur acceptors.
Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur and selenium atoms from cysteine and selenocysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins. Also functions as a selenium delivery protein in the pathway for the biosynthesis of selenophosphate.
A double eutM-eutN strain grows as well as wild-type on ethanolamine (EA) and cyanocobalamin, but a quadruple eutL-eutK-eutM-eutN strain does not grow (PubMed:16291677). A non-polar deletion mutant grows on EA at pH 5.5 to pH 7.0 but not at pH 8.0 or pH 8.5, releases increased amounts of acetaldehyde on EA plus vitamin B12. Preventing acetaldehyde vapor loss allow growth up to pH 8.5 (PubMed:16585748).
Probably forms vertices in the bacterial microcompartment (BMC) shell dedicated to ethanolamine degradation. Expression of eutK, eutL, eutM, eutN, eutS (eutSMNLK) in E.coli leads to formation of a single BMC (PubMed:22428024, PubMed:27063436). Coexpression of eutQ with eutSMNLK permits E.coli to make cells with more than one mobile BMC, as is usual in vivo (PubMed:27063436). It may be involved in transporting positively charged molecules into and out of the BMC (By similarity).
The ethanolamine (EA) catabolic bacterial microcompartment (BMC) probably concentrates low levels of ethanolamine catabolic enzymes, concentrates volatile reaction intermediates, keeps the level of toxic acetaldehyde low, generates enough acetyl-CoA to support cell growth, and maintains a pool of free coenzyme A (CoA) and NAD.
Belongs to the ABC transporter superfamily. Thiamine importer (TC 3.A.1.19.1) family.
Part of the ABC transporter complex ThiBPQ involved in thiamine import (PubMed:9535878). Responsible for energy coupling to the transport system (Probable). Is also involved in thiamine pyrophosphate (TPP) transport (PubMed:9535878).
Belongs to the major facilitator superfamily. EntS (TC 2.A.1.38) family.
Component of an export pathway for enterobactin.
Deletion of the osmU operon eliminates the residual osmoprotection by glycine betaine in a mutant that is lacking the ProP and the ProU systems. OsmU deletion has no effect on the utilization of glycine betaine as an osmoprotectant when ProP or ProU are functional.
Induced by osmotic stress. Part of the osmU operon, which consists of four genes (osmV, osmW, osmX and osmY).
Part of the OsmU ABC transporter complex, which is involved in the uptake of osmoprotectants such as choline-O-sulfate and glycine betaine. Probably responsible for energy coupling to the transport system.
The complex is composed of two ATP-binding proteins (OsmV), two transmembrane proteins (OsmW and OsmY) and a solute-binding protein (OsmX).
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.
Putative function in virulence. Could be involved in promoting S.typhimurium survival within macrophages.
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 (By similarity).
Belongs to the ZIP transporter (TC 2.A.5) family. ZupT subfamily.
Expressed at basal levels in rich medium (PubMed:24430377). Expression increases under zinc limiting conditions (PubMed:24430377).
Mediates zinc uptake (PubMed:24430377). May also transport other divalent cations (Probable). Contributes to zinc acquisition during infection and plays a role in the ability of S.typhimurium to colonize the host tissues (PubMed:24430377).
Mutant lacking this gene is impaired in its ability to grow in metal devoid environments (PubMed:24430377). Mutant lacking znuABC and zupT exhibits a severe growth defect in zinc devoid media, is hypersensitive to oxidative stress and contains reduced levels of intracellular free zinc (PubMed:24430377).
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).
Mg(2+). Mn(2+) can replace Mg(2+) as the divalent metal. The role of the metal is to bind 5-phosphoribose 1-diphosphate and form a Mg-5-phosphoribose 1-diphosphate complex which then serves as substrate for OPRTase.
Belongs to the RNR ribonuclease family. RNase II subfamily.
Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3' to 5' direction.
Catalyzes the strictly specific dephosphorylation of 2'-deoxyribonucleoside 5'-monophosphates.
Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.
Catalyzes the conversion of L-lactate to pyruvate. Is coupled to the respiratory chain.
Belongs to the CcmF/CycK/Ccl1/NrfE/CcsA family.
Belongs to the major facilitator superfamily. DHA1 family. NepI (TC 2.A.1.2.26) subfamily.
Involved in the efflux of purine ribonucleosides, such as inosine and guanosine.
Plays an important role in virulence (PubMed:15213144). A highly abundant outer membrane lipoprotein that controls the distance between the inner and outer membranes. The only protein known to be covalently linked to the peptidoglycan network (PGN). Also non-covalently binds the PGN. The link between the cell outer membrane and PGN contributes to maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane (By similarity).
The integrity of the cell envelope in a lpp null mutant (double-knockout) is not affected.
Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division.
Part of an enzyme complex containing four subunits: a flavoprotein (FrdA), an iron-sulfur protein (FrdB), and two hydrophobic anchor proteins (FrdC and FrdD).
Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; fumarate reductase is used in anaerobic growth, and succinate dehydrogenase is used in aerobic growth. Anchors the catalytic components of the fumarate reductase complex to the cell inner membrane, binds quinones.
A probably major component of the bacterial microcompartment (BMC) shell dedicated to ethanolamine degradation. Expression of eutK, eutL, eutM, eutN, eutS (eutSMNLK) in E.coli leads to formation of a single BMC; expression of this protein alone can also form BMCs (which may be less tightly closed than eutSMNLK shells). The 'bent' shape of this subunit is required for integration of cargo proteins into these BMCs (PubMed:22428024). Coexpression of eutQ with eutSMNLK permits E.coli to make cells with more than one mobile BMC, as is usual in vivo (PubMed:27063436). Targets at least 2 proteins (EutC and EutE) to the interior of the BMC (PubMed:22428024, PubMed:27063436, PubMed:27450681). Proteins such as EutS containing circularly permuted BMC domains may play a key role in conferring heterogeneity and flexibility in this BMC (Probable).
Adding an N- or C-terminal His-tag to this protein prevents it forming BMCs (PubMed:27450681). One side of the hexamer is concave and lined by hydrophobic residues, the other side has a slightly protruding, 6-stranded beta-barrel (By similarity).
Artificial BMCs can be made in E.coli by expressing eutK, eutL, eutM, eutN, eutS (eutSMNLK) or eutS alone. Cargo proteins can be targeted to both BMCs; beta-galactosidase (lacZ) was active within the BMC, showing the BMC allows passage of substrate into the interior. This can lead to the development of tailored BMCs for specific metabolic reactions (PubMed:22428024, PubMed:27063436). The addition of eutQ to the eutSMNLK construct results in biogenesis of multiple BMCs (PubMed:27063436).
Homohexamer with a central pore; the hexamer is probably bent by about 40 degrees rather that symmetric; bending depends on Gly-39 (Probable). Interacts with the N-terminus of EutC, targeting it to the interior of the BMC (PubMed:22428024, PubMed:27063436, PubMed:27450681). Interacts with the N-terminus of EutE, targeting it to the interior of the BMC (PubMed:27450681).
Not required for aerobic growth on ethanolamine (EA) supplemented with cobalamin (vitamin B12) (PubMed:10464203, PubMed:16291677). A non-polar deletion mutant grows on EA from pH 5.5 to pH 8.0, but does not grow at pH 8.5, releases increased amounts of acetaldehyde on EA plus vitamin B12 (PubMed:16585748).
The first gene of the 17-gene eut operon transcribed from a single promoter, induced by ethanolamine and adenosylcobalamin (AdoCbl, vitamin B12) (PubMed:3045078). Expressed at low levels following mouse infection, not induced in infected macrophages or in spleen (PubMed:26565973).
Belongs to the FtsK/SpoIIIE/SftA family.
Consists of an N-terminal domain, which is sufficient for the localization to the septal ring and is required for cell division, 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. The alpha and beta subdomains multimerise to produce a hexameric ring, contain the nucleotide binding motif and form the DNA pump. The gamma subdomain is a regulatory subdomain that controls translocation of DNA by recognition of KOPS motifs and interacts with XerD recombinase (By similarity).
Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the replication terminus region. Translocation stops specifically at Xer-dif sites, where FtsK interacts with the Xer recombinase, allowing activation of chromosome unlinking by recombination. FtsK orienting polar sequences (KOPS) guide the direction of DNA translocation. FtsK can remove proteins from DNA as it translocates, but translocation stops specifically at XerCD-dif site, thereby preventing removal of XerC and XerD from dif (By similarity).
Homohexamer. Forms a ring that surrounds DNA (By similarity).
Involved in protein export. Participates in an early event of protein translocation.
Part of a membrane-bound tetrathionate reductase that catalyzes the reduction of tetrathionate to thiosulfate. TtrC probably anchors TtrA and TtrB to the periplasmic face of the cytoplasmic membrane. May transfer electrons from membrane quinol to TtrB. During mice infection, the ability to use tetrathionate as an electron acceptor is a growth advantage for S.typhimurium over the competing microbiota in the lumen of the inflamed gut.
Probably composed of three subunits: TtrA, TtrB and TtrC.
Transcriptionally regulated by Fnr and by the TtrR/TtrS two-component regulatory system.
Belongs to the UDP-glucose/GDP-mannose dehydrogenase family. WecC subfamily.
Catalyzes the four-electron oxidation of UDP-N-acetyl-D-mannosamine (UDP-ManNAc), reducing NAD(+) and releasing UDP-N-acetylmannosaminuronic acid (UDP-ManNAcA).
Belongs to the amino acid/polyamine transporter 2 family. SdaC/TdcC subfamily.
Involved in the import of threonine and serine into the cell, with the concomitant import of a proton (symport system).
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. Csd subfamily.
Belongs to the cytidine and deoxycytidylate deaminase family.
This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
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 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.
Belongs to the complex I subunit 3 family.
NDH-1 is composed of 13 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex.
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Belongs to the major facilitator superfamily. Nucleoside:H(+) symporter (NHS) (TC 2.A.1.10) family.
Broad-specificity transporter of purine and pyrimidine nucleosides. Transport is driven by a proton motive force.
Belongs to the metallo-dependent hydrolases superfamily. Adenosine and AMP deaminases family. Adenosine deaminase subfamily.
Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine.
Catalyzes the interconversion of L-alanine and D-alanine. Provides the D-alanine required for cell wall biosynthesis.
Homodimer. Polymerizes to form helical filaments.
Negative regulator of replication initiation, which contributes to regulation of DNA replication and ensures that replication initiation occurs exactly once per chromosome per cell cycle. Binds to pairs of hemimethylated GATC sequences in the oriC region, thus preventing assembly of replication proteins and re-initiation at newly replicated origins. Repression is relieved when the region becomes fully methylated.
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.
Belongs to the PdxA family. PdxA2 subfamily.
Catalyzes the NAD-dependent oxidation and subsequent decarboxylation of D-threonate 4-phosphate to produce dihydroxyacetone phosphate (DHAP) (PubMed:27402745). Can also use 4-hydroxy-L-threonine 4-phosphate as substrate (PubMed:27294475, PubMed:27402745).
Deletion mutant is unable to use D-threonate as a carbon source.
Belongs to the RIC family. YtfE subfamily.
Di-iron-containing protein involved in the repair of iron-sulfur clusters damaged by oxidative and nitrosative stress conditions.
Belongs to the ABC transporter superfamily. Spermidine/putrescine importer (TC 3.A.1.11.1) family.
Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system.
The complex is composed of two ATP-binding proteins (PotA), two transmembrane proteins (PotB and PotC) and a solute-binding protein (PotD).
Belongs to the acyltransferase 3 family. OpgC subfamily.
Necessary for the succinyl substitution of periplasmic glucans. Could catalyze the transfer of succinyl residues from the cytoplasmic side of the membrane to the nascent glucan backbones on the periplasmic side of the membrane.
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 (PubMed:9521740). 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 (PubMed:7503993, PubMed:9521740, PubMed:9521741).
Belongs to the glutamate:Na(+) symporter (ESS) (TC 2.A.27) family.
Catalyzes the sodium-dependent transport of glutamate.
Belongs to the succinylarginine dihydrolase family.
Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)-succinylornithine, ammonia and CO(2).
Artificial BMCs can be made in E.coli by expressing eutK, eutL, eutM, eutN, eutS (eutSMNLK) or eutS alone. Cargo proteins can be targeted to them using the first 19 residues of this protein. Beta-galactosidase (lacZ) was active within the BMC, showing the BMC allows passage of substrate into the interior. This can lead to the development of tailored BMCs for specific metabolic reactions.
Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds (Probable). It is spontaneously inactivated by its substrate and reactivated by EutA (By similarity). May play a role in bacterial microcompartment (BMC) assembly or maintenance (Probable). Directly targeted to the BMC (PubMed:22428024, PubMed:27063436, PubMed:27450681).
No aerobic growth on ethanolamine (EA) supplemented with cobalamin (vitamin B12) (PubMed:10464203, PubMed:2656649). A non-polar deletion mutant does not grow on EA between pH 5.5 and pH 8.5 (PubMed:16585748). A deletion allows growth on acetate, suggesting BMC assembly or maintenance is impaired (PubMed:23585538).
The basic unit is a heterodimer which dimerizes to form tetramers (PubMed:1550360). The heterotetramers trimerize; 6 large subunits form a core ring with 6 small subunits projecting outwards (Probable). Interacts with EutS, which targets it to the interior of the BMC (PubMed:22428024, PubMed:27063436, PubMed:27450681).
The first 19 residues target foreign proteins (tested with eGFP, mCherry and lacZ) to the BMC both in situ and in E.coli. The cargo is only detected by Western blot in broken shells, strongly suggesting this protein is normally found inside the BMC and not on its exterior.
Catalyzes the phosphorylation of thiamine to thiamine phosphate.
Belongs to the acyl coenzyme A hydrolase family.
Catalyzes the hydrolysis of the thioester bond in palmitoyl-CoA and malonyl-CoA.
Belongs to the Maf family. YceF subfamily.
Nucleoside triphosphate pyrophosphatase that hydrolyzes 7-methyl-GTP (m(7)GTP) (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).
Belongs to the metallo-dependent hydrolases superfamily. Phosphotriesterase family.
Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family.
Serves to protect the cell against DNA damage by alkyl hydroperoxides. It can use either NADH or NADPH as electron donor for direct reduction of redox dyes or of alkyl hydroperoxides when combined with the AhpC protein.
The active site is a redox-active disulfide bond.
Binds 4 Mg(2+) or Mn(2+) ions per subunit.
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.
Incises the DNA at the 3' side of a lesion during nucleotide excision repair. Incises the DNA farther away from the lesion than UvrC. Not able to incise the 5' site of a lesion. When a lesion remains because UvrC is not able to induce the 3' incision, Cho incises the DNA. Then UvrC makes the 5' incision. The combined action of Cho and UvrC broadens the substrate range of nucleotide excision repair (By similarity).
Belongs to the anaerobic G-3-P dehydrogenase subunit B family.
Composed of a catalytic GlpA/B dimer and of membrane bound GlpC.
Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses fumarate or nitrate as electron acceptor.
Involved in translocation of long-chain fatty acids across the outer membrane. FadL may form a specific channel (By similarity).
Belongs to the major facilitator superfamily. YhhS family.
Involved in the biosynthesis of the capsular polysaccharide colanic acid.
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 cation transport ATPase (P-type) (TC 3.A.3) family. Type IA subfamily.
Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit is responsible for energy coupling to the transport system and for the release of the potassium ions to the cytoplasm.
The system is composed of three essential subunits: KdpA, KdpB and KdpC.
Belongs to the heme-copper respiratory oxidase family.
Involved in cell filamentation induced by cyclic AMP.
Probable adenylyltransferase that mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (By similarity). Involved in cell filamentation induced by cyclic AMP.
Plays a role in the transport of magnesium and cobalt ions.
Actin-binding protein that interferes with host cell actin cytoskeleton. It stimulates actin polymerization and counteracts F-actin destabilizing proteins. Potentiates SipC activity; both are required for an efficient bacterial internalization. In vitro, forms a complex with host cell protein T-plastin increasing actin bundling. It inhibits ADF/cofilin-directed depolymerization both by preventing binding of ADF and cofilin and by displacing them from F-actin. Also protects F-actin from gelsolin-directed severing and reanneals gelsolin-severed F-actin fragments.
Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 1 subfamily.
Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
Belongs to the ferredoxin--NADP reductase type 1 family.
Involved in the regulation of ptsG expression by binding and inactivating Mlc.
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 (By similarity).
Forms an icosahedral capsid composed of 60 subunits, arranged as a dodecamer of pentamers.
Necessary for formate dehydrogenase activity.
Belongs to the protein kinase superfamily. KdkA/RfaP family.
Catalyzes the phosphorylation of heptose(I) of the outer membrane lipopolysaccharide core.
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.
Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
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.
Belongs to the RelB/DinJ antitoxin family.
Belongs to the major facilitator superfamily. YcaD (TC 2.A.1.26) family.
Belongs to the IPP isomerase type 1 family.
Binds 1 Mg(2+) ion per subunit. The magnesium ion binds only when substrate is bound.
Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).
Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with (2E,6E)-farnesyl diphosphate (E,E-FPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E,38E)-undecaprenyl diphosphate (di-trans,octa-cis-UPP). UPP is the precursor of glycosyl carrier lipid in the biosynthesis of bacterial cell wall polysaccharide components such as peptidoglycan and lipopolysaccharide.
Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic.
Part of a complex composed of FtsB, FtsL and FtsQ.
Modulates cellular lipopolysaccharide (LPS) levels by regulating LpxC, which is involved in lipid A biosynthesis. May act by modulating the proteolytic activity of FtsH towards LpxC. May also coordinate assembly of proteins involved in LPS synthesis at the plasma membrane.
Adds the galactose(I) group on the glucose(I) group of LPS.
Belongs to the glycosyltransferase 8 family.
This protein activates the transcription of the IlvC gene in the presence of acetolactate or acetohydroxybutyrate. IlvY is also a negative regulator of its own expression.
Belongs to the bacterial-type ferredoxin family. FixX subfamily.
Could be part of an electron transfer system required for anaerobic carnitine reduction. Could be a 3Fe-4S cluster-containing protein (By similarity).
Acquisition of Mn(2+) in addition to Fe(2+) is required for intercellular survival, replication in macrophages in vitro and for full virulence in vivo.
Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. FeoB GTPase (TC 9.A.8) family.
Iron uptake is repressed by the global regulator Fur.
Probable transporter for a GTP-driven Fe(2+) uptake system.
Binds 5 heme c groups covalently per monomer.
Catalyzes the reduction of nitrite to ammonia, consuming six electrons in the process.
Belongs to the major facilitator superfamily. Set transporter family.
Involved in the efflux of sugars. The physiological role may be the detoxification of non-metabolizable sugar analogs. Can transport lactose and glucose (By similarity).
This gene is probably the major expressed form.
Belongs to the ABC-2 integral membrane protein family.
DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. It degrades transiently denatured and unfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. Its proteolytic activity is essential for the survival of cells at elevated temperatures. It can degrade IciA, ada, casein, globin and PapA. DegP shares specificity with DegQ. DegP is also involved in the biogenesis of partially folded outer-membrane proteins (OMP) (By similarity).
DegP can reversibly switch between different oligomeric forms that represent inactive (6-mer) and active (12- and 24-mer) protease states. Substrate binding triggers the conversion of the resting DegP trimer and hexamer into catalytically active 12- and 24-mers. The conversion of 6-mer (DegP6) into 12-mer (DegP12) or 24-mer (DegP24) is crucial in regulating protease activity (By similarity).
DegP is indispensable for bacterial survival at temperatures above 42 degrees Celsius, however is also able to digest its natural substrates in a reducing environment at temperatures as low as 20 degrees Celsius.
Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Functions as substrate-specific channel for nucleosides and deoxynucleosides. Functions also in albicidin uptake and as receptor for colicin K.
Accumulation of full-length 23S rRNA as well as larger precursor rRNA transcripts. Strain grows slower than wild-type.
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). Removes small helical intervening sequences (IVSs) from all 7 of the 23S rRNA transcripts. Probably also processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Probably processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.
This organism contains small helical (90-110 nucleotide) intervening sequences (IVSs) in all 7 23S rRNA genes at either the 550-bp or 1170-bp positions or both, accumulating the 23S rRNA as 2.4, 1.7, 1.6, 0.7, and 0.5 kb pieces.
Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
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 (By similarity).
Protein L4 is a both a transcriptional repressor and a translational repressor protein. It regulates transcription of the S10 operon (to which L4 belongs) by causing premature termination of transcription within the S10 leader. L4 controls the translation of the S10 operon by binding to its mRNA.
Belongs to the Maf family. YhdE subfamily.
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.
Involved in the transcriptional regulation of the propionate catabolism operon.
Belongs to the RNA polymerase alpha chain family.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
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 (By similarity).
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 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).
Belongs to the ABC transporter superfamily. Lipoprotein translocase (TC 3.A.1.125) family.
Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner.
The complex is composed of two ATP-binding proteins (LolD) and two transmembrane proteins (LolC and LolE).
Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
Heterododecamer (2C3:3R2) of six catalytic PyrB chains organized as two trimers (C3), and six regulatory PyrI chains organized as three dimers (R2).
Belongs to the DsbB family. DsbI subfamily.
Required for disulfide bond formation in some proteins. Part of a redox system composed of DsbI and DsbL that mediates formation of an essential disulfide bond in AssT.
Was originally given the gene name dsbB; however another gene encoding a dsbB more closely related to that of the characterized E.coli protein bears this gene name (DSBB_SALTY, AC Q8XG65).
Belongs to the glycosyl hydrolase 3 family. NagZ subfamily.
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. Plays a role in beta-lactam antibiotic resistance via its role in generating anhydro-N-acetylmuramic acid-linked peptides; these peptides function as signaling molecules that induce high-level expression of the beta-lactamase AmpC.
Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamA, the core component of the assembly machinery.
Heterohexamer, formed by a dimer of trimers. The hexameric TusBCD complex contains 2 copies each of TusB, TusC and TusD. The TusBCD complex interacts with TusE.
Part of a sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions.
Belongs to the short-chain dehydrogenases/reductases (SDR) family.
Positive regulator for the plasmid-encoded virulence factors SpvA, SpvB, and SpvC.
Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides.
Belongs to the SIS family. PHI subfamily.
Belongs to the autoinducer-2 exporter (AI-2E) (TC 2.A.86) family.
Belongs to the glutamate synthase family.
Catalyzes the phosphorylation of D-xylulose to D-xylulose 5-phosphate.
Involved in iron-sulfur (Fe-S) cluster assembly. May act as a regulator of Fe-S biogenesis.
Belongs to the Orn/Lys/Arg decarboxylase class-I family.
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.
Belongs to the Nudix hydrolase family. NudF subfamily.
Low-potential electron donor to a number of redox enzymes (Potential). Involved in the reactivation of inactive cob(II)alamin in methionine synthase.
Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis.
Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit binds the periplasmic potassium ions and delivers the ions to the membrane domain of KdpB through an intramembrane tunnel.
Belongs to the glycosyltransferase 9 family.
Hexamer formed by 3 homodimers (By similarity). Homodimer.
Involved in the catabolism of quinolinic acid (QA).
Single-stranded-DNA-specific exonuclease. Required for many types of recombinational events, although the stringency of the requirement for RecJ appears to vary with the type of recombinational event monitored and the other recombination gene products which are available.
Belongs to the DNA mismatch repair MutL/HexB family.
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.
Catalyzes the proton-dependent uptake of 2-keto-3-deoxygluconate (KDG) into the cell.
The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. Involved in lambda inhibition of host protein synthesis. PTH activity may, directly or indirectly, be the target for lambda bar RNA leading to rap cell death (By similarity).
Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This 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.
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.
Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
In the C-terminal section; belongs to the NnrD/CARKD family.
In the N-terminal section; belongs to the NnrE/AIBP family.
Belongs to the bacterial ribosomal protein bS18 family.
Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit.
Part of the 30S ribosomal subunit. Forms a tight heterodimer with protein S6 (By similarity).
Belongs to the small heat shock protein (HSP20) family.
Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protease targets the host cell ubiquitin pathway by acting as a deubiquitinase in infected host cells. Specifically hydrolyzes mono- and polyubiquitin substrates in vitro with a preference for 'Lys-63'-linked ubiquitin chains, suggesting that it interferes with a signaling pathway rather than inhibiting proteasomal-dependent degradation of its targets. Does not possess desumoylating activity. Is required for the Salmonella-induced delayed cytotoxicity in macrophages and full virulence. Is not required for intracellular bacterial replication.
Expression of the gene is induced inside phagocytic cells and is dependent on the SsrA/SsrB system.
Belongs to the RbsD / FucU family. FucU mutarotase subfamily.
Involved in the anomeric conversion of L-fucose.
Called LivF in S.typhimurium, but we renamed it to LivG for the sake of consistency with the E.coli protein.
Displays glyoxalase activity, catalyzing the conversion of glyoxal to glycolate.
Belongs to the aerobic coproporphyrinogen-III oxidase family.
Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX.
Required for proper surface expression of the autotransporter adhesin SadA. Could be directly involved in the biogenesis of functionally active SadA.
The homotrimer is held together by an extended N-terminal coiled coil, which leads into three separate globular C-terminal domains of beta-sandwich topology.
Belongs to the methyltransferase superfamily. RsmC family.
Specifically methylates the guanine in position 1207 of 16S rRNA in the 30S particle.
Belongs to the methyltransferase superfamily. RsmI family.
Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA.
Belongs to the HAD-like hydrolase superfamily. SerB family.
Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34.
In the C-terminal section; belongs to the DAO family.
In the N-terminal section; belongs to the methyltransferase superfamily. tRNA (mnm(5)s(2)U34)-methyltransferase family.
Belongs to the TrkH potassium transport family.
Low-affinity potassium transport system. Interacts with Trk system potassium uptake protein TrkA and requires TrkE for transport activity (By similarity).
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.
Expressed in response to both environmental conditions and genetic regulatory factors. Transcription is subject to complex control and is stimulated by the SPI1-encoded HilC and HilD.
The main transcriptional regulator of the Salmonella pathogenicity island 1 (SPI1) gene expression. Activates the expression of invasion genes by a direct action at their promoters and also indirectly by increasing the level of InvF. Also binds upstream of prgH and directly activates the expression of prgHIJK operon.
Belongs to the NAD(P)-dependent epimerase/dehydratase family. SDR39U1 subfamily.
Belongs to the complex I 51 kDa subunit family.
Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family.
The enzymes which catalyze the reversible phosphorolysis of pyrimidine nucleosides are involved in the degradation of these compounds and in their utilization as carbon and energy sources, or in the rescue of pyrimidine bases for nucleotide synthesis.
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 rotation of the flagellar motor. Probable transmembrane proton channel (By similarity).
Part of the ABC transporter complex LsrABCD involved in autoinducer 2 (AI-2) import. Probably responsible for the translocation of the substrate across the membrane (Probable).
Belongs to the ABC1 family. UbiB subfamily.
Is probably a protein kinase regulator of UbiI activity which is involved in aerobic coenzyme Q (ubiquinone) biosynthesis.
Belongs to the protein kinase superfamily. RfaY/WaaY family.
Catalyzes the phosphorylation of heptose(II) of the outer membrane lipopolysaccharide core.
Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L-selenocysteine. Selenocysteine lyase activity is however unsure in vivo.
Homodimer. Interacts with SufE and the SufBCD complex composed of SufB, SufC and SufD. The interaction with SufE is required to mediate the direct transfer of the sulfur atom from the S-sulfanylcysteine.
Belongs to the mandelate racemase/muconate lactonizing enzyme family.
Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfC subfamily.
Belongs to the SMC family. MukB subfamily.
Homodimerization via its hinge domain. Binds to DNA via its C-terminal region. Interacts, and probably forms a ternary complex, with MukE and MukF via its C-terminal region. The complex formation is stimulated by calcium or magnesium. Interacts with tubulin-related protein FtsZ.
Plays a central role in chromosome condensation, segregation and cell cycle progression. Functions as a homodimer, which is essential for chromosome partition. Involved in negative DNA supercoiling in vivo, and by this means organize and compact chromosomes. May achieve or facilitate chromosome segregation by condensation DNA from both sides of a centrally located replisome during cell division.
The hinge domain, which separates the large intramolecular coiled coil regions, allows the homodimerization, forming a V-shaped homodimer.
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
In the N-terminal section; belongs to the 2-acyl-GPE acetyltransferase family.
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Molecular chaperone required for SptP stabilization and secretion.
The structure of the SptP-SicP complex contains four molecules of the chaperone SicP, aligned in a linear fashion and arranged in two sets of tightly bound homodimers that bind two SptP molecules. The SicP homodimers do not interact with each other, but are held together by a molecular interface formed between two SptP molecules. The chaperone-binding domain of SptP does not adopt a globular fold for interaction with SicP. Each SptP molecule is wrapped around by three SicP chaperones (two chaperones from one homodimer and a third one from the opposite homodimer pair). SptP interacts with SicP chaperone dimers mainly through four regions of its chaperone-binding domain.
Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine.
Belongs to the prokaryotic sulfate-binding protein family.
Part of the ABC transporter complex CysAWTP (TC 3.A.1.6.1) involved in sulfate/thiosulfate import. This protein specifically binds thiosulfate and is involved in its transmembrane transport (By similarity).
Belongs to the universal ribosomal protein uL24 family.
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 EndA/NucM nuclease family.
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.
Belongs to the acetylglutamate kinase family. ArgB subfamily.
Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Could be involved in the maturation of NapA, the catalytic subunit of the periplasmic nitrate reductase, before its export into the periplasm.
Interacts with the cytoplasmic NapA precursor.
Belongs to the methylthiotransferase family. RimO subfamily.
Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12.
Belongs to the phosphate acetyltransferase and butyryltransferase family.
Can use ethanolamine (EA) as a nitrogen source but not as a carbon source (PubMed:2656649, PubMed:23585538). Not required for aerobic growth on EA supplemented with cobalamin (vitamin B12); deletions and mutations in this gene probably have polar effects on downstream gene expression. A double eutD-eutM and a quadruple eutP-eutQ-eutT-eutD deletion are not required for growth in the above conditions (PubMed:10464203). Somewhat reduced growth on EA, no excretion of acetate from cells. Reduced growth is due to residual nutrients from rich medium (PubMed:16272400, PubMed:23585538). A non-polar deletion mutant does not grow on EA between pH 5.5 and pH 8.5, releases slightly increased amounts of acetaldehyde on EA plus vitamin B12 (PubMed:16585748).
Required for the use of ethanolamide (EA) as carbon, but not nitrogen, source (Probable). Involved in acetate metabolism during growth on EA, when expressed independently of the eut operon it can restore growth to a double pta-acs deletion mutant (PubMed:14996820). Required for acetate excretion during growth on EA (PubMed:16272400).
Belongs to the TRAP transporter small permease family.
A translation factor that gates the progression of the 70S ribosomal initiation complex (IC, containing tRNA(fMet) in the P-site) into the translation elongation cycle by using a mechanism sensitive to the ATP/ADP ratio. Binds to the 70S ribosome E-site where it modulates the state of the translating ribosome during subunit translocation. ATP hydrolysis probably frees it from the ribosome, which can enter the elongation phase.
Belongs to the ABC transporter superfamily. ABCF family. Translational throttle EttA subfamily.
Monomer. Probably contacts ribosomal proteins L1, L5, L33 and S7, the 16S and 23S rRNA and the P-site containing tRNA(fMet).
The P-site tRNA interaction motif (PtIM domain) probably interacts with the P-site tRNA(fMet) as well as the 23S rRNA.
The arm domain is inserted in the first ABC transporter domain. Probably contacts ribosomal protein L1.
Belongs to the gluconeogenesis factor family.
Required for morphogenesis under gluconeogenic growth conditions.
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.
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.
Belongs to the DNA/RNA non-specific endonuclease family.
Activates the cell division inhibited by chromosomal DNA over-replication.
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.
AcrA-AcrB-AcrZ-TolC is a drug efflux protein complex with a broad substrate specificity. This protein binds to AcrB and is required for efflux of some but not all substrates, suggesting it may influence the specificity of drug export.
Part of the AcrA-AcrB-AcrZ-TolC efflux pump, interacts directly with AcrB.
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 to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth.
Belongs to the mannonate dehydratase family.
Catalyzes the dehydration of D-mannonate.
Belongs to the TorD/DmsD family. TorD subfamily.
Involved in the biogenesis of TorA. Acts on TorA before the insertion of the molybdenum cofactor and, as a result, probably favors a conformation of the apoenzyme that is competent for acquiring the cofactor.
Component of the PhsABC thiosulfate reductase that catalyzes the reduction of thiosulfate to sulfite and hydrogen sulfide, with menaquinol as the sole electron donor. Proton motive force (PMF) is required to drive transmembrane electron transfer within the reductase. The PhsB subunit transfers electrons between PhsC and PhsA.
Composed of three subunits: PhsA, PhsB and PhsC.
BMC production is induced by growth on 1,2-PD vitamin B12 medium (PubMed:10498708). By either propanediol or glycerol.
Belongs to the diol/glycerol dehydratase medium subunit family.
Cells lacking this gene are defective in aerobic degradation of propanediol and display no propanediol dehydratase activity. A triple pduC-pduD-pduE deletion releases no acetaldehyde when grown on propanediol (PubMed:16585748).
Part of the PduCDE complex that catalyzes the dehydration of 1,2-propanediol (1,2-PD) to propionaldehyde. Required for S.typhimurium growth on 1,2-PD as the sole carbon and energy source (Probable) (PubMed:9023178). This subunit is directly targeted to the bacterial microcompartment (BMC) dedicated to 1,2-PD degradation, and is also responsible for targeting the other 2 subunits (pduC and pduE) (PubMed:21821773, PubMed:26283792).
The first 18 residues targets this enzyme and foreign proteins (tested with GST and eGFP) to the BMC. The cargo is only detected by Western blot in broken shells, strongly suggesting this protein is normally found inside the BMC and not on its exterior (PubMed:21821773, PubMed:26283792). PduD and PduP compete for encapsulation in BMCs, suggesting PduD also binds to PduA and/or PduJ (PubMed:26283792).
The propanediol dehydratase enzyme is a heterotrimeric complex composed of a large (PduC), a medium (PduD) and a small (PduE) subunit.
Cells lacking this gene do not produce Sifs in epithelial cells and show attenuated virulence in mice.
Domains throughout the protein, and not only the N-terminus, are required for secretion and translocation. Both N- and C-terminal domains are also required for formation of tubules.
Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is required for endosomal tubulation and formation of Salmonella-induced filaments (Sifs), which are filamentous structures containing lysosomal membrane glycoproteins within epithelial cells. Sif formation is concomitant with intracellular bacterial replication.
Interacts with host PLEKHM2. Interacts with SseJ; the interaction is indirect.
Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules (By similarity). Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria. Involved in the regulation of cellulose production (By similarity).
Global transcriptional regulator, which plays an important role in the regulation of carbon metabolism.
Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring.
A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and facilitates RecA-binding to the ssDNA for homologous DNA recombination and repair. Holoenzyme degrades any linearized DNA that is unable to undergo homologous recombination. In the holoenzyme this subunit contributes ATPase, 3'-5' helicase, exonuclease activity and loads RecA onto ssDNA.
Heterotrimer of RecB, RecC and RecD. All subunits contribute to DNA-binding. Interacts with RecA.
The C-terminal domain has nuclease activity and interacts with RecD. It interacts with RecA, facilitating its loading onto ssDNA.
The N-terminal DNA-binding domain is a ssDNA-dependent ATPase and has ATP-dependent 3'-5' helicase function. This domain interacts with RecC.
Belongs to the AAA ATPase family. RarA/MGS1/WRNIP1 subfamily.
DNA-dependent ATPase that plays important roles in cellular responses to stalled DNA replication processes.
Belongs to the aldolase class II family. AraD/FucA subfamily.
Involved in the degradation of L-fucose and D-arabinose. Catalyzes the reversible cleavage of L-fuculose 1-phosphate (Fuc1P) to yield dihydroxyacetone phosphate (DHAP) and L-lactaldehyde.
Belongs to the heat shock protein 70 family.
Belongs to the [NiFe]/[NiFeSe] hydrogenase small subunit family.
A minor shell protein of the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation. The isolated BMC shell component protein ratio for J:A:B':B:K:T:U is approximately 15:10:7:6:1:1:2 (PubMed:12923081). Not required for structural integrity of BMCs nor to mitigate propionaldehyde toxicity, may selectively transport specific metabolites (PubMed:21239588). May be involved in electron transport across the BMC shell (Probable). Can be engineered to alter permeability of the BMC shell (PubMed:31674899).
Homotrimerizes to form a pseudohexamer; in wild-type the central triangular pore is probably blocked by the [4Fe-4S] center (PubMed:20870711, PubMed:22654060). Interacts with PduS (By similarity).
No visible effect on BMC morphology. Slight growth impairment on 1,2-propanediol and vitamin B12.
Probably bound by a single Cys residue from each subunit; which protein provides the fourth ligand is unknown.
Removal of the [4Fe-4S] center by mutagenesis and different substitutions of Cys-38 allows an increased growth rate under certain limiting-conditions ('L-40' in PduA, pduQ deletion), strongly suggesting this subunit has acquired the ability to transport 1,2-PD, propionaldehyde and NAD(+)/NADH across the BMC shell.
When mutated at 9 positions (construct O3-33 with these mutations; K15A, M67L, N148A, N149L, E156S, E160A, K161Y, R167A, V169L) self-assembles into bodies with 24 subunits, suitable for nanotechnology uses.
Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway. Required for inducing polymorphonuclear leukocytes migration across the intestinal epithelium. Preferentially uses host UBE2D1 (UBCH5A), UBE2D2 (UBCH5B) and UBE2L3 (UBCH7) as E2 ubiquitin-conjugating enzymes.
Requires SpaK/InvB as a chaperone for its stability and for secretion.
The N-terminal 45 amino acids are necessary and sufficient for secretion and translocation into host cells. This N-terminal region binds the SpaK/InvB chaperone. Contains a C-terminal HECT-like domain.
Catalyzes the phosphorylation of autoinducer-2 (AI-2) to phospho-AI-2, which subsequently inactivates the transcriptional regulator LsrR and leads to the transcription of the lsr operon. Phosphorylates the ring-open form of (S)-4,5-dihydroxypentane-2,3-dione (DPD), which is the precursor to all AI-2 signaling molecules, at the C5 position.
Belongs to the SEDS family. FtsW subfamily.
Peptidoglycan polymerase that is essential for cell division.
Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. GhrA subfamily.
Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively.
Endopeptidase that degrades small peptides of less than 7 kDa, such as glucagon and insulin.
Belongs to the nucleobase:cation symporter-2 (NCS2) (TC 2.A.40) family. Azg-like subfamily.
Monomer. Interacts with the transcription termination factor Rho and with RNA polymerase.
Participates in transcription elongation, termination and antitermination. In the absence of Rho, increases the rate of transcription elongation by the RNA polymerase (RNAP), probably by partially suppressing pausing. In the presence of Rho, modulates most Rho-dependent termination events by interacting with the RNAP to render the complex more susceptible to the termination activity of Rho. May be required to overcome a kinetic limitation of Rho to function at certain terminators. Also involved in ribosomal RNA transcriptional antitermination.
Involved in the invasion of the cells of the intestinal epithelium. Could be involved in the translocation of the InvE protein.
Binds 2 Zn(2+) ions per subunit. One is catalytic and the other provides a structural contribution.
Belongs to the ABC transporter superfamily. 2-aminoethylphosphonate importer (TC 3.A.1.11.5) family.
Induced when inorganic phosphate is limiting; this is controlled by PhoB.
Maps to a phosphate-starvation-inducible locus previously known as psiC.
Probably part of the PhnSTUV complex (TC 3.A.1.11.5) involved in 2-aminoethylphosphonate import. Probably responsible for energy coupling to the transport system.
Belongs to the methyltransferase superfamily. RsmJ family.
Specifically methylates the guanosine in position 1516 of 16S rRNA.
Activity is lost when the metal is removed through urea denaturation or chelation, and can be regained by addition of metal.
Belongs to the histidinol dehydrogenase family.
Binds 1 zinc ion per subunit. At high pH manganese can replace zinc.
Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
PubMed:3533140 originally reported Cys-117 to be the active site. PubMed:8314784 has shown this to be wrong.
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.
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.
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).
Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.
Belongs to the complex I subunit 2 family.
Transfers a phosphoglycerol residue from phosphatidylglycerol to the membrane-bound nascent glucan backbones.
Belongs to the SecD/SecF family. SecD subfamily.
Forms a complex with SecF. Part of the essential Sec protein translocation apparatus which comprises SecA, SecYEG and auxiliary proteins SecDF-YajC and YidC.
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.
Once thought to be involved in copper homeostasis, experiments in E.coli have shown this is not the case.
Belongs to the BCCT transporter (TC 2.A.15) family. CaiT subfamily.
Catalyzes the exchange of L-carnitine for gamma-butyrobetaine.
The glycine cleavage system catalyzes the degradation of glycine.
The glycine cleavage system is composed of four proteins: P, T, L and H.
Belongs to the complex I 20 kDa subunit family.
NDH-1 is composed of 13 different subunits. Subunits NuoB, CD, E, F, and G constitute the peripheral sector of the complex.
By DNA damage, as part of the SOS response.
Component of the SOS system and an inhibitor of cell division. Accumulation of SulA causes rapid cessation of cell division and the appearance of long, non-septate filaments. In the presence of GTP, binds a polymerization-competent form of FtsZ in a 1:1 ratio, thus inhibiting FtsZ polymerization and therefore preventing it from participating in the assembly of the Z ring. This mechanism prevents the premature segregation of damaged DNA to daughter cells during cell division.
Is rapidly cleaved and degraded by the Lon protease once DNA damage is repaired.
Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
Forms a complex composed of PxpA, PxpB and PxpC.
Disruption of the gene results in a defective outer membrane barrier with elevated sensitivity to a range of compounds (PubMed:30201701). Mutant shows attenuated virulence in an oral infection model and during the early stages of systemic infection (PubMed:30201701). Loss of the gene does not have a global effect on outer membrane proteins, lipopolysaccharide or lipoprotein production, and does not impact adhesion, invasion or intracellular survival (PubMed:30201701).
Plays an important role in maintaining outer membrane integrity (PubMed:30201701). Contributes to virulence (PubMed:30201701).
Transcriptionally regulated by sigma-E factor.
This protein is an aporepressor. When complexed with L-tryptophan it binds the operator region of the trp operon (5'-ACTAGT-'3') and prevents the initiation of transcription. The complex also regulates trp repressor biosynthesis by binding to its regulatory region (By similarity).
Belongs to the IpgE/SigE chaperone family.
Molecular chaperone required for SopB/SigD stabilization and secretion.
Transcriptionally regulated by InvF and SicA. Also regulated by SirA.
Homododecamer composed of two hexameric rings; when bound to DNA in the presence of ATP and magnesium. Forms a complex with RuvA (By similarity).
The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing.
Belongs to the argininosuccinate synthase family. Type 2 subfamily.
Member of the two-component regulatory system TtrR/TtrS, which is required for synthesis of tetrathionate reductase. Probably functions as a sensor protein kinase which is autophosphorylated at a histidine residue in response to tetrathionate, and transfers its phosphate group to TtrR. During mice infection, the ability to use tetrathionate as an electron acceptor is a growth advantage for S.typhimurium over the competing microbiota in the lumen of the inflamed gut.
Mutants are defective in tetrathionate respiration.
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.
Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Involved in the translocation of the substrate across the membrane.
The complex is composed of two ATP-binding proteins (BtuD), two transmembrane proteins (BtuC) and a solute-binding protein (BtuF).
Required for invasion of epithelial cells. Could be involved in protein secretion.
Belongs to the outer membrane OOP (TC 1.B.6) superfamily. OmpA family.
Required for conjugation with F-type plasmids; probably serves as the mating receptor on recipient cells.
The extracellular loops are most variable in sequence, and in some bacteria confer sensitivity to phage and/or colicins.
With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm. Acts as a porin with low permeability that allows slow penetration of small solutes; an internal gate slows down solute passage.
Cells do not make BMCs, diol dehydratase is found in diffuse aggregates near the cell pole; it was later found this a double pduA-pduBB' deletion (PubMed:11844753). A single deletion forms larger than normal BMCs; it is not fully complemented by protein produced from a plasmid (PubMed:21239588, PubMed:27561553). Grows in an interrupted manner on 1,2-PD and vitamin B12; grows for a while then stops, then restarts as toxic propionaldehyde accumulates and then decreases (PubMed:11844753, PubMed:28585808, PubMed:21239588, PubMed:18296526, PubMed:33227310). Increased DNA mutagenesis, showing propionaldehyde is a mutagen (PubMed:18296526). Makes slightly larger BMCs; this phenotype can be rescued by PduA, but PduJ encoded on a plasmid cannot rescue a PduA deletion. When pduJ is cloned in the chromosomal position of pduA it substantially rescues the pduA deletion (PubMed:27561553, PubMed:33227310). Single pduA deletion makes BMCs but a double pduA-pduJ deletion does not (PubMed:33227310).
Homohexamer with a central pore of about 5.6 Angstroms in diameter. The hexamers pack against each other in arrays (PubMed:20870711, PubMed:24747050, Ref.22, PubMed:25713376). Interacts with the N-terminus of PduP which targets PduP to the BMC (PubMed:22927404). Modeling suggests PduC, PduD, PduE, PduL and PduP interact with a cleft formed by the C-terminal segments of 2 adjacent PduA subunits (on the BMC luminal side) in the hexamer (Probable).
One of the major shell proteins of the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation (PubMed:11844753, PubMed:21239588) (Probable). At least one of PduA or PduJ is required for BMC assembly; it must be encoded as the first gene in the pdu operon (PubMed:33227310, PubMed:27561553). Not required for structural integrity of BMCs, it is required to mitigate propionaldehyde toxicity (PubMed:21239588). Controls diffusion of 1,2-PD into and propionaldehyde out of the BMC shell; residue 40 is particularly important for pore permeability (PubMed:28585808, PubMed:25713376, PubMed:27561553) (Probable). Overexpression of this protein leads to aberrant filaments that extend the length of the cell, cross the cleavage furrow and impair division. The filaments form nanotubes with a hollow center (PubMed:11844753, PubMed:33227310). The isolated BMC shell component protein ratio for J:A:B':B:K:T:U is approximately 15:10:7:6:1:1:2 (PubMed:12923081). Edge residues (particularly Lys-26) are important for function and assembly of the BMC, and influence array formation by hexamers (PubMed:24747050). Interaction with PduA allows encapsulation of at least PduP in BMCs (PubMed:22927404). Probably also targets PduD to the BMC (Probable). PduA is probably the hub for binding multiple enzymes to the interior of the BMC; modeling suggests PduC, PduD, PduE, PduG, PduL and PduP are targeted to PduA (Probable).
The C-terminal 14 residues mediate binding to the N-terminus of PduP, which encapsulates PduP into BMCs.
The first gene in the pdu operon. BMC production is induced by growth on 1,2-PD vitamin B12 medium (PubMed:10498708, PubMed:26283792). No change when grown in the presence of 1,2-PD, ethanolamine and vitamin B12, suggesting it is possible for both the eut and pdu operons to be expressed at the same time (PubMed:26283792).
Upon overexpression and mixing of purified sheets with 2-ethyl-1-hexanol, will form closed shells. Enzymes (tested with endogenous BMC enzyme DDH and the peroxidase activity of cytC) can be encapsulated in the shells; the enzyme is active in the shells. The shells are permeable to a variety of compounds, showing they could be used to make protein based synthetic bioreactors.
Multifunctional regulator of fatty acid metabolism. Represses transcription of at least eight genes required for fatty acid transport and beta-oxidation including fadA, fadB, fadD, fadL and fadE. Activates transcription of at least three genes required for unsaturated fatty acid biosynthesis: fabA, fabB and iclR, the gene encoding the transcriptional regulator of the aceBAK operon encoding the glyoxylate shunt enzymes. Binding of FadR is specifically inhibited by long chain fatty acyl-CoA compounds (By similarity).
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 (By similarity). A ribosome-stimulated GTPase, GTPase activity increases 4 fold in the presence of 70S ribosomes. Bind to 70S ribosomes in the presence of GTP or its non-hydrolyzable analog GMPPNP; in the presence of ppGpp or under stress conditions it binds to 30S ribosomal subunits (PubMed:18621905, PubMed:19803466).
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. BipA subfamily.
Has 5 domains; domain I (residues 1-202, also called the G domain), II (203-305, also called the beta barrel domain), III (306-386) V (387-479) and the C-terminal domain (CTD 480-607) which is BipA-specific. Domains I-V are homologous to domains in EF-G and LepA; although the domains are similar, their relative arrangement among these proteins is different. Domains I and II are not required for ribosome binding, although in their absence no 30S binding under stress is seen, whereas domains III, V and the CTD are required to bind both 70S and 30S ribosomes. The data suggests interdomain communication modulates GTPase and ribosome binding.
Induced 7-fold when cells are treated with human bactericidal permeability-increasing protein (BPI, AC P17213) (at protein level).
Ribosome-associated GTPase is not affected by low levels of ppGpp, >40 uM ppGpp and >50 uM GDP inhibit GTPase (PubMed:18621905). The C-terminus (residues 387-607 or 481-607) inhibits GTPase activity, in its absence kcat increases, but GTPase is no longer stimulated by 70S ribosome or 30S or 50S subunits (PubMed:19803466).
Belongs to the sigma-70 factor family. ECF subfamily.
ECF sigma-E is held in an inactive form by its cognate anti-sigma factor (RseA) until released by regulated intramembrane proteolysis (RIP). RIP occurs when an extracytoplasmic signal (periplasmic stress and excess LPS) triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The anti-sigma factor RseA is an inner membrane protein, binding sigma-E in the cytoplasm and RseB in the periplasm. RseA is first cut extracytoplasmically (site-1 protease, S1P, by DegS), then within the membrane itself (site-2 protease, S2P, by RseP), while cytoplasmic proteases (predominantly ClpX-ClpP) finish degrading the regulatory protein, liberating sigma-E. Degradation of RseA requires 2 signals to activate DegS; an outer membrane protein (OMP) signal activates DegS, while an LPS signal causes release of RseB from RseA, freeing RseA to be cleaved (By similarity).
Interacts transiently with the RNAP catalytic core formed by RpoA, RpoB, RpoC and RpoZ (2 alpha, 1 beta, 1 beta' and 1 omega subunit) to form the RNAP holoenzyme that can initiate transcription. Interacts 1:1 with anti-sigma-E factor RseA which prevents binding to RNAP catalytic core (By similarity).
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-E controls the envelope stress response, responding to periplasmic protein stress, increased levels of periplasmic lipopolysaccharide (LPS) as well as acid stress, heat shock and oxidative stress; it controls protein processing in the extracytoplasmic compartment (By similarity).
The sigma-70 factor domain-2 mediates sequence-specific interaction with the -10 element in promoter DNA, and plays an important role in melting the double-stranded DNA and the formation of the transcription bubble. The sigma-70 factor domain-2 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. The domain also mediates interaction with the RNA polymerase subunit RpoA. Interactions between sigma-70 factor domain-4 and anti-sigma factors prevents interaction of sigma factors with the RNA polymerase catalytic core (By similarity).
Belongs to the threonine synthase family.
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.
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. Component of the ClpAP and ClpXP complexes.
Belongs to the 6-phosphogluconate dehydrogenase family.
Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH.
Belongs to the tellurite-resistance/dicarboxylate transporter (TDT) family.
Belongs to the shaker potassium channel beta subunit family.
Belongs to the PPP phosphatase family. PP-1 subfamily.
Can hydrolyze phosphorylated Ser-, Thr- or Tyr-substrates in vitro. The natural substrate is unknown.
Inhibited by cadmium, copper, zinc when added activity but with less efficiency.
Neither magnesium nor calcium stimulates activity.
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 (By similarity).
Probably formed by programmed ribosomal frameshifting to a premature stop codon in the -1 frame at codon 430.
Produced by full-length translation of the dnaX gene.
Seems to interact with the delta subunit to transfer the beta subunit on the DNA.
Serves as a scaffold to help in the dimerization of the core complex.
The DNA polymerase holoenzyme is a complex that contains 10 different types of subunits. These subunits are organized into 3 functionally essential subassemblies: the pol III core, the beta sliding clamp processivity factor and the clamp-loading complex. The pol III core (subunits alpha, epsilon and theta) contains the polymerase and the 3'-5' exonuclease proofreading activities. The polymerase is tethered to the template via the sliding clamp processivity factor. The clamp-loading complex assembles the beta processivity factor onto the primer template and plays a central role in the organization and communication at the replication fork. This complex contains delta, delta', psi and chi, and copies of either or both of two different DnaX proteins, gamma and tau. The composition of the holoenzyme is, therefore: (alpha,epsilon,theta)[2]-(isoform:gamma/tau)[3]-delta,delta', psi,chi-beta[4] (By similarity).
Belongs to the galactose-1-phosphate uridylyltransferase type 1 family.
Binds 1 zinc ion per subunit. Zinc binding seems to play a structural role.
In vitro catalyzes the addition of water to fumarate, forming malate. Cannot catalyze the reverse reaction. Cannot use the cis-isomer maleate as substrate.
Belongs to the bacterial histone-like protein family.
Histone-like DNA-binding protein which is capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions.
Accepts electrons from ETF and reduces ubiquinone.
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. PhnW subfamily.
The crystal structure does not show the Schiff base that is expected to form between Lys-194 and the pyridoxal phosphate cofactor.
Thr-243 of one partner binds the pyridoxal phosphate moiety of the other.
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.
Belongs to the glycosyl hydrolase 4 family.
Methylated by PrmC. Methylation increases the termination efficiency of RF2 (By similarity).
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-25; a naturally occurring frameshift enables complete translation of RF-2. This provides a mechanism for the protein to regulate its own production.
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. May be involved in a specialized protein export pathway that proceeds without signal peptide cleavage.
Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues.
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.
Negatively regulates its own expression and that of the subsequent genes in the proximal part of the division and cell wall (dcw) gene cluster. Acts by binding directly to DNA. May also regulate the expression of genes outside the dcw cluster.
Belongs to the enoyl-CoA hydratase/isomerase family.
Catalyzes the reversible dehydration of L-carnitinyl-CoA to crotonobetainyl-CoA.
Repressor of the mgl operon. Binds galactose and D-fucose as inducers. GalS binds to an operator DNA sequence within its own coding sequence (By similarity).
Belongs to the amino acid-polyamine-organocation (APC) superfamily. Amino acid transporter (AAT) (TC 2.A.3.1) family.
Permease that is involved in the active transport across the cytoplasmic membrane of all three aromatic amino acids, phenylalanine, tyrosine and tryptophan.
Belongs to the arylamine N-acetyltransferase family.
Catalyzes both the acetyl-CoA-dependent N-acetylation of aromatic amines and the O-acetylation of N-hydroxyarylamines. In vitro, catalyzes the O-acetylation of N-hydroxy-Glu-P-1, and the N-acetylation of isoniazid and 2-aminofluorene.
Inhibited by N-ethylmaleimide and iodoacetamide.
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.
Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Prokaryotic type I sub-subfamily.
Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
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.
Seems to associate with BFR; could be a general redox and/or regulatory component participating in the iron storage mobilization functions of BFR. Could participate in the release or the delivery of iron from/to bacterioferritin (or other iron complexes) (By similarity).
Forms an energy-coupling factor (ECF) transporter complex composed of an ATP-binding protein (A component, CbiO), a transmembrane protein (T component, CbiQ) and 2 possible substrate-capture proteins (S components, CbiM and CbiN) of unknown stoichimetry. Expression of just CbiMN in E.coli confers some cobalt uptake.
Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import. The complex confers cobalt uptake upon expression in E.coli; can also transport nickel with a very low affinity.
Belongs to the ABC-4 integral membrane protein family. FtsX subfamily.
Forms a membrane-associated complex with FtsE.
Part of the ABC transporter FtsEX involved in cellular division.
Belongs to the archaeal-type GPI family.
Belongs to the class I-like SAM-binding methyltransferase superfamily. MenG/UbiE family.
Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
Belongs to the aldehyde dehydrogenase family. AstD subfamily.
Catalyzes the NAD-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Belongs to the anaerobic coproporphyrinogen-III oxidase family.
Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Cells lacking this gene accumulate coproporphyrinogen III under anaerobic conditions.
Involved in the heme biosynthesis. Catalyzes the anaerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen III to yield the vinyl groups in protoporphyrinogen IX.
Monomer and homodimer. Part of the essential Sec protein translocation apparatus which comprises SecA, SecYEG and auxiliary proteins SecDF-YajC and YidC.
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 both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Repressed under conditions of excess protein secretion capacity and derepressed when protein secretion becomes limiting. This is regulated by SecM.
Belongs to the bacterial solute-binding protein ModA family.
External glucose-6-phosphate induces the expression of the UHP-region.
Mediates the exchange of external hexose 6-phosphate and internal inorganic phosphate.
May play a specific role in the degradation of signal peptides after they are released from precursor forms of secreted proteins. Can cleave N-acetyl-L-Ala(4).
Belongs to the gamma-glutamyltransferase family.
Cleaved by autocatalysis into a large and a small subunit.
This enzyme consists of two polypeptide chains, which are synthesized in precursor form from a single polypeptide.
Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens conductance with a slight preference for anions.
Adds the terminal N-acetyl-D-glucosamine group on the glucose(II) group of LPS.
Belongs to the cation diffusion facilitator (CDF) transporter (TC 2.A.4) family. SLC30A subfamily.
Involved in zinc efflux across the cytoplasmic membrane, thus reducing zinc accumulation in the cytoplasm and rendering bacteria more resistant to zinc. It may contribute to zinc homeostasis at low concentrations of zinc.
Part of the binding-protein-dependent transport system for molybdenum; probably responsible for the translocation of the substrate across the membrane.
Involved in the triggering of intracellular events that lead to microbial internalization. These events include increase in calcium level, redistribution of actin microfilaments, and changes in the normal structure of the microvilli. Encoded within the type III secretion system (SPI-1 TTSS), it is essential for the translocation of protein effectors into host cells. Forms a complex with SipB and SipC in the presence of their chaperone SicA. Positively regulates the secretion of SPI-1 TTSS effector proteins SipB, SipC and SipD and negatively influences the secretion of SipA, SopA and SptP.
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).
Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB (By similarity).
Belongs to the bacterial ribosomal protein bS6 family.
Binds together with S18 to 16S ribosomal RNA.
Associates exclusively with 100S ribosomes.
Belongs to the ribosome modulation factor family.
During stationary phase, converts 70S ribosomes to an inactive dimeric form (100S ribosomes). May form immature 90S particles, which are converted to mature 100S ribosomes by the hibernation promoting factor Hpf.
Belongs to the drug/metabolite transporter (DMT) superfamily. Small multidrug resistance (SMR) (TC 2.A.7.1) family. MdtJ subfamily.
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.
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 class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily.
Deacetylates O-acetyl-ADP ribose to yield ADP-ribose and free acetate. Down-regulates ribonuclease 3 (RNase III) activity. Acts by interacting directly with the region of the ribonuclease that is required for dimerization/activation.
Cells lacking this gene are unable to accumulate propionyl-CoA.
Homodimer at low concentrations and converted to a larger oligomers at higher concentrations.
Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the Claisen condensation of propionyl-CoA and oxaloacetate (OAA) to yield 2-methylcitrate (2-MC) and CoA. Also catalyzes the condensation of oxaloacetate with acetyl-CoA or butyryl-CoA but with a lower specificity.
In the C-terminal section; belongs to the homoserine dehydrogenase family.
In the N-terminal section; belongs to the aspartokinase family.
Interacts with CbpA and inhibits both the DnaJ-like co-chaperone activity and the DNA binding activity of CbpA. Together with CbpA, modulates the activity of the DnaK chaperone system. Does not inhibit the co-chaperone activity of DnaJ.
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. Forms a bridge to the 30S subunit in the 70S ribosome.
Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily.
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.
In contrast to other thiamine biosynthetic genes, thiL is not transcriptionally regulated by thiamine-pyrophosphate. Appears to be constitutively expressed.
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.
Autophosphorylated; GrpE inhibits the autophosphorylation.
By stress conditions e.g. heat shock (By similarity).
Belongs to the outer membrane factor (OMF) (TC 1.B.17) family.
Belongs to the purine-cytosine permease (2.A.39) family.
Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. Does not appear to be required for the formation or the maintenance of either Salmonella-containing vacuole (SCV) or the Salmonella-induced filaments (Sifs). Not required for intracellular replication in phagocytic cells.
Expression is regulated by the two-component regulatory system SsrA/SsrB. Induced after bacterial entry into host cell.
Degradation of inorganic polyphosphates (polyP). Releases orthophosphate processively from the ends of the polyP chain.
Belongs to the P-Pant transferase superfamily. AcpS family.
Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Murein-degrading enzyme. Catalyzes the cleavage of the glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine residues in peptidoglycan. May play a role in recycling of muropeptides during cell elongation and/or cell division (By similarity).
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 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.
Transcription factor that regulates the expression of several genes involved in the transport and metabolism of L-arabinose.
Belongs to the major facilitator superfamily. TCR/Tet family.
Major efflux pump for acriflavine and other quaternary ammonium compounds (QACs). Also required for resistance to methyl viologen (By similarity).
Responsible for the coupling of flagellin expression to flagellar assembly by preventing expression of the flagellin genes when a component of the middle class of proteins is defective. It negatively regulates flagellar genes by inhibiting the activity of FliA by directly binding to FliA.
The N-terminal domain is essential for export and the C-terminal domain possess the FliA binding site.
Belongs to the elongation factor P family.
Adds the glucose(II) group on the galactose(I) group of LPS.
Belongs to the uroporphyrinogen-III synthase family.
Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
Belongs to the 4-toluene sulfonate uptake permease (TSUP) (TC 2.A.102) family.
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.
Belongs to the phosphoglycerate mutase family. GpmB subfamily.
Homodimer. Forms a membrane-associated complex with FtsX.
Part of the ABC transporter FtsEX involved in cellular division. Important for assembly or stability of the septal ring.
Catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to formate and tetrahydrofolate (FH4).
Belongs to the SIS family. DiaA subfamily.
Required for the timely initiation of chromosomal replication via direct interactions with the DnaA initiator protein.
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(+).
Belongs to the phosphoethanolamine transferase family. EptB subfamily.
Catalyzes the addition of a phosphoethanolamine (pEtN) moiety to the outer 3-deoxy-D-manno-octulosonic acid (Kdo) residue of a Kdo(2)-lipid A. Phosphatidylethanolamines with one unsaturated acyl group functions as pEtN donors and the reaction releases diacylglycerol.
Permease that is involved in the transport across the cytoplasmic membrane of proline.
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.
Belongs to the methyltransferase superfamily.
Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
Cells lacking this gene show no phenotype during growth on propionate, acetate, succinate, glycerol and glucose. The acnAB double mutant does not grow on propionate even when supplemented with glutamate and is unable to respire propionate under anaerobic growth conditions.
Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. Also catalyzes the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate. The (2S,3S)-2-methylcitrate (2-MC) is a very poor substrate (PubMed:11294638). The apo form of AcnA functions as a RNA-binding regulatory protein (By similarity).
Belongs to the HypA/HybF family. HybF subfamily.
Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase.
Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis.
Belongs to the GTP cyclohydrolase II family.
Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.
Belongs to the protein N5-glutamine methyltransferase family. PrmB subfamily.
Specifically methylates the 50S ribosomal protein L3 on 'Gln-150'.
Belongs to the ETF alpha-subunit/FixB family.
Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
Belongs to the complex I 23 kDa subunit family.
Belongs to the CDP-alcohol phosphatidyltransferase class-II family.
Belongs to the rhamnose mutarotase family.
Involved in the anomeric conversion of L-rhamnose.
Belongs to the aldehyde dehydrogenase family.
Decreased propionate kinase activity, cells grow to lower density on 1,2-PD and excrete more propionate into the medium (PubMed:12700259). A double acs-pta deletion excretes but no longer recpautres acetate (PubMed:16272400).
In the C-terminal section; belongs to the phosphate acetyltransferase and butyryltransferase family.
In the N-terminal section; belongs to the CobB/CobQ family.
Involved in acetate metabolism. Catalyzes the reversible interconversion of acetyl-CoA and acetyl phosphate. The direction of the overall reaction changes depending on growth conditions. Required for acetate recapture but not for acetate excretion when this organism is grown on ethanolamine (EA); is unable to complement an eutD deletion during growth on EA (PubMed:16272400). Works with proprionate kinase PduW to capture exogenous propionate and regenerate propionyl-CoA during degradation of propionate and 1,2-propanediol (1,2-PD) (PubMed:12700259).
The N-terminal region seems to be important for proper quaternary structure. The C-terminal region contains the substrate-binding site (By similarity).
Belongs to the FPP/GGPP synthase family.
Belongs to the invasin protein D family.
Required for translocation of effector proteins via the type III secretion system SPI-1, which is essential for an efficient bacterial internalization. Probably acts by modulating the secretion of SipA, SipB, and SipC.
The N-terminal domain is an intra-molecular chaperone that prevents premature oligomerization of the residues on the coiled-coil region that are involved in interactions with the needle and/or itself. The residues in the C-terminal domain probably form oligomeric structures at the tip of the needle that are responsible for the regulation of secretion of other effectors (By similarity).
Transcriptionally regulated by SicA and InvF. Also regulated by InvE.
Mediates a global response to leucine. Exogenous leucine affects the expression of a number of different operons; lrp mediates this effect for at least some of these operons. For example it is regulator of the branched-chain amino acid transport genes.
Belongs to the uroporphyrinogen decarboxylase family.
Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Activates the transcription of the soxS gene which itself controls the superoxide response regulon. SoxR contains a 2Fe-2S iron-sulfur cluster that may act as a redox sensor system that recognizes superoxide. The variable redox state of the Fe-S cluster is employed in vivo to modulate the transcriptional activity of SoxR in response to specific types of oxidative stress (By similarity).
Required for anaerobic carnitine reduction. May bring reductant to CaiA.
Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine.
In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.
Belongs to the methyltransferase superfamily. RsmD family.
Specifically methylates the guanine in position 966 of 16S rRNA in the assembled 30S particle.
Acts as a receptor for citrate and mediates taxis away from phenol. Also mediates an attractant response to metal-citrate complexes.
Methylation level is increased by citrate and decreased by phenol.
Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
An FAD assembly protein, which accelerates covalent attachment of the cofactor into other proteins. Plays an essential role in the assembly of succinate dehydrogenase (SDH, respiratory complex II), an enzyme complex that is a component of both the tricarboxylic acid cycle and the electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Required for flavinylation (covalent attachment of FAD) of the flavoprotein subunit SdhA of SDH and other flavinylated proteins as well.
Belongs to the SdhE FAD assembly factor family.
10,000-fold reduction in virulence in male BALB/c mice (for strain ATCC 14028). Decreased tolerance to acid stress.
Member of the two-component regulatory system PhoP/PhoQ which regulates the expression of genes involved in virulence, adaptation to acidic and low Mg(2+) environments and resistance to host defense antimicrobial peptides (PubMed:2544889, PubMed:9573193, PubMed:25972862). Essential for intramacrophage survival of S.typhimurium. In low periplasmic Mg(2+), PhoQ phosphorylates PhoP, resulting in the expression of PhoP-activated genes (PAG) and repression of PhoP-repressed genes (PRG). In high periplasmic Mg(2+), PhoQ dephosphorylates phospho-PhoP, resulting in the repression of PAG and may lead to expression of some PRG. Essential for transcription of spiC inside macrophages by controlling the expression of the two-component regulatory system SsrB/SpiR (SsrA) and Pir at transcriptional and post-transcriptional levels respectively. Promotes expression of the two-component regulatory system PmrA/PmrB via activation of pmrD gene. Is required to attenuate bacterial growth within fibroblast cells and to enhance bacterial resistance to bile in intestinal cells. Negatively regulates prgH, which is required for invasion of epithelial cells. PhoP uses multiple mechanisms to promote transcription and activates promoters for PAG at low (uM range) Mg(2+) concentrations (Probable). Involved in acid tolerance.
Monomer in the inactive, unphosphorylated state and dimer in the active, phosphorylated state.
PhoP/PhoQ-signaling cascade, which activates virulence membrane proteins (PagC, PagO, PagD, PagK, PgtE and PhoN), is induced by cationic antimicrobial peptides (CAMP) (polymyxin, alpha-helical peptide C18G and sheet peptide protegrin-1) at sublethal concentrations.
Phosphorylated and dephosphorylated by PhoQ.
The phoP/phoQ operon is positively autoregulated by both PhoP and PhoQ in a Mg(2+)-dependent manner. Repressed by RcsB via sigma factor RpoS.
Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit.
Reduces trimethylamine-N-oxide (TMAO) into trimethylamine; an anaerobic reaction coupled to energy-yielding reactions.
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 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 or 10-formyltetrahydrofolate or 5,10-methylenetetrahydrofolate, leading to folylpolyglutamate derivatives.
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 (By similarity).
Belongs to the glycosyltransferase 20 family.
Probably involved in the osmoprotection via the biosynthesis of trehalose. Catalyzes the transfer of glucose from UDP-alpha-D-glucose (UDP-Glc) to D-glucose 6-phosphate (Glc-6-P) to form trehalose-6-phosphate. Acts with retention of the anomeric configuration of the UDP-sugar donor.
Belongs to the pyridoxine kinase family. PdxY subfamily.
Pyridoxal kinase involved in the salvage pathway of pyridoxal 5'-phosphate (PLP). Catalyzes the phosphorylation of pyridoxal to PLP.
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 helicase family. RecQ subfamily.
Involved in the RecF recombination pathway; its gene expression is under the regulation of the SOS system. It is a DNA helicase.
Monomer. Binds directly to the core enzyme of the DNA-dependent RNA polymerase and to nascent RNA.
Participates in both transcription termination and antitermination.
Belongs to the CDP-alcohol phosphatidyltransferase class-I family.
This protein catalyzes the committed step to the synthesis of the acidic phospholipids.
Required for the expression of anaerobic nitric oxide (NO) reductase, acts as a transcriptional activator for at least the norVW operon. Activation also requires sigma-54.
Belongs to the disproportionating enzyme family.
The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing some disulfides in a coupled system with glutathione reductase (By similarity).
Belongs to the UbiX/PAD1 family. YclB subfamily.
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.
Belongs to the mandelate racemase/muconate lactonizing enzyme family. GlucD subfamily.
Belongs to the isochorismate synthase family.
Binds RpoD and negatively regulates RpoD-mediated transcription activation by preventing the interaction between the primary sigma factor RpoD with the catalytic core of the RNA polymerase and with promoter DNA. May be involved in replacement of the RNA polymerase sigma subunit from RpoD to RpoS during the transition from exponential growth to the stationary phase.
The SPOR domain binds septal peptidoglycans and is required to target DamX to the septal ring.
A non-essential division protein that localizes to the septal ring in low ionic strength medium.
Belongs to the DNA polymerase type-B family.
Part of a membrane-bound tetrathionate reductase that catalyzes the reduction of tetrathionate to thiosulfate. TtrA is the catalytic subunit. During mice infection, the ability to use tetrathionate as an electron acceptor is a growth advantage for S.typhimurium over the competing microbiota in the lumen of the inflamed gut.
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.
Catalyzes the deamination of dCTP to dUTP.
Belongs to the HAD-like hydrolase superfamily. MPGP family.
Functions in complex with FlhD as a master transcriptional regulator that regulates transcription of several flagellar and non-flagellar operons by binding to their promoter region. Activates expression of class 2 flagellar genes, including fliA, which is a flagellum-specific sigma factor that turns on the class 3 genes. Also regulates genes whose products function in a variety of physiological pathways (Probable).
Heterohexamer composed of two FlhC and four FlhD subunits. Each FlhC binds a FlhD dimer, forming a heterotrimer, and a hexamer assembles by dimerization of two heterotrimers (Probable). YdiV binds to FlhD which inhibits the ability of FlhC(2)FlhD(4) to bind DNA.
Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
Belongs to the Nudix hydrolase family. NudI subfamily.
Catalyzes the hydrolysis of nucleoside triphosphates, with a preference for pyrimidine deoxynucleoside triphosphates (dUTP, dTTP and dCTP).
Belongs to the adrenodoxin/putidaredoxin family.
Catalyzes the hydrolysis of 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) to 3-deoxy-D-manno-octulosonate (KDO) and inorganic phosphate.
In the N-terminal section; belongs to the FGAMS family.
Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate.
Belongs to the transaldolase family. Type 3A subfamily.
Catalyzes the reversible formation of fructose 6-phosphate from dihydroxyacetone and D-glyceraldehyde 3-phosphate via an aldolization reaction.
Belongs to the SUA5 family. TsaC subfamily.
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.
Belongs to the HpcH/HpaI aldolase family.
Catalyzes the reversible retro-aldol cleavage of 4-hydroxy-2-ketoheptane-1,7-dioate (HKHD) to pyruvate and succinic semialdehyde.
Belongs to the nucleoside phosphorylase PpnP family.
Catalyzes the phosphorolysis of diverse nucleosides, yielding D-ribose 1-phosphate and the respective free bases. Can use uridine, adenosine, guanosine, cytidine, thymidine, inosine and xanthosine as substrates. Also catalyzes the reverse reactions.
Belongs to the methyltransferase superfamily. tRNA (adenine-N(6)-)-methyltransferase family.
Specifically methylates the adenine in position 37 of tRNA(1)(Val) (anticodon cmo5UAC).
Belongs to the RNase E/G family. RNase E subfamily.
Belongs to the RNase E/G family. RNase G subfamily.
Component of the RNA degradosome, which is a multiprotein complex involved in RNA processing and mRNA degradation. Within the RNA degradosome, RNase E assembles into a homotetramer formed by a dimer of dimers.
Endoribonuclease that plays a central role in RNA processing and decay. Required for the maturation of 5S and 16S rRNAs and the majority of tRNAs. Also involved in the degradation of most mRNAs.
A protein that aids in conversion of cob(III)alamin to cob(II)alamin and then to cob(I)alamin in the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation (PubMed:15817784, PubMed:20656910). The latter step requires PduO. No free cob(I)alamin is released, suggesting a complex is formed with PduO that finishes conversion to adenosylcobalamin. PduS and PduO allow regeneration of the adenosylcobalamin cofactor within the BMC (PubMed:15817784). Another study showed reduction of cob(II)alamin to cob(I)alamin in the absence of PduO. Both reactions require NADH. Cyanocobalamin (CN-Cbl) is not a substrate for the first reaction (PubMed:20656910). Cobalamin reduction probably occurs spontaneously in the presence of free reduced flavin nucleotides, this protein may be involved in electron transfer for this reduction (Probable).
Belongs to the PduS cobalamin reductase family.
Binds 2 [4Fe-4S] clusters (By similarity). The two centers are coupled but must possess different redox potentials (By similarity).
Binds one FMN non-covalently per monomer.
Grows more slowly and to a lower cell density than wild-type.
Monomeric when purified anaerobically, dimeric under aerobic conditions (PubMed:20656910). Forms a complex with PduO (PubMed:15817784, PubMed:20656910). Interacts with PduT, probably via the N-terminus of PduS (By similarity).
Required for PgtP expression, it may act jointly with the PgtA/PgtB signaling proteins.
Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. GhrB subfamily.
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 phosphoethanolamine transferase family. EptA subfamily.
Catalyzes the addition of a phosphoethanolamine moiety to the lipid A. The phosphoethanolamine modification is required for resistance to polymyxin.
Belongs to the manganese catalase family.
Controls both the activation and catalytic activity of PanD in a coenzyme A (CoA)-dependent fashion (By similarity). Binding of CoA or a derivative to PanM leads to interaction with PanD, which promotes the processing and activation of pro-PanD, and subsequent substrate-mediated inhibition of the active form of PanD (By similarity) (PubMed:22497218, PubMed:22782525). Lacks acetyltransferase activity (PubMed:22782525).
Deletion results in a pantothenate auxotrophy. Deletion mutant accumulates pro-PanD.
Interacts with PanD in the presence of CoA (PubMed:22497218, PubMed:22782525). Monomer (PubMed:22497218).
Lacks the conserved catalytic glutamate found in many enzymatically active members of the Gcn5-like N-acetyltransferase (GNAT) family.
Component of the Rcs signaling system, which controls transcription of numerous genes. RcsB is the response regulator that binds to regulatory DNA regions. Can function both in an RcsA-dependent or RcsA-independent manner.
Binds to the N-terminal domain of the chaperone ClpA.
Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation.
Part of the cysteine synthase complex formed at a ratio of 1 copy of this protein and 2 copies of O-acetylserine sulfhydrylase (cysK). The complex reversibly dissociates in the presence of O-acetyl-L-serine in the absence of hydrogen sulfide.
Sensitive to feedback inhibition by L-cysteine.
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.
Belongs to the NiCoT transporter (TC 2.A.52) family. RcnA subfamily.
Forms pores that allow passive diffusion of small molecules across the outer membrane.
Belongs to the ATPase delta chain family.
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.
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.
Catalyzes the synthesis of GMP from XMP.
Specifically methylates the adenine in position 2030 of 23S rRNA.
Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Heptose transfer to the lipopolysaccharide core. It transfers the innermost heptose to [4'-P](3-deoxy-D-manno-octulosonic acid)2-IVA.
This protein is involved in control of the biosynthesis of tryptophan.
Autocleaved. Generates the alpha and beta subunits. The beta subunit is thought to be responsible for the nucleophile hydrolase activity.
Degrades proteins damaged by L-isoaspartyl residue formation (also known as beta-Asp residues). Degrades L-isoaspartyl-containing di- and tripeptides. Acts best on iso-Asp-Leu, followed by iso-Asp-Ala, -His and to a lesser extent iso-Asp-Lys, -Phe and iso-Asp-Leu-Ala. Does not act on internal iso-Asp bonds (Als-iso-Asp-Leu-Ala). Does not act on alpha-Asp bonds. Has poor L-asparaginase activity.
Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers.
By elevated osmotic pressure in the growth medium.
Provides resistance to osmotic stress. May be important for stationary-phase survival (By similarity).
Activator of the cell wall hydrolase AmiC. Required for septal murein cleavage and daughter cell separation during cell division (By similarity).
Belongs to the E.coli NlpD/Haemophilus LppB 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)).
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.
Part of the 30S ribosomal subunit. Contacts proteins S3 and S10.
Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.
Repressor of rcnA expression. Acts by binding specifically to the rcnA promoter in the absence of nickel and cobalt. In the presence of one of these metals, it has a weaker affinity for rcnA promoter (By similarity).
Catalyzes the transfer of laurate from lauroyl-acyl carrier protein (ACP) to Kdo(2)-lipid IV(A) to form Kdo(2)-(lauroyl)-lipid IV(A).
Belongs to the Fe(2+)-trafficking protein family.
Could be a mediator in iron transactions between iron acquisition and iron-requiring processes, such as synthesis and/or repair of Fe-S clusters in biosynthetic enzymes. Necessary to maintain high levels of aconitase under oxidative stress.
Part of the binding-protein-dependent transport system for oligopeptides; probably responsible for the translocation of the substrate across the membrane.
Does not bind DNA by a helix-turn-helix motif.
This regulatory protein, when combined with SAM (S-adenosylmethionine) represses the expression of the methionine regulon and of enzymes involved in SAM synthesis. It is also autoregulated (By similarity).
High affinity, high specificity proton-dependent sulfate transporter, which mediates sulfate uptake. Provides the sulfur source for the cysteine synthesis pathway.
Belongs to the glycosyl hydrolase 8 (cellulase D) family.
Catalyzes the conversion of chorismate to isochorismate.
Belongs to the protease inhibitor I11 (ecotin) family.
General inhibitor of pancreatic serine proteases: inhibits chymotrypsin, trypsin, elastases, factor X, kallikrein as well as a variety of other proteases.
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.
Belongs to the FNT transporter (TC 2.A.44) family.
Catalyzes nitrite uptake and nitrite export across the cytoplasmic membrane.
Component of the Rcs signaling system, which controls transcription of numerous genes. RcsD is a phosphotransfer intermediate between the sensor kinase RcsC and the response regulator RcsB. It acquires a phosphoryl group from RcsC and transfers it to RcsB.
Has been proposed to be a redox modulator.
Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
The subtype gamma methyltransferase (M) subunit of a type I restriction enzyme. The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues of the sequence 5'-GAGN(6)GTRC-3'. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance MTase modifying the DNA so that both strands become methylated. After locating a non-methylated recognition site, the enzyme complex serves as a molecular motor that translocates DNA in an ATP-dependent manner until a collision occurs that triggers cleavage.
The type I restriction/modification system is composed of three polypeptides R, M and S; the restriction enzyme has stoichiometry R(2)M(2)S(1) while the methyltransferase is M(2)S(1).
Type I restriction and modification enzymes are complex, multifunctional systems which require ATP, S-adenosyl methionine and Mg(2+) as cofactors and, in addition to their endonucleolytic and methylase activities, are potent DNA-dependent ATPases.
Belongs to the LpxT phosphotransferase family.
Involved in the modification of the lipid A domain of lipopolysaccharides (LPS). Transfers a phosphate group from undecaprenyl pyrophosphate (C55-PP) to lipid A to form lipid A 1-diphosphate. Contributes to the recycling of undecaprenyl phosphate (C55-P).
Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+).
Binds 1 thiamine pyrophosphate per subunit.
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.
Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step in folate biosynthesis pathway.
Belongs to the inorganic phosphate transporter (PiT) (TC 2.A.20) family. Pit subfamily.
Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. Is the first of four enzymes commited to biosynthesis of dTDP-L-rhamnose in S.typhimurium LT2. Is also able to convert non natural substrates such as a wide array of alpha-D-hexopyranosyl, deoxy-alpha-D-glucopyranosyl, aminodeoxy-alpha-D-hexopyranosyl and acetamidodeoxy-alpha-D-hexopyranosyl phosphates to their corresponding dTDP- and UDP-nucleotide sugars.
The position of the magnesium ion observed in the crystallographic structure is different from that observed in the structure of E.coli RmlA2 (RffH) and does not seem to correspond to the binding site for the catalytically essential magnesium ion. Therefore, we choose to propagate in the feature lines the positions found in the E.coli structure.
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.
Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. TolB occupies a key intermediary position in the Tol-Pal system because it communicates directly with both membrane-embedded components, Pal in the outer membrane and TolA in the inner membrane.
The Tol-Pal system is composed of five core proteins: the inner membrane proteins TolA, TolQ and TolR, the periplasmic protein TolB and the outer membrane protein Pal. They form a network linking the inner and outer membranes and the peptidoglycan layer.
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.
May link the O-antigen tetrasaccharide units into long chains, giving rise to typical smooth LPS.
Belongs to the ABC transporter superfamily. Methionine importer (TC 3.A.1.24) family.
Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
The complex is composed of two ATP-binding proteins (MetN), two transmembrane proteins (MetI) and a solute-binding protein (MetQ).
Essential for cellulose biosynthesis. May play a role in subcellular localization of an active cellulose biosynthesis apparatus at the bacterial cell pole (By similarity).
Belongs to the acetokinase family. TdcD subfamily.
Catalyzes the conversion of propionyl phosphate and ADP to propionate and ATP. It can also use acetyl phosphate as phosphate group acceptor.
Belongs to the phage portal family. PBSX subfamily.
Belongs to the iron/manganese superoxide dismutase family.
Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Belongs to the NAD(P)H dehydrogenase (quinone) family. KefG subfamily.
Regulatory subunit of a potassium efflux system that confers protection against electrophiles. Required for full activity of KefB.
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 RNase Z family. RNase BN subfamily.
Zinc phosphodiesterase, which has both exoribonuclease and endoribonuclease activities.
A triple pduC-pduD-pduE deletion releases no acetaldehyde when grown on propanediol.
Belongs to the diol/glycerol dehydratase small subunit family.
Part of the PduCDE complex that catalyzes the dehydration of 1,2-propanediol (1,2-PD) to propionaldehyde. Required for S.typhimurium growth on 1,2-PD as the sole carbon and energy source. Localized in the bacterial microcompartment (BMC) dedicated to 1,2-PD degradation.
Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.
Individual Salmonella serotypes usually alternate between the production of 2 antigenic forms of flagella, termed phase 1 and phase 2, each specified by separate structural genes.
Belongs to the OXA1/ALB3/YidC family. Type 1 subfamily.
Interacts with the Sec translocase complex via SecD. Specifically interacts with transmembrane segments of nascent integral membrane proteins during membrane integration.
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. Aids folding of multispanning membrane proteins.
Repressor of the marRAB operon which is involved in the activation of both antibiotic resistance and oxidative stress genes. Binds to the marO operator/promoter site.
Belongs to the ribose 5-phosphate isomerase family.
Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
Involved in the degradation of certain denaturated proteins, including DnaA, during heat shock stress.
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.
Belongs to the NAD-dependent DNA ligase family. LigB subfamily.
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.
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. Contacts protein L29, and trigger factor when it is bound to the ribosome.
Required for maturation of 30S ribosomal subunits.
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.
Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Binds vitamin B12 and delivers it to the periplasmic surface of BtuC (By similarity).
Belongs to the class A bacterial acid phosphatase family.
Heterotetramer of 2 PreA and 2 PreT subunits.
Involved in pyrimidine base degradation. Catalyzes physiologically the reduction of uracil to 5,6-dihydrouracil (DHU) by using NADH as a specific cosubstrate. It also catalyzes the reverse reaction and the reduction of thymine to 5,6-dihydrothymine (DHT) (By similarity).
In contrast to classical PTS systems, the fructose-specific PTS has no requirement for HPr; FruB combines a IIA domain with a HPr domain.
Induced by fructose and repressed by FruR.
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 FruAB PTS system is involved in fructose transport.
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.
In the C-terminal section; belongs to the peptidase M41 family.
In the central section; belongs to the AAA ATPase family.
Fimbriae (also called pili), polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, enable bacteria to colonize the epithelium of specific host organs.
Belongs to the bacterial solute-binding protein 5 family.
Part of the ABC transporter complex GsiABCD involved in glutathione import. Binds glutathione.
The complex is composed of two ATP-binding proteins (GsiA), two transmembrane proteins (GsiC and GsiD) and a solute-binding protein (GsiB).
Belongs to the ketol-acid reductoisomerase family.
In the presence of acetohydroxybutyrate and acetolactate.
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.
Homodimer. The ends of the coiled-coil dimer bind to each other, forming polymers. Interacts with FtsZ.
Non-essential, abundant cell division factor that is required for proper Z-ring formation. It is recruited early to the divisome by direct interaction with FtsZ, stimulating Z-ring assembly and thereby promoting cell division earlier in the cell cycle. Its recruitment to the Z-ring requires functional FtsA or ZipA.
Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.
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.
Belongs to the tRNA-modifying YgfZ family.
Folate-binding protein involved in regulating the level of ATP-DnaA and in the modification of some tRNAs. It is probably a key factor in regulatory networks that act via tRNA modification, such as initiation of chromosomal replication.
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.
H(+)-stimulated, divalent metal cation uptake system. Involved in manganese and iron uptake.
Belongs to the IMPDH/GMPR family. GuaC type 1 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.
Belongs to the peptide transporter carbon starvation (CstA) (TC 2.A.114) family.
Divalent metal cations. Prefers magnesium or manganese.
In the N-terminal section; belongs to the malic enzymes family.
P-II indirectly controls the transcription of the glutamine synthetase gene (GlnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme (By similarity).
In the C-terminal section; belongs to the transglycosylase Slt family.
In the N-terminal section; belongs to the bacterial solute-binding protein 3 family.
Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella.
The N-terminal domain does not have lytic activity and probably modulates enzymatic activity. The C-terminal domain is the catalytic active domain.
Belongs to the glycosyltransferase 1 family. Bacterial/plant glycogen synthase subfamily.
Synthesizes alpha-1,4-glucan chains using ADP-glucose.
Belongs to the major facilitator superfamily. Sialate:H(+) symporter (SHS) (TC 2.A.1.12) family.
Catalyzes the proton-dependent transport of sialic acid.
Belongs to the CobB/CobQ family. CobQ subfamily.
Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.
Belongs to the low molecular weight phosphotyrosine protein phosphatase family.
Dephosphorylates Wzc. Required for the extracellular polysaccharide colanic acid synthesis. Probably involved in the export of colanic acid from the cell to medium. Involved in protection of cells against contact-dependent growth inhibition (CDI).
Belongs to the thr operon leader peptide family.
This protein is involved in control of the biosynthesis of threonine.
Acts on guanine, xanthine and to a lesser extent hypoxanthine.
Belongs to the purine/pyrimidine phosphoribosyltransferase family. XGPT subfamily.
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 guanine and xanthine to form the corresponding ribonucleotides GMP (guanosine 5'-monophosphate) and XMP (xanthosine 5'-monophosphate), with the release of PPi. To a lesser extent, also acts on hypoxanthine.
Belongs to the 'phage' integrase family. XerD subfamily.
Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. Binds cooperatively to specific DNA consensus sequences that are separated from XerC binding sites by a short central region, forming the heterotetrameric XerC-XerD complex that recombines DNA substrates. The 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. In the complex XerD specifically exchanges the bottom DNA strands (By similarity).
Part of the phosphate (Pho) regulon, which plays a key role in phosphate homeostasis. PhoU is essential for the repression of the Pho regulon at high phosphate conditions.
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.
Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family.
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.
Binds 2 Zn(2+) ions per subunit. Zn(2+) ion 1 is bound in the active site. Zn(2+) ion 2 is bound at the dimer interface by residues from both subunits.
Murein endopeptidase that cleaves the D-alanyl-meso-2,6-diamino-pimelyl amide bond that connects peptidoglycan strands. Likely plays a role in the removal of murein from the sacculus.
Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
4'-phosphopantetheine is transferred from CoA to a specific serine of apo-IacP.
Part of the UhpABC signaling cascade that controls the expression of the hexose phosphate transporter UhpT. UhpB functions as a membrane-associated protein kinase that autophosphorylates in response to interaction with UhpC, and subsequently transfers its phosphate group to the response regulator UhpA. Can also dephosphorylate UhpA.
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.
Catalyzes the methylation of C-5 in cobalt-precorrin-7 to form cobalt-precorrin-8.
Belongs to the diacylglycerol/lipid kinase family. YegS lipid kinase subfamily.
Binds 1 Mg(2+) ion per subunit. Ca(2+) may be able to substitute. 2 Ca(2+) ions are seen in the crystal structure; one of the two occupies the same site as Mg(2+) in other family members.
Homodimer. May interact with the periplasmic chaperone Skp (also known as OmpH); this suggests the protein may be translocated to the periplasm and then sorted to the outer membrane.
In vitro does not phosphorylate diacylglycerol, sphingosine, N,N-dimethylsphingosine; threo-dihydrosphingosine, erythro-dihydrosphingosine, C2 ceramide, C6 ceramide, phosphatidylinositol or dimethylsphingosine. The potential in vivo substrate is unknown.
Cells lacking this gene display a strong clockwise motor bias; in combination with a yhjH disruption cells switch to a counterclockwise bias.
Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity (PubMed:2991277, PubMed:9760239). The N-terminal domain is not essential for catalysis (PubMed:2991277).
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 (PubMed:2991277, PubMed:2677005, PubMed:9760239). Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid (By similarity).
Phosphorylated by CheA (PubMed:3280143, PubMed:2677005, PubMed:9465023). Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity (PubMed:2677005, PubMed:9760239).
Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Two forms were isolated, the intact protein and a proteolytic fragment (147-349) that is 15-fold more active than its precursor.
Member of the two-component regulatory system BtsS/BtsR. BtsR regulates expression of btsT by binding to its promoter region.
Belongs to the HPS/KGPDC family. KGPDC subfamily.
Catalyzes the decarboxylation of 3-keto-L-gulonate-6-P into L-xylulose-5-P. Is involved in the anaerobic L-ascorbate utilization.
Ferrioxamine binding and uptake, in association with the TonB protein.
Belongs to the ThrE exporter (TC 2.A.79) family.
Control of the last step in methionine biosynthesis; MetR is a positive activator of the metA, metE and metH genes. It is also a negative regulator of its own expression.
Belongs to the 4-hydroxybenzoyl-CoA thioesterase 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 four rings (L,P,S, and M) mounted on a central rod. The M ring is integral to the inner membrane of the cell and may be connected to the flagellar rod via the S ring. The S (supramembrane ring) lies just distal to the M ring. The L and P rings lie in the outer membrane and the periplasmic space, respectively.
Interacts with phosphorylated BasR protein to mediate transcriptional induction of BasR-activated genes to induce polymyxin resistance.
Belongs to the dihydropyrimidine dehydrogenase family.
Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis.
Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+).
Phosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP to their respective diphosphate derivatives. Probably excludes non-canonical purines from DNA/RNA precursor pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
Homodimer; disulfide-linked, upon oxidation (PubMed:2643600, PubMed:8555198). 5 homodimers assemble to form a ring-like decamer (PubMed:11969410).
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.
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.
This protein is required for primosome-dependent normal DNA replication; it is also involved in inducing stable DNA replication during SOS response. It forms, in concert with DnaB protein and other prepriming proteins DnaC, N, N', N'' a prepriming protein complex on the specific site of the template DNA recognized by protein N'.
Belongs to the phosphoglycerate mutase family. Ais subfamily.
Catalyzes the dephosphorylation of heptose(II) of the outer membrane lipopolysaccharide core. Required for iron(3+) resistance.
Not essential for the ability to invade cultured HeLa cells (the invasive phenotype).
Required for maximal expression of sirC, not required to invade host cells.
Catalyzes the acetylation of dTDP-fucosamine (dTDP-4-amino-4,6-dideoxy-D-galactose) to dTDP-Fuc4NAc, which is utilized in the biosynthesis of the enterobacterial common antigen (ECA).
Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
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.
Involved in UV protection and mutation. Essential for induced (or SOS) mutagenesis. May modify the DNA replication machinery to allow bypass synthesis across a damaged template.
All four putative extracellular loops are crucial for invasion of mammalian cells.
Haemagglutinin that facilitates the adhesion to and invasion of epithelial mammalian cells. Utilizes heparinated proteoglycan as a receptor to successfully invade host cells.
Induced by both low pH and low Mg(2+) via the PhoQ/PhoP two-component regulatory system. Responds to general intracellular signals that are present both in initial and in progressive stages of infection.
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.
N-epsilon-lysine acetyltransferase that catalyzes acetylation of a large number of proteins.
Belongs to the DNA photolyase class-1 family.
Binds 1 5,10-methenyltetrahydrofolate (MTHF) non-covalently per subunit.
Involved in repair of UV radiation-induced DNA damage. Catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl pyrimidine dimers (in cis-syn configuration), which are formed between adjacent bases on the same DNA strand upon exposure to ultraviolet radiation.
Submitted sequence seems to have every 20th amino acid deleted.
Belongs to the UPF0758 family. YicR subfamily.
Derepression of genes that are usually coregulated by H-NS and Hha (PubMed:23515315).
Interacts with H-NS and in this complex might contact DNA, which could provide an additional surface for DNA binding to the H-NS-Hha complex; may not bind DNA in the absence of H-NS (PubMed:23515315). In vitro improves the ability of H-NS to bind DNA under a precise set of conditions (PubMed:23515315).
Interacts with H-NS; crystal structures suggest each subunit of an H-NS dimer could bind 1 Hha monomer (PubMed:23515315).
Heterotetramer of two alpha chains (FadB) and two beta chains (FadA).
In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.
Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate.
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 L12 dimers bind in a sequential fashion forming a multimeric L10(L12)X complex.
Heterodimer of a catalytic subunit (MsrP) and a heme-binding subunit (MsrQ).
Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.
Belongs to the type-I restriction system S methylase family.
Contains two DNA recognition domains, each specifying recognition of one of the two defined components of the target sequence (PubMed:3025838, PubMed:2838725). The recognition domains can be exchanged between different S proteins, generating enzymes that have new sequence specificities (PubMed:2838725).
The specificity (S) subunit of a type I restriction enzyme; this subunit dictates DNA sequence specificity. The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues of the sequence 5'-GAGN(6)GTRC-3'. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance MTase modifying the DNA so that both strands become methylated (PubMed:3025838, PubMed:12654995). After locating a non-methylated recognition site, the enzyme complex serves as a molecular motor that translocates DNA in an ATP-dependent manner until a collision occurs that triggers cleavage (By similarity).
Activation of anaerobic ribonucleoside-triphosphate reductase under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine.
Belongs to the selenophosphate synthase 1 family. Class I subfamily.
Synthesizes selenophosphate from selenide and ATP.
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.
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.
Belongs to the HAD-like hydrolase superfamily. PhnX family.
Belongs to the metallophosphoesterase superfamily. YfcE family.
Component of the lipopolysaccharide transport and assembly complex. Interacts with LptD.
Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane.
ATPase activity is slightly increased in the presence of HisM and HisQ, and strongly increased when HisJ is also present.
Part of the histidine permease ABC transporter. Also part of a lysine/arginine/ornithine transporter. Responsible for energy coupling to the transport system.
Belongs to the heat shock protein 90 family.
Molecular chaperone. Has ATPase activity.
Belongs to the glycosyl hydrolase 33 family.
Cleaves the terminal sialic acid (N-acetyl neuraminic acid) from carbohydrate chains in glycoproteins providing free sialic acid which can be used as carbon and energy sources. Sialidases have been suggested to be pathogenic factors in microbial infections.
Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily.
Catalyzes the biosynthesis of agmatine from arginine.
Belongs to the complex I 24 kDa subunit family.
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.
A bidirectional acetate kinase that may drive flux through the ethanolamine (EA) degradation pathway under anoxic conditions found when this bacteria infects the host intestine. It may generate ATP that can be used by other enzymes (EutA and EutT) in the eut pathway. Can use GTP instead of ATP with reduced efficiency (PubMed:26448059). Might be required to correctly target EutE to bacterial microcompartments (BMC) (Probable). Required for the biogenesis of multiple mobile BMCs per cell. Might serve as an assembly hub for BMC shell proteins. Expression of eutK, eutL, eutM, eutN, eutS (eutSMNLK) in E.coli leads to formation of a single BMC; coexpression of eutQ with eutSMNLK permits E.coli to make cells with more than one mobile BMC, as is usual in vivo. EutS alone also forms BMCs, but in the presence of eutQ both BMCs and protein filaments are formed (PubMed:27063436).
A quadruple eutP-eutQ-eutT-eutD deletion is not impaired for aerobic growth on ethanolamine (EA) supplemented with cobalamin (vitamin B12) (PubMed:10464203). A non-polar deletion mutant grows on EA from pH 5.5 to pH 8.0, but does not grow at pH 8.5, releases increased amounts of acetaldehyde on EA plus vitamin B12 (PubMed:16585748). Does not grow on EA and tetrathionate under anoxic conditions; complemented by acetate/propionate kinases AckA, PduW or TdcD (PubMed:26448059). Only makes a single immobile BMC localized near the cell pole (PubMed:27063436).
Artificial BMCs can be made in E.coli by expressing eutK, eutL, eutM, eutN, eutS (eutSMNLK). Cargo proteins can be targeted to them. The addition of eutQ to the eutSMNLK construct results in biogenesis of multiple BMCs. This can lead to the development of tailored BMCs for specific metabolic reactions.
Homodimer (Probable). Interacts with the N-terminus of EutM; a probably cytoplasm-facing helix (EutM 'Val-49' to 'Gln-64') interacts with N-terminus of EutQ (PubMed:27063436).
Belongs to the ATPase gamma chain family.
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.
Component of the lipopolysaccharide transport and assembly complex.
Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. May form a bridge between the inner membrane and the outer membrane, via interactions with LptC and LptD, thereby facilitating LPS transfer across the periplasm.
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.
Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
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.
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. 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.
Part of the signal recognition particle protein translocation system, which is composed of SRP and FtsY. SRP is a ribonucleoprotein composed of Ffh and a 4.5S RNA molecule.
Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family.
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.
Uptake of inorganic phosphate, phosphorylated compounds, and some other negatively charged solutes.
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).
Probably involved in the export of the extracellular polysaccharide colanic acid from the cell to medium.
Binds 1 [4Fe-4S] cluster per subunit. The cluster is chelated by three Cys residues, the fourth Fe has a free coordination site that may bind a sulfur atom transferred from the persulfide of IscS.
Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system.
Loss of cytidine thiolation in position 32 in tRNA. The deletion mutant grows at the same rate as the congenic wild-type strain, but several specific steps in the translational decoding process are affected in the mutant.
The thiolation reaction likely consists of two steps: a first activation step by ATP to form an adenylated intermediate of the target base of tRNA, and a second nucleophilic substitution step of the sulfur (S) atom supplied by the hydrosulfide attached to the Fe-S cluster.
Transcriptional regulator required for the expression of several genes encoding type III secretion system SPI1 effector proteins. The interaction with SicA is necessary for the activation of sigDE (sopB pipC), sicAsipBCDA, and sopE.
Belongs to the alanine or glycine:cation symporter (AGCS) (TC 2.A.25) family.
Member of a two-component regulatory system QseB/QseC. Activates the flagella regulon by activating transcription of FlhDC. May activate QseB by phosphorylation (By similarity).
Confers a modal distribution of chain length on the O-antigen component of lipopolysaccharide (LPS). Gives rise to a reduced number of short chain molecules and increases in numbers of longer molecules, with a modal value of 20.
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).
Belongs to the major facilitator superfamily. LplT (TC 2.A.1.42) family.
Catalyzes the facilitated diffusion of 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) into the cell.
Belongs to the GST superfamily. Zeta family.
Low-potential electron donor to a number of redox enzymes.
This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control.
Member of the two-component regulatory system BasS/BasR. BasR induces the transcription of the ugd, ais, arnBCADTEF and eptA-basRS loci, all involved in resistance to polymyxin. Represses the transcription of pmrD. Plays a role in the adaptation of the organism to the host environment, in particular to neutrophils, and therefore it plays a role in virulence as well.
The activity of the BasR protein is controlled at a post-transcriptional level by the PmrD protein, under low Mg(2+) concentration conditions.
Homodimer. Forms a complex with the accessory proteins ExbB and ExbD (By similarity).
Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates such as cobalamin, and various iron compounds (such as iron dicitrate, enterochelin, aerobactin, etc.). In the absence of TonB these receptors bind their substrates but do not carry out active transport. TonB also interacts with some colicins and is involved in the energy-dependent, irreversible steps of bacteriophages phi 80 and T1 infection. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins.
Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide.
Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG).
Methyltransferase that likely catalyzes the ring contraction and methylation of C-17 in cobalt-factor III to form cobalt-factor IV. May also convert cobalt-precorrin-3 to cobalt-precorrin-4.
A role in zinc efflux has been proposed by Worlock et al, but ZntB was later shown in E.coli to likely mediate zinc uptake, using a transport mechanism that does not resemble the one proposed for homologous CorA channels.
Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35) family.
Disruption of the gene has a marked effect on resistance levels to zinc and cadmium, but does not significantly alter the sensitivities to cobalt, nickel or manganese.
Forms a funnel-like structure. Contains three Zn(2+) binding sites, two of which could be involved in Zn(2+) transport.
Homopentamer (PubMed:21565704). Can assemble pentamers in the absence of the transmembrane regions (PubMed:21565704).
Zinc transporter (PubMed:12142406). Acts as a Zn(2+):proton symporter, which likely mediates zinc ion uptake (By similarity).
The IMP cyclohydrolase activity resides in the N-terminal region.
Belongs to the complex I subunit 1 family.
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone.
Belongs to the GreA/GreB family. GreB subfamily.
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. GreB releases sequences of up to 9 nucleotides in length.
To the N-terminal of the FimA/PapA family of fimbria proteins.
Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP.
Involved in formation and maintenance of cell shape.
Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.
Overproduction of CaiE stimulates the activity of CaiB and CaiD.
Binds 1 zinc ion per glycerol kinase EIIA-Glc dimer. The zinc ion is important for dimerization.
Heterodimer with glycerol kinase (glpk).
In mutants defective in enzyme I and histidine-containing phosphate carrier protein (HPr), cells lacking this gene are able to grow on the non-PTS compounds such as glycerol, maltose, melibiose, mannose 6-phosphate, and alpha-glycerol phosphate.
The EIIA domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the EIIB 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 complex composed of PtsG and Crr is involved in glucose transport (PubMed:6754734, PubMed:6292227). It can also phosphorylate mannose, methyl alpha-glucoside and 2-deoxy-glucose (PubMed:6292227). The non-phosphorylated EIII-Glc is an inhibitor for uptake of certain sugars such as maltose, melibiose, lactose, and glycerol. Phosphorylated EIII-Glc, however, may be an activator for adenylate cyclase (PubMed:789369).
Two forms of III-Glc (called IIIGlc Slow and IIIGlc Fast) are present in living cells. IIIGlc Fast, derived from IIIGlc Slow by cleavage of the seven NH2-terminal amino acids, is present only in trace quantities and has slight activity (only 2-3% of phospho-IIIGlc Slow) in the phosphorylation of sugar. Both forms accept phosphate from phosphoenolpyruvate via Enzyme I and HPr, however only IIIGlc Slow participates in the phosphorylation of glucose or methyl alpha-D-glucoside. IIIGlc Fast may play a role in the regulation of non-PTS sugar transport systems.
Belongs to the glycosyltransferase 51 family.
Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors.
Belongs to the metallo-dependent hydrolases superfamily. TatD-type hydrolase family.
Catalyzes the ATP-dependent phosphorylation of fructose-l-phosphate to fructose-l,6-bisphosphate.
Functions as a ribosomal silencing factor. Interacts with ribosomal protein L14 (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 L14 (rplN).
This protein is a positive regulator for the phosphate regulon. Transcription of this operon is positively regulated by PhoB and PhoR when phosphate is limited.
ATPase component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (PubMed:15060043, PubMed:16208377, PubMed:26170413). Acts as a molecular motor to provide the energy that is required for the export of proteins (Probable). Required for type III secretion apparatus (T3SA) formation, proper protein secretion, host cell invasion and virulence (PubMed:8045880, PubMed:14762212, PubMed:15060043, PubMed:26170413). May play a critical role in T3SS substrate recognition, disassembly of the effector/chaperone complex and unfolding of the effector in an ATP-dependent manner prior to secretion (PubMed:16208377). Releases the effector protein SptP from the chaperone SicP in an ATP-dependent manner (PubMed:16208377).
Belongs to the ATPase alpha/beta chains family. T3SS ATPase subfamily.
Binding of ATP leads to conformational changes of two loops located outside of the catalytic site. These changes could be critical for interaction with the stalk protein InvI/SctO or with chaperone and effector proteins during type III secretion.
Deletion of the gene affects the overall stability of the cytoplasmic sorting platform (PubMed:28283062). Disruption mutant is defective in its ability to enter cultured epithelial cells (PubMed:8045880).
The core secretion machinery of the T3SS is composed of approximately 20 different proteins, including cytoplasmic components, a base, an export apparatus and a needle (PubMed:30107569, PubMed:28283062). This subunit is part of the cytosolic complex (PubMed:15060043, PubMed:31288030, PubMed:28283062). Forms homohexamers (PubMed:15060043, PubMed:28283062). Interacts directly with OrgB/SctL (stator protein) and InvI/SctO (stalk protein) (PubMed:15060043, PubMed:31288030, PubMed:28283062). Forms a complex with SpaO/SctQ and OrgB/SctL (PubMed:31288030). Interacts with the chaperone/effector protein complex SicP-SptP via its C terminus (PubMed:16208377). Interacts with the effector protein SopD (PubMed:20185511).
Mutants lack the ability to produce a biofilm.
Required for cellulose biosynthesis (PubMed:11929533). May have protease activity (PubMed:11929533), but BcsA is not targeted (PubMed:24942809). Binds bis-(3'-5') cyclic diguanylic acid (c-di-GMP) (PubMed:24942809).
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily.
Belongs to the L-rhamnose transporter (TC 2.A.7.6) family.
Uptake of L-rhamnose across the cytoplasmic membrane with the concomitant transport of protons into the cell (symport system).
Belongs to the 2H phosphoesterase superfamily. ThpR family.
Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
Belongs to the major facilitator superfamily. TsgA family.
Belongs to the glycosyltransferase group 1 family.
Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Required for O(2)-independent ubiquinone (coenzyme Q) biosynthesis. Likely functions as an accessory factor.
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.
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).
Part of an enzyme complex containing four subunits: a flavoprotein, an iron-sulfur protein, plus two membrane-anchoring proteins, SdhC and SdhD. The complex can form homotrimers (By similarity).
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.
Belongs to the uracil-DNA glycosylase (UDG) superfamily. TDG/mug family.
Excises ethenocytosine and uracil, which can arise by alkylation or deamination of cytosine, respectively, from the corresponding mispairs with guanine in ds-DNA. It is capable of hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of the DNA and the mispaired base. The complementary strand guanine functions in substrate recognition. Required for DNA damage lesion repair in stationary-phase cells.
Member of the two-component regulatory system ZraS/ZraR. When activated by ZraS it acts in conjunction with sigma-54 to regulate the expression of zraP. Positively autoregulates the expression of the zraSR operon (By similarity).
Belongs to the bacterial ribosomal protein bL36 family.
Belongs to the RNA polymerase beta chain family.
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.
Belongs to the leucine-binding protein family.
This protein is a component of the leucine-specific transport system, which is one of the two periplasmic binding protein-dependent transport systems of the high-affinity transport of the branched-chain amino acids.
Involved in the import of serine and threonine into the cell, with the concomitant import of sodium (symport system).
Belongs to the glycosyltransferase 4 family. WecA subfamily.
Catalyzes the transfer of the GlcNAc-1-phosphate moiety from UDP-GlcNAc onto the carrier lipid undecaprenyl phosphate (C55-P), yielding GlcNAc-pyrophosphoryl-undecaprenyl (GlcNAc-PP-C55).
Autophosphorylated. Activation probably requires a transfer of a phosphate group from a His in the transmitter domain to an Asp in the receiver domain.
Component of the Rcs signaling system, which controls transcription of numerous genes. RcsC functions as a membrane-associated protein kinase that phosphorylates RcsD in response to environmental signals. The phosphoryl group is then transferred to the response regulator RcsB.
Catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide.
Belongs to the SorC transcriptional regulatory family.
In the absence of autoinducer 2 (AI-2), represses transcription of the lsrACDBFGE operon and its own transcription. In the presence of AI-2, LsrR is inactivated by binding phospho-AI-2, leading to the transcription of the lsr genes.
Inhibited by cadmium, copper, zinc when added cobalt when added concomitantly with manganese.
Belongs to the SIS family. GutQ/KpsF subfamily.
Catalyzes the reversible aldol-ketol isomerization between D-ribulose 5-phosphate (Ru5P) and D-arabinose 5-phosphate (A5P). It is also able of sustaining the biosynthetic pathway of 3-deoxy-D-manno-octulosonate (KDO), a unique 8-carbon sugar component of lipopolysaccharides (LPSs) (By similarity).
Belongs to the binding-protein-dependent transport system permease family. MalFG subfamily.
Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Probably responsible for the translocation of the substrate across the membrane.
The complex is composed of two ATP-binding proteins (MalK), two transmembrane proteins (MalG and MalF) and a solute-binding protein (MalE).
Belongs to the Cu-Zn superoxide dismutase family.
Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Belongs to the methylthiotransferase family. MiaB subfamily.
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.
A GTPase-activating protein (GAP) that modifies Der/EngA GTPase function. May play a role in ribosome biogenesis.
Catalyzes the phosphorylation of L-fuculose.
Belongs to the thioester dehydratase family. FabA subfamily.
Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length.
Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.
Belongs to the radical SAM superfamily. ThiH family.
Catalyzes the radical-mediated cleavage of tyrosine to 2-iminoacetate and 4-cresol.
The product 2-iminoacetate hydrates in vitro to yield glyoxylate and ammonium.
Belongs to the polyribonucleotide nucleotidyltransferase family.
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. Is a global regulator of virulence and persistency.
This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Belongs to the major facilitator superfamily. DHA1 family. MdtH (TC 2.A.1.2.21) subfamily.
Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. It is required for pilus biogenesis (By similarity).
Involved in O antigen modification. Involved in the translocation of bactoprenol-linked glucose across the cytoplasmic membrane.
Flagellar protein that affects chemotactic events.
Associates with aggregated proteins, together with IbpA, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent.
Homodimer. Forms homomultimers of about 100-150 subunits at optimal growth temperatures. Conformation changes to oligomers at high temperatures or high ionic concentrations. The decrease in size of the multimers is accompanied by an increase in chaperone activity.
The N- and C-terminal flexible termini are involved in oligomerization and in the binding of non-native substrate proteins, and are essential for chaperone activity.
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 (By similarity).
Has four distinct domains: an N-terminal nucleotidyltransferase (NT) domain responsible for UTase activity, a central HD domain that encodes UR activity, and two C-terminal ACT domains that seem to have a role in glutamine sensing.
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Uridylyltransferase (UTase) activity is inhibited by glutamine, while glutamine activates uridylyl-removing (UR) activity.
Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily.
Catalytic subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from NapB and catalyzes the reduction of nitrate to nitrite.
Catalyzes the isomerization of L-ribulose 5-phosphate to D-xylulose 5-phosphate. Is involved in the anaerobic L-ascorbate utilization.
Belongs to the glycyl radical enzyme (GRE) family. PFL subfamily.
Could be a 3Fe-4S cluster-containing protein.
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).
Belongs to the RNA polymerase beta' chain family.
Chromosomal supercoiling density is controlled by a combination of RNA polymerase and DNA gyrase activity; negative supercoiling increases upstream of transcribed regions while it decreases downstream, DNA gyrase introduces negative supercoils into underwound DNA (PubMed:22916023).
Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.
Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
May be a transcriptional activator of genes involved in the multiple antibiotic resistance (Mar) phenotype. It can also activate genes such as sodA, zwf and micF.
Acts as a flagellar brake, regulating swimming and swarming in a bis-(3'-5') cyclic diguanylic acid (c-di-GMP)-dependent manner. Overexpression of this gene decreases swimming and swarming motility; those cells that are motile turn predominantly counterclockwise. The D-118 mutant is still able to bind FliM but no longer affects motility upon overexpression. Binds 1 c-di-GMP dimer per subunit.
Monomer. Interacts with the flagellar basal bodies (By similarity).
No visible motility phenotype. Disruption of this gene suppresses the reduced motility of a yhjH disruption, thus the double knockout is motile. Overexpression of this gene in a yhjH disruption has the converse effect, i.e. it reduces motility further.
The N-terminal domain is involved in FliG binding, the C-terminal domain is involved in FliM binding.
Binds to and stimulates the transcription of the CCAAT-containing, cold-shock-inducible promoters of the H-NS and GyrA proteins. Binds also to the inverted repeat 5'-ATTGG-3' (By similarity).
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. PrfC subfamily.
Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP.
Could be involved in insertion of integral membrane proteins into the membrane.
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. Is able to use other nucleotide triphosphates as substrate, such as GTP or UTP, although less efficiently than ATP.
Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP and cobyrinate and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate.
The a and c carboxylates of cobyrinate are activated for nucleophilic attack via formation of a phosphorylated intermediate by ATP. CbiA catalyzes first the amidation of the c-carboxylate, and then that of the a-carboxylate.
Belongs to the inositol monophosphatase superfamily. CysQ family.
Converts adenosine-3',5'-bisphosphate (PAP) to AMP.
Strongly repressed during nitrogen excess.
Global transcription factor that controls the expression of over 100 target genes in response to anoxia. It facilitates the adaptation to anaerobic growth conditions by regulating the expression of gene products that are involved in anaerobic energy metabolism. When the terminal electron acceptor, O(2), is no longer available, it represses the synthesis of enzymes involved in aerobic respiration and increases the synthesis of enzymes required for anaerobic respiration (By similarity).
Calcium ions stabilize the structure, and may inhibit FabG activity by obstructing access to the active site.
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.
Belongs to the RNA 3'-terminal cyclase family. Type 1 subfamily.
Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing.
Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily.
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.
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.
Belongs to the LDH2/MDH2 oxidoreductase family. DlgD subfamily.
Catalyzes the reduction of 2,3-diketo-L-gulonate in the presence of NADH, to form 3-keto-L-gulonate.
Adopts a GT-A fold and acts as an inverting enzyme that converts the alpha-configuration in the UDP-N-acetyl-alpha-D-glucosamine donor to the beta configuration in the N-linked (GlcNAc) arginine product.
Belongs to the glycosyltransferase NleB family.
Protein-arginine N-acetylglucosaminyltransferase activity is inhibited by 100066N compound (flavone analog) and 102644N compound (a substituted isoxazole).
Protein-arginine N-acetylglucosaminyltransferase effector that catalyzes the transfer of a single N-acetylglucosamine (GlcNAc) to a conserved arginine residue in the death domain of host proteins such as FADD: arginine GlcNAcylation prevents homotypic/heterotypic death domain interactions (PubMed:28522607). Also acts on host proteins without a death domain: catalyzes arginine GlcNAcylation of host small Rab1 GTPase, thereby preventing GTPase activity and leading to impaired host vesicular protein transport (By similarity). In contrast to Ssek1, not able to disrupt TNF signaling in infected cells (PubMed:28522607).
Catalyzes the sodium-dependent uptake of extracellular L-proline.
Expression may be repressed by PutA in the absence of proline.
Belongs to the SLC13A/DASS transporter (TC 2.A.47) family. DIT1 subfamily.
During infection of the host cells. Down-regulated by itself. Activated by Mg(2+) starvation in a phoP dependent manner.
Transcription regulator that can specifically activate or repress expression of target genes. Required for virulence and survival in the macrophage environment. Probably activates expression of ispA, xseB genes, and of omp operon.
Was originally thought to be a toxin with hemolytic and cytolytic activity.
Belongs to the pyrroline-5-carboxylate reductase family.
Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Cells lacking this gene accumulate 2-methylcitrate during growth on propionate.
Involved in the catabolism of short chain fatty acids (SCFA) via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the dehydration of 2-methylcitrate (2-MC) to yield the cis isomer of 2-methyl-aconitate. It is also able to catalyze the dehydration of citrate at a lower rate, and the hydration of cis-aconitate. It has no aconitase-like activity and is unable to catalyze the hydration of 2-methyl-cis-aconitate.
Belongs to the ATP-dependent AMP-binding enzyme family.
Catalyzes the synthesis of propionyl-CoA from propionate and CoA. Also converts acetate to acetyl-CoA but with a lower specific activity.
Interacts, and probably forms a ternary complex, with MukE and MukB via its C-terminal region. The complex formation is stimulated by calcium or magnesium. It is required for an interaction between MukE and MukB.
Involved in chromosome condensation, segregation and cell cycle progression. May participate in facilitating chromosome segregation by condensation DNA from both sides of a centrally located replisome during cell division. Not required for mini-F plasmid partitioning. Probably acts via its interaction with MukB and MukE. Overexpression results in anucleate cells. It has a calcium binding activity.
Belongs to the peptidase M20A family. ArgE subfamily.
Binds 2 Zn(2+) or Co(2+) ions per subunit.
Catalyzes the hydrolysis of the amide bond of N(2)-acetylated L-amino acids. Cleaves the acetyl group from N-acetyl-L-ornithine to form L-ornithine, an intermediate in L-arginine biosynthesis pathway, and a branchpoint in the synthesis of polyamines.
Part of the ABC transporter complex LsrABCD involved in autoinducer 2 (AI-2) import. Binds AI-2 and delivers it to the LsrC and LsrD permeases (Probable).
Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
The enzyme has distinct binding sites for each of the allosteric effectors such as acetyl-CoA, fructose 1,6-bisphosphate, guanosine 3'-diphosphate 5'-diphosphate, long chain fatty acids, and L-aspartate.
Belongs to the RapZ-like family. RapZ subfamily.
Modulates the synthesis of GlmS, by affecting the processing and stability of the regulatory small RNA GlmZ. When glucosamine-6-phosphate (GlcN6P) concentrations are high in the cell, RapZ binds GlmZ and targets it to cleavage by RNase E. Consequently, GlmZ is inactivated and unable to activate GlmS synthesis. Under low GlcN6P concentrations, RapZ is sequestered and inactivated by an other regulatory small RNA, GlmY, preventing GlmZ degradation and leading to synthesis of GlmS.
Cells lacking this gene are conditional thiamine auxotrophs, and display phenotypic behaviors similar to those of strains lacking isc (iron-sulfur [Fe-S] cluster biosynthesis) operon functions.
Flavin transferase that catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein such as NqrB and NqrC, two subunits of the NQR complex.
Was originally thought to be involved in synthesis of the pyrimidine moiety of thiamine and/or in metabolism of Fe-S clusters.
Belongs to the major facilitator superfamily. SotB (TC 2.A.1.2) family.
Involved in the efflux of sugars. The physiological role may be the reduction of the intracellular concentration of toxic sugars or sugar metabolites.
Part of the ABC transporter complex GsiABCD involved in glutathione import. Probably responsible for the translocation of the substrate across the membrane.
Required for the biogenesis of type 1 fimbriae. Binds and interact with FimH.
Belongs to the phosphoethanolamine transferase family. EptC/CptA subfamily.
Catalyzes the addition of a phosphoethanolamine moiety to the outer membrane lipopolysaccharide core.
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.
2-keto-L-gulonic acid is a key intermediate in the production of L-ascorbic acid (vitamin C).
Belongs to the aldo/keto reductase family.
Catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA(Lys), tRNA(Glu) and tRNA(Gln), leading to the formation of s(2)U34, the first step of tRNA-mnm(5)s(2)U34 synthesis. Sulfur is provided by IscS, via a sulfur-relay system. Binds ATP and its substrate tRNAs.
3'-to-5' exoribonuclease specific for small oligoribonucleotides.
Belongs to the oligoribonuclease family.
Belongs to the bacterial ribosomal protein bS1 family.
Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence.
Increases expression of the entire cob operon about 90-fold irrespective of the growth medium; expression retains its sensitivity to vitamin B12 repression (PubMed:8071226). Cells lacking this gene are defective in aerobic and anaerobic degradation of propanediol (PubMed:9023178, PubMed:7559322).
Positive regulatory protein of pdu and cob operons (PubMed:8071226, PubMed:7559322, PubMed:9023178). Positively autoregulates its own expression (PubMed:7559322).
Cell division factor that enhances FtsZ-ring assembly. Directly interacts with FtsZ and promotes bundling of FtsZ protofilaments, with a reduction in FtsZ GTPase activity.
Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell.
Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family.
Member of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. Under conditions of nitrogen limitation, NtrB autophosphorylates and transfers the phosphoryl group to NtrC. In the presence of nitrogen, acts as a phosphatase that dephosphorylates and inactivates NtrC.
Belongs to the cytochrome c oxidase subunit 3 family.
Chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. Involved in the maturation of IscU.
Belongs to the SIMIBI class G3E GTPase family. ZNG1 subfamily.
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).
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.
Activates expression of the rhaSR operon in response to L-rhamnose.
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.
Belongs to the succinate/malate CoA ligase beta 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 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.
Converts holo-ACP to apo-ACP by hydrolytic cleavage of the phosphopantetheine prosthetic group from ACP.
Belongs to the UPF0312 family. Type 1 subfamily.
Part of the OsmU ABC transporter complex, which is involved in the uptake of osmoprotectants such as choline-O-sulfate and glycine betaine. Probably responsible for the translocation of the substrate across the membrane.
Activator for CDC42 by directly engaging this Rho GTPase and acting as potent guanine nucleotide exchange factor (GEF). This activation results in actin cytoskeleton rearrangements and stimulates membrane ruffling, promoting bacterial entry into non-phagocytic cells. Also activates NF-kB, p38 and ERK kinases, which are known to be involved in the induction of IL-8 expression. Chaperone InvB is required for secretion, translocation and stabilization of intracellular levels of sopE2.
Belongs to the GEF (guanine exchange factor) SopE family.
SopE2 is highly conserved among Salmonella isolates of the SARA collection.
Belongs to the pyruvate, phosphate/water dikinase regulatory protein family. PSRP subfamily.
Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the phosphoenolpyruvate synthase (PEPS) by catalyzing its phosphorylation/dephosphorylation.
Belongs to the outer membrane porin (Opr) (TC 1.B.25) family.
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.
Belongs to the purine nucleoside phosphorylase YfiH/LACC1 family.
Deletion of this gene impairs bacterial replication in mouse macrophages but not in human epithelial cells.
Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. Contributes to replication in macrophages. Plays a role, cooperatively with SopB, in membrane fission and macropinosome formation during invasion.
Transcriptional activator of the superoxide response regulon of E.coli that includes at least 10 genes such as sodA, nfo, zwf and micF. Binds the DNA sequence 5'-GCACN(7)CAA-3'. It also facilitates the subsequent binding of RNA polymerase to the micF and the nfo promoters (By similarity).
Component of the lipopolysaccharide transport and assembly complex. The LptBFG transporter is composed of two ATP-binding proteins (LptB) and two transmembrane proteins (LptF and LptG).
Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane.
Involved in the oxidation of myo-inositol (MI) to 2-keto-myo-inositol (2KMI or 2-inosose).
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 adenylyl cyclase class-1 family.
The regulatory domain is involved in the regulation of cyclase activity by the carbon source. Activated by the PTS system, glucose-specific IIA component (CRR).
Belongs to the transpeptidase family. MrdA subfamily.
Catalyzes cross-linking of the peptidoglycan cell wall.
A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and facilitates RecA-binding to the ssDNA for homologous DNA recombination and repair. Holoenzyme degrades any linearized DNA that is unable to undergo homologous recombination. In the holoenzyme this subunit recognizes the wild-type Chi sequence, and when added to isolated RecB increases its ATP-dependent helicase processivity.
Heterotrimer of RecB, RecC and RecD. All subunits contribute to DNA-binding.
Belongs to the thioesterase PaaI family.
Homotetramer. Dimer of dimers. Interacts specifically with the aryl carrier protein (ArCP) domain of EntB.
Required for optimal enterobactin synthesis. Acts as a proofreading enzyme that prevents EntB misacylation by hydrolyzing the thioester bound existing between EntB and wrongly charged molecules.
Belongs to the AAE transporter (TC 2.A.81) family. YidE subfamily.
Activated by ATP and maltotriose, which are both required for DNA binding.
Monomer in solution. Oligomerizes to an active state in the presence of the positive effectors ATP and maltotriose.
Positively regulates the transcription of the maltose regulon whose gene products are responsible for uptake and catabolism of malto-oligosaccharides. Specifically binds to the promoter region of its target genes, recognizing a short DNA motif called the MalT box.
Cells lacking EF-P display highly pleiotropic phenotypes similar to those lacking EmpA or EmpB. They exhibit reduced growth rates, and they display increased susceptibility to hypoosmotic conditions, antibiotics, and detergents and enhanced resistance to the compound S-nitrosoglutathione. The susceptibility phenotypes are largely explained by the enhanced membrane permeability of the efp mutant. Analysis of the membrane proteomes of wild-type and efp mutant strains reveals few changes, including the prominent overexpression of a single porin, KdgM (STM1131), in the efp mutant outer membrane.
Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Modification of Lys-34 is required for alleviation.
Is beta-lysylated on the epsilon-amino group of Lys-34 by the combined action of EpmA and EpmB, and then hydroxylated on the C5 position of the same residue by EpmC. Lysylation is critical for the stimulatory effect of EF-P on peptide-bond formation. The lysylation moiety would extend toward the peptidyltransferase center and stabilize the terminal 3-CCA end of the tRNA. The hydroxylation of the C5 position on Lys-34 would allow additional potential stabilizing hydrogen-bond interactions with the P-tRNA (Probable) (PubMed:20670890).
The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity.
Belongs to the GatZ/KbaZ family. GatZ subfamily.
Component of the tagatose-1,6-bisphosphate aldolase GatYZ that is required for full activity and stability of the Y subunit. Could have a chaperone-like function for the proper and stable folding of GatY. When expressed alone, GatZ does not show any aldolase activity. Is involved in the catabolism of galactitol.
Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
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.
Belongs to the Fre/LuxG FAD/NAD(P) flavoprotein oxidoreductase family.
Catalyzes the reduction of soluble flavins by reduced pyridine nucleotides.
Belongs to the class I-like SAM-binding methyltransferase superfamily. Cx-SAM synthase family.
Catalyzes the conversion of S-adenosyl-L-methionine (SAM) to carboxy-S-adenosyl-L-methionine (Cx-SAM).
Deletion mutant shows accumulation of 5-methoxyuridine (mo5U34) and 5-hydroxyuridine (ho5U34) in tRNA.
Was originally thought to be a transferase that mediates the conversion of mo5U(34) to cmo5U(34) in tRNAs.
Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation of a transient KdpB/KdpC/ATP ternary complex.
Nitric oxide-sensitive repressor of genes involved in protecting the cell against nitrosative stress. May require iron for activity. Represses hmp expression under conditions of elevated intracellular iron concentrations, in the absence of nitric oxide.
Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-polyprenylbenzoic acid decarboxylase UbiD. The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN.
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 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 complex composed of PtsG and Crr is involved in glucose transport. Also functions as a chemoreceptor monitoring the environment for changes in sugar concentration. It can also phosphorylate mannose, methyl alpha-glucoside and 2-deoxy-glucose.
Belongs to the AB hydrolase superfamily. Carboxylesterase BioH family.
The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters.
Probably involved in the diffusion of protonated ethanolamine (EA) into the cell at low pH. At low pH most EA is protonated, and this permease becomes necessary (Probable). Contributes to bacterial survival and replication in acidified macrophage vacuoles, but not to bacterial uptake by macrophages (PubMed:29531136).
Unable to grow with ethanolamine (EA) as sole carbon source. Slightly attenuated in a mouse model of infection (PubMed:7868611). A double eutG-eutH deletion is not impaired for aerobic growth on EA supplemented with cobalamin (vitamin B12) (PubMed:10464203). Cells are unable to grow on EA at low pH (PubMed:15466042). A non-polar deletion mutant does not grow on EA at pH 5.5 or pH 8.5, poorly at pH 6.0 but wild-type at pH 7.0 and pH 8.0, slight decrease in acetaldehyde release on EA plus vitamin B12 (PubMed:16585748). About 25% reduction in survival in mouse macrophage assays. Bacterial growth is not enhanced by exogenous EA in macrophage survival assays. Decreased survival in mouse intraperitoneal infection, no phenotype in mouse colitis infections (PubMed:29531136).
Belongs to the ROK (NagC/XylR) family. NanK subfamily.
Catalyzes the phosphorylation of N-acetylmannosamine (ManNAc) to ManNAc-6-P.
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.
Binds 1 Ca(2+) ion per monomer. In the dimeric form the Ca(2+) is bound by different amino acids with binding of each Ca(2+) shared with ligands coming from each monomer. The Ca(2+) ion may have a role in catalysis.
Homodimer; dimerization is reversible, and the dimeric form is the active one.
Hydrolysis of phosphatidylcholine with phospholipase A2 (EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities.
Belongs to the SurE nucleotidase family.
Nucleotidase with a broad substrate specificity as it can dephosphorylate various ribo- and deoxyribonucleoside 5'-monophosphates and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP. Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the preference for short-chain-length substrates (P20-25). Might be involved in the regulation of dNTP and NTP pools, and in the turnover of 3'-mononucleotides produced by numerous intracellular RNases (T1, T2, and F) during the degradation of various RNAs.
Belongs to the class-II aminoacyl-tRNA synthetase family. AsnA subfamily.
Disruption of the gene prevents the efficient use of AIRs as a source of thiamine.
Does not show significant conformational changes upon substrate binding.
Phosphorylates 5-amino-1-(beta-D-ribosyl)imidazole (AIRs) to form 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole (AIR), an important intermediate in the purine and thiamine biosynthetic pathways (PubMed:12486071). It allows the use of exogenous aminoimidazole riboside (AIRs) to satisfy the cellular requirement for purines and thiamine (PubMed:12486071).
Belongs to the protease inhibitor I39 (alpha-2-macroglobulin) family. Bacterial alpha-2-macroglobulin subfamily.
Protects the bacterial cell from host peptidases.
Belongs to the dTDP-4-dehydrorhamnose reductase family.
Binds 1 Mg(2+) ion per monomer. Mg(2+) is important for dimerization.
Involved in the biosynthesis of the dTDP-L-rhamnose which is an important component of lipopolysaccharide (LPS). Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose. RmlD uses NADH and NADPH nearly equally well.
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.
Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
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).
Auto-glycosylated: arginine GlcNAcylation is required for activity toward death domain-containing host target proteins.
Protein-arginine N-acetylglucosaminyltransferase effector that disrupts TNF signaling in infected cells, including NF-kappa-B signaling, apoptosis and necroptosis (PubMed:23955153, PubMed:28522607, PubMed:28069818). Acts by catalyzing the transfer of a single N-acetylglucosamine (GlcNAc) to a conserved arginine residue in the death domain of host proteins TRADD and, to a lower extent, FADD: arginine GlcNAcylation prevents homotypic/heterotypic death domain interactions and assembly of the oligomeric TNF-alpha receptor complex, thereby disrupting TNF signaling (PubMed:23955153, PubMed:28069818). Also acts on host proteins without a death domain: catalyzes arginine GlcNAcylation of host GAPDH protein, thereby preventing GAPDH interaction with TRAF2, leading to inhibit NF-kappa-B signaling (PubMed:28522607). Catalyzes GlcNAcylation of host tubulin-folding cofactor TBCB, thereby promoting microtubule stability (PubMed:32366039). Also mediates auto-GlcNAcylation, which is required for activity toward death domain-containing host target proteins (PubMed:32366039).
Transcription is dependent on PhoP/PhoQ two-component system.
Possible formation of a ternary complex RavA-ViaA-CadA.
Belongs to the asparagine synthetase family.
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. AstC subfamily.
Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase.
Belongs to the nucleoid occlusion factor SlmA family.
Required for nucleoid occlusion (NO) phenomenon, which prevents Z-ring formation and cell division over the nucleoid. Acts as a DNA-associated cell division inhibitor that binds simultaneously chromosomal DNA and FtsZ, and disrupts the assembly of FtsZ polymers. SlmA-DNA-binding sequences (SBS) are dispersed on non-Ter regions of the chromosome, preventing FtsZ polymerization at these regions.
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. 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.
Allosterically activated by fructose-1,6-bisphosphate (F16BP) and inhibited by AMP.
Belongs to the bacterial/plant glucose-1-phosphate adenylyltransferase family.
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.
Autokinase and kinase activities depend on low (uM range) Mg(2+) concentrations. Phosphatase activity is stimulated by high (mM range) Mg(2+) concentrations and ADP at 1 mM. Autokinase inhibited by radicicol.
Binds up to 3 divalent cations (Ca(2+) or Mg(2+)); increasing concentrations of divalent cations allows better binding to phospholipids.
Homodimer (Probable); probably dimerizes via the cytoplasmic domain. Interacts with MgrB in the periplasm, altering its activity and that of downstream effector PhoP (By similarity).
Member of the two-component regulatory system PhoP/PhoQ which regulates the expression of genes involved in virulence, adaptation to acidic and low Mg(2+) environments and resistance to host defense antimicrobial peptides. Essential for intramacrophage survival of S.typhimurium. In low periplasmic Mg(2+), PhoQ functions as a membrane-associated protein kinase that undergoes autophosphorylation and subsequently transfers the phosphate to PhoP, resulting in the expression of PhoP-activated genes (PAG) and repression of PhoP-repressed genes (PRG). In high periplasmic Mg(2+), acts as a protein phosphatase that dephosphorylates phospho-PhoP, resulting in the repression of PAG and may lead to expression of some PRG. Essential for transcription of spiC inside macrophages by controlling the expression of the two-component regulatory system SsrB/SpiR (SsrA) and Pir at transcriptional and post-transcriptional levels respectively. Promotes expression of the two-component regulatory system PmrA/PmrB via activation of pmrD gene. Is required to attenuate bacterial growth within fibroblast cells and to enhance bacterial resistance to bile in intestinal cells. Negatively regulates prgH, which is required for invasion of epithelial cells. Involved in acid tolerance.
Substitutions experiments show that amino acid Thr-48 may be involved in the conformational changes responsible for the balance between kinase-dominant state and phosphatase-dominant state.
The PhoP/PhoQ-signaling cascade, which activates virulence membrane genes (pagC, pagO, pagD, pagK, pgtE and phoN), is induced by cationic antimicrobial peptides (CAMP) (polymyxin, alpha-helical peptide C18G and sheet peptide protegrin-1) at sublethal concentrations.
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. Probably interacts with PlsY.
Belongs to the bacterial ribosomal protein bS20 family.
Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB) (PubMed:8206834, PubMed:10587435, PubMed:11441022, Ref.7, PubMed:24121107). Able to use a variety of other nucleotide bases as substrate to create alternative lower ligands for cobamide (PubMed:11441022, Ref.7, PubMed:24121107).
In vitro assays of this enzyme are performed at pH 10 because at physiological pH (7.0) its activity is undetectable; this makes it difficult to assess the role of mutagenesis of potential proton acceptor active site residues (Glu-174 and Glu-317) (PubMed:24121107).
No growth on cobinamide (CBI); double cobB-cobT deletion mutants do not grow on CBI and DMB (PubMed:8206834).
Adds the O-antigen on the glucose(II) group of LPS.
Belongs to the O-antigen polymerase family.
Catalyzes the ADP transfer from ATP to D-glycero-beta-D-manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-heptose.
Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7-phosphate at the C-1 position to selectively form D-glycero-beta-D-manno-heptose-1,7-bisphosphate.
In the C-terminal section; belongs to the cytidylyltransferase family.
In the N-terminal section; belongs to the carbohydrate kinase PfkB 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.
Member of a two-component regulatory system QseB/QseC. Activates the flagella regulon by activating transcription of flhDC (By similarity).
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).
Belongs to the polysaccharide deacetylase family. ArnD deformylase subfamily.
Catalyzes the deformylation of 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol to 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides (Probable).
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.
Associates with the 50S ribosomal subunit.
Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. EngA (Der) GTPase family.
GTPase that plays an essential role in the late steps of ribosome biogenesis.
Probably part of the PhnSTUV complex (TC 3.A.1.11.5) involved in 2-aminoethylphosphonate import.
Belongs to the phospholipase D family. Cardiolipin synthase subfamily. ClsB sub-subfamily.
Catalyzes the phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol.
Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). A mannose-binding adhesin (By similarity).
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.
A putative bidirectional acetate kinase that may drive flux through the ethanolamine (EA) degradation pathway under anoxic conditions found when this bacteria infects host intestine. It may generate ATP that can be used by other enzymes (EutA and EutT) in the eut pathway. Can use GTP instead of ATP with reduced efficiency (PubMed:26448059). Overexpression in E.coli yields elongated protein sheets; prevents artificial BMC formation by eutS alone or by eutK, eutL, eutM, eutN, eutS in E.coli (PubMed:27063436).
Not required for aerobic growth on ethanolamine (EA) supplemented with cobalamin (vitamin B12). A quadruple eutP-eutQ-eutT-eutD deletion is also not required for growth in the above conditions (PubMed:10464203). A non-polar deletion mutant grows on EA from pH 5.5 to pH 8.0, but does not grow at pH 8.5, releases slightly increased amounts of acetaldehyde on EA plus vitamin B12 (PubMed:16585748). No visible phenotype when grown on EA and tetrathionate under anoxic conditions (PubMed:26448059).
Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring. Also required for the recruitment to the septal ring of downstream cell division proteins.
Interacts with FtsZ via their C-terminal domains.
Belongs to the ABC transporter superfamily. Galactose/methyl galactoside importer (TC 3.A.1.2.3) family.
Part of the ABC transporter complex MglABC involved in galactose/methyl galactoside import. Responsible for energy coupling to the transport system.
Stimulated 3-fold by galactose and inhibited by vanadate, N-ethylmaleimide, and 5-methoxyindole-2-carboxylic acid.
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.
Belongs to the DEAD box helicase family. SrmB subfamily.
DEAD-box RNA helicase involved in the assembly of the 50S ribosomal subunit at low temperature. Exhibits RNA-stimulated ATP hydrolysis and RNA unwinding activity.
Interacts with the 50S ribosomal subunit.
Belongs to the chloride channel (TC 2.A.49) family.
Belongs to the OMP decarboxylase family. Type 1 subfamily.
Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
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.
Belongs to the radical SAM superfamily. 7-carboxy-7-deazaguanine synthase family.
Binds 1 S-adenosyl-L-methionine per subunit.
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.
Activated by inorganic phosphate (PubMed:4306285, PubMed:4324215). In addition to form a complex with ATP, Mg(2+) also acts as a cofactor (PubMed:4306285, PubMed:4324215). Strongly inhibited by ADP (or Mg-ADP) through competitive binding at the activation site and at a specific allosteric site (PubMed:4324215, PubMed:4346344, PubMed:6277896). Competitively inhibited by Ca(2+) (PubMed:4324215, PubMed:4346344).
Belongs to the ribose-phosphate pyrophosphokinase family. Class I subfamily.
Binds 2 Mg(2+) ions per subunit (Potential). Can also use Mn(2+) ions (PubMed:4306285).
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.
Dual transcriptional regulator of the TyrR regulon, which includes a number of genes coding for proteins involved in the biosynthesis or transport of the three aromatic amino acids, phenylalanine, tyrosine and tryptophan. These three aromatic amino acids act as effectors which bind to the TyrR protein to form an active regulatory protein. Acts by binding specifically to TyrR boxes in the promoter region of the target genes.
Homodimer. In presence of tyrosine (or high concentrations of phenylalanine or tryptophan) and ATP, it self-associates to form an hexamer.
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.
Binds to DNA non-specifically. Could be a regulatory factor involved in maltose metabolism.
Probably plays an important role in intracellular peptide degradation.
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. Forms a loose heterodimer with protein S19. Forms two bridges to the 50S subunit in the 70S ribosome.
Belongs to the acetokinase family. PduW subfamily.
Decreased propionate kinase activity, cells grow to lower density on 1,2-PD and excrete more propionate into the medium. A double pduW-pduX deletion grows as well as wild-type on 1,2-PD.
Was originally (Ref.1) thought to be AckA.
Works with phosphate acetyltransferase (pta) to capture exogenous propionate and regenerate propionyl-CoA during degradation of propionate and 1,2-propanediol (1,2-PD). Ectopic expression partially complements a cobB deletion allowing some growth on propionate (PubMed:12700259). Restores growth to an eutQ deletion on ethanolamine and tetrathionate under anoxic conditions (PubMed:26448059).
Cells display drastically reduced virulence in vitro and in vivo. Mice infected with the deletion mutant show no signs of illness during the course of the experiment. This suggests that the mutation results in defects in either invasion of intestinal epithelial cells, macrophage survival, or both.
Hfq expression was decreased during the space flight and expression of 64 genes of the hfq regulon was altered. Likewise, several small RNAs that interact with hfq were differentially regulated during the flight (PubMed:17901201).
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 (By similarity). Plays a central regulatory role in the microbial response to space flight conditions. Is essential for virulence and is required for efficient invasion of non-phagocytic cells.
Catalyzes the hydrolysis of 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) to 1,4-dihydroxy-2-naphthoate (DHNA).
A DNA-binding protein that acts in a fashion similar to H-NS, repressing gene transcription. A subset of H-NS/StpA-regulated genes require auxillary proteins for repression; these auxillary proteins (Hha and other similar proteins) may also modulate oligomerization of the H-NS/StpA complex (By similarity).
Belongs to the histone-like protein H-NS family.
Forms homodimers, can interact with H-NS.
Belongs to the NADPH-dependent sulphite reductase flavoprotein subunit CysJ family.
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.
In the N-terminal section; belongs to the flavodoxin family.
Belongs to the helicase family. DinG subfamily. Type 1 sub-subfamily.
DNA-dependent ATPase and 5'-3' DNA helicase.
Belongs to the glycosyltransferase 83 family.
Catalyzes the transfer of the L-Ara4N moiety of the glycolipid undecaprenyl phosphate-alpha-L-Ara4N to lipid A. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides.
Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1A (PBP1a).
Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP.
Belongs to the transpeptidase family. FtsI subfamily.
Catalyzes cross-linking of the peptidoglycan cell wall at the division septum.
In the C-terminal section; belongs to the glutathionylspermidine synthase preATP-grasp family.
Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
Homodecamer; pentamer of dimers. Binds only one seryl-tRNA(Sec) per dimer.
An anti-sigma factor for extracytoplasmic function (ECF) sigma factor sigma-E (RpoE). ECF sigma factors are held in an inactive form by an anti-sigma factor until released by regulated intramembrane proteolysis (RIP). 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, DegS), then within the membrane itself (site-2 protease, S2P, RseP), while cytoplasmic proteases finish degrading the anti-sigma factor, liberating sigma-E.
Interacts 1:1 with ECF RNA polymerase sigma-E (RpoE); this inhibits the interaction of sigma-E with the RNA polymerase catalytic core and leads to a decreased expression of sigma-E-regulated genes. Interacts with RseB.
Component of the PhsABC thiosulfate reductase that catalyzes the reduction of thiosulfate to sulfite and hydrogen sulfide, with menaquinol as the sole electron donor. Proton motive force (PMF) is required to drive transmembrane electron transfer within the reductase. The PhsA subunit contains the active site molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor.
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.
Involved in a secretory pathway responsible for the surface presentation of determinants needed for the entry of Salmonella species into mammalian cells. Chaperone specialized in the storage of effectors within the bacterial cytoplasm, maintaining them in a secretion-competent state, and allowing their immediate delivery to target cells upon contact of the bacterium with the host cells. Has been shown to chaperone SopA, SopE, SopE2 and SipA.
Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily.
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.
Inhibited by p-hydroxymercuribenzoate and N-ethylmaleimide, but not by iodoacetate or iodoacetamide.
Acts as a radical domain for damaged PFL and possibly other radical proteins.
Belongs to the BPG-independent phosphoglycerate mutase family.
Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 1 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).
Catalyzes the conversion of cobalt-precorrin-8 to cobyrinate.
Acetylates the N-terminal alanine of ribosomal protein S18.
Belongs to the acetyltransferase family. RimI subfamily.
Plays a role in the extracellular assembly of CsgA into thin aggregative fimbriae (Tafi) fibers. Assembly may also require CsgE. Tafi are thought to be assembled via an extracellular nucleation-precipitation (ENP) pathway, and possibly also via an intracellular non-CsgC-dependent pathway (By similarity).
Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
Homodimer. Part of the PDH complex, consisting of multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
Belongs to the bacterial ribosomal protein bS16 family.
In addition to being a ribosomal protein, S16 also has a cation-dependent endonuclease activity.
May be involved in the translocation process of the nascent O-polysaccharide molecules and/or its ligation to lipid A core units.
Involved in formation of the rod shape of the cell. May also contribute to regulation of formation of penicillin-binding proteins.
Belongs to the ABC transporter superfamily. Glutathione importer (TC 3.A.1.5.11) family.
Part of the ABC transporter complex GsiABCD involved in glutathione import. Responsible for energy coupling to the transport system.
Proton symporter that senses osmotic shifts and responds by importing osmolytes such as proline, glycine betaine, stachydrine, pipecolic acid, ectoine and taurine. It is both an osmosensor and an osmoregulator which is available to participate early in the bacterial osmoregulatory response (By similarity).
Belongs to the ABC transporter superfamily. Outer membrane lipopolysaccharide export (TC 1.B.42) family.
Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane. Probably responsible for energy coupling to the transport system.
Belongs to the universal ribosomal protein uL30 family.
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.
Catalyzes the dehydration of 6-phospho-D-gluconate to 2-dehydro-3-deoxy-6-phospho-D-gluconate.
By phosphate starvation and limiting magnesium, via the transcriptional regulator PhoP and the alarmone ppGpp.
Inhibits RpoS proteolysis by regulating RssB activity, thereby increasing the stability of the sigma stress factor RpoS especially during phosphate and magnesium starvation, but also in stationary phase and during nitrogen starvation. Its effect on RpoS stability is due to its interaction with RssB, which probably blocks the interaction of RssB with RpoS, and the consequent delivery of the RssB-RpoS complex to the ClpXP protein degradation pathway.
Ectopic overexpression in E.coli induces the YoeB toxin, but this is not the cause of VapC toxicity.
Induced by amino acid starvation and by chloramphenicol treatment.
Toxic component of a type II toxin-antitoxin (TA) system. A site-specific tRNA-(fMet) endonuclease, it cleaves both charged and uncharged tRNA-(fMet) between positions 38 and 39 at the anticodon stem-loop boundary. Does not cleave tRNA(Met), tRNA(Arg2), tRNA(His), tRNA(Leu), tRNA(Phe) tRNA(Thr1), tRNA(Tyr) or tRNA(Val). Overexpression in E.coli inhibits translation, leads to loss of cell growth and degradation of tRNA(fMet), these effects are neutralized by expression of cognate antitoxin VapB. Expression also activates translation initiation at correctly positioned elongator codons (AAA and to a lesser extent AAG).
Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
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.
Contributes to the efficiency of the cell division process by stabilizing the polymeric form of the cell division protein FtsZ. Acts by promoting interactions between FtsZ protofilaments and suppressing the GTPase activity of FtsZ.
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Transcriptional repressor of the FliC phase-1 flagellin.
Required for resistance to DNA-damaging agents.
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.
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.
Belongs to the class B bacterial acid phosphatase family.
Cells lacking this gene show a severely decreased growth rate on 5'-UMP as pyrimidine source.
Dephosphorylates several organic phosphate monoesters such as 3'-UMP, 5'-UMP and pNPP (PubMed:6256351). Also has a phosphotransferase activity catalyzing the transfer of low-energy phosphate groups from organic phosphate monoesters to free hydroxyl groups of various organic compounds such as the 2'-, 3-, or 5'-hydroxyls of nucleosides and nucleotides (PubMed:3049613). Also displays significant phosphomutase activity since it is able to catalyze the transfer of the phosphate group of 3'-AMP from the 3'-position both to the 2'- and 5'-positions. One of the physiological functions of the phosphohydrolytic activity of the enzyme is believed to be the scavenging of organic phosphate esters that otherwise cannot pass the cytoplasmic membrane (PubMed:6256351).
Nucleosides, and particularly 2'-deoxyribonucleosides, are potent inhibitors of the phosphatase activity. The phosphatase activity is also inhibited by inorganic phosphate and EDTA in vitro.
Aminoalkylphosphonate N-acetyltransferase which is able to acetylate a range of aminoalkylphosphonic acids, including (S)-1-aminoethylphosphonate ((S)-1AEP) and 2-aminoethylphosphonate, using acetyl-CoA as acetyl donor. Its physiological role in S.typhimurium is unclear. However, by acetylating (S)-1AEP, PhnO would protect against the deleterious effects of (S)-1AEP, a structural analog of D-alanine that has antibacterial properties.
Reaction proceeds via an ordered, sequential kinetic mechanism with AcCoA binding first followed by aminoalkylphosphonate.
Requires a divalent metal ion for activity. In vitro, exhibits a preference for Ni(2+) followed by Mn(2+) and very poor activity with Mg(2+). However, it is unclear what the physiologically relevant metal ion is.
A substrate-binding catalytic site, located on R1, is formed only in the presence of the second subunit R2.
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R2 contains the tyrosyl radical required for catalysis.
Tetramer of two alpha (R1) and two beta (R2) subunits. The B1 protein is a dimer of alpha subunits. A radical transfer pathway occurs between Tyr-123 of R2 and R1 (By similarity).
Belongs to the precorrin-6x reductase family.
Catalyzes the reduction of the macrocycle of cobalt-precorrin-6A to cobalt-precorrin-6B.
Belongs to the GpW/Gp25 family. IraD subfamily.
Inhibits RpoS proteolysis by regulating RssB activity, thereby increasing the stability of the sigma stress factor RpoS during oxidative stress. Its effect on RpoS stability is due to its interaction with RssB, which probably blocks the interaction of RssB with RpoS, and the consequent delivery of the RssB-RpoS complex to the ClpXP protein degradation pathway.
Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
A mutant in which deletion of the last 50 residues is combined with the 'Tyr-56' mutation in rsmG is highly resistant to streptomycin and has a small colony phenotype (which grow slowly and are resistant to aminoglycoside anitbiotics).
Belongs to the UbiA prenyltransferase family.
Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate.
Belongs to the band 7/mec-2 family. HflC subfamily.
HflC and HflK could regulate a protease.
Phosphorylated. Phosphorylation stimulates the interaction with RpoS and, therefore, the proteolysis of RpoS.
Regulates the turnover of the sigma S factor (RpoS) by promoting its proteolysis in exponentially growing cells. Acts by binding and delivering RpoS to the ClpXP protease. RssB is not co-degraded with RpoS, but is released from the complex and can initiate a new cycle of RpoS recognition and degradation.
Actin-binding protein that interferes with host cell actin cytoskeleton. Nucleates actin polymerization and condensates actin filaments into cables (bundling). SipA potenciates SipC activity and both are required for an efficient bacterial internalization by the host cell.
Belongs to the invasin protein C family.
Expression is under the control of the two-component regulatory system PhoQ/PhoP.
Belongs to the AAE transporter (TC 2.A.81) family. YbjL subfamily.
Belongs to the bacterial ribosomal protein bL32 family.
Acts as an alpha-ketoglutarate-dependent dioxygenase catalyzing hydroxylation of glutarate (GA) to L-2-hydroxyglutarate (L2HG). Functions in a L-lysine degradation pathway that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate.
Belongs to the glutarate hydroxylase family.
Catalyzes the esterification, concomitant with transport, of exogenous long-chain fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids.
Belongs to the cyclic nucleotide phosphodiesterase class-III family.
Hydrolyzes cAMP to 5'-AMP. Plays an important regulatory role in modulating the intracellular concentration of cAMP, thereby influencing cAMP-dependent processes.
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.
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 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.
Binds 1 divalent metal cation per subunit. Can probably use ions such as Zn(2+), Mg(2+) or Co(2+).
Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
The active site is located at the dimer interface.
RNA chaperone with significant RNA binding, RNA strand exchange and RNA duplexing activities. May regulate ProP activity through an RNA-based, post-transcriptional mechanism.
Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Involved in the cleavage of a C-terminal peptide of 11 residues from the precursor form of penicillin-binding protein 3 (PBP3). May be involved in protection of the bacterium from thermal and osmotic stresses (By similarity).
Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane).
Probably involved in the control of the structural glucose backbone of osmoregulated periplasmic glucans (OPGs).
Part of the mgtC/mgtB operon. Induced by low extracellular levels of Mg(2+). Transcriptionally regulated by extracellular magnesium via the two-component regulatory system PhoQ/PhoP.
Virulence factor required for growth in low Mg(2+) medium and for intramacrophage survival. May be involved in regulating membrane potential by activating Na(+)/K(+)-ATPase.
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.
IHF also plays a crucial role in the lysogenic life cycle of bacteriophage lambda, as it is required not only in the recombination reaction, which inserts lambda DNA into the E.coli chromosome, but also for the synthesis of int and cI repressor, two phage proteins necessary for DNA insertion and repression, respectively. The synthesis of int and cI proteins is regulated indirectly by IHF via translational control of the lambda cII protein.
Belongs to the Nudix hydrolase family. NudJ subfamily.
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. Putrescine aminotransferase subfamily.
Catalyzes the aminotransferase reaction from putrescine to 2-oxoglutarate, leading to glutamate and 4-aminobutanal, which spontaneously cyclizes to form 1-pyrroline. This is the first step in one of two pathways for putrescine degradation, where putrescine is converted into 4-aminobutanoate (gamma-aminobutyrate or GABA) via 4-aminobutanal. Also functions as a cadaverine transaminase in a a L-lysine degradation pathway to succinate that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate.
Responsible for preventing unproductive conjugation between bacteria carrying like plasmids.
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.
Involved in a late step of protoheme IX synthesis.
Involved in the assembly of lipopolysaccharide (LPS).
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).
Belongs to the HAD-like hydrolase superfamily. CbbY/CbbZ/Gph/YieH family.
Specifically catalyzes the dephosphorylation of 2-phosphoglycolate. Is involved in the dissimilation of the intracellular 2-phosphoglycolate formed during the DNA repair of 3'-phosphoglycolate ends, a major class of DNA lesions induced by oxidative stress.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIIB subfamily.
Induced by low levels of proline and by osmotic shock. The leader of mgtA mRNA functions as a riboswitch, favoring transcription under low Mg(2+) conditions. Under limiting proline levels the MgtL peptide encoded within the mgtA leader cannot be translated, thereby favoring the transcription of the mgtA ORF. Induction by osmotic shock also depends on translational regulation by MgtL (Probable). Induced by low extracellular levels of Mg(2+).
Mediates magnesium influx to the cytosol.
Part of the mgtC/mgtB operon. Induced by low extracellular levels of Mg(2+).
Belongs to the 3-oxoacid CoA-transferase family.
CoA transferase having broad substrate specificity for short-chain acyl-CoA thioesters with the activity decreasing when the length of the carboxylic acid chain exceeds four carbons.
Belongs to the protein kinase superfamily.
Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is a kinase, which is required for SPI-2 TTSS-dependent F-actin meshwork formation in infected host cells.
Expression is regulated by the two-component regulatory system SsrA/SsrB.
Belongs to the universal stress protein B family.
Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction. Has broad substrate specificity and can also utilize GTP, UTP and CTP. Can also phosphorylate propionate, but has very low activity with formate and is inactive with butyrate.
Does not grow on ethanolamine and tetrathionate under anoxic conditions; complemented by acetate kinases EutQ.
Inhibited by EDTA, butyrate and citrate.
A minor shell protein of the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation. The isolated BMC shell component protein ratio for J:A:B':B:K:T:U is approximately 15:10:7:6:1:1:2 (PubMed:12923081). Not required for structural integrity of BMCs nor to mitigate propionaldehyde toxicity, may selectively transport specific metabolites (PubMed:21239588). Proteins such as this one with circularly permuted BMC domains may play a key role in conferring heterogeneity and flexibility in this BMC (Probable).
Homohexamer with a central pore lined by a beta-barrel. Hexamers pack into a loose array (PubMed:18786396). Interacts with PduV, probably via the beta-barrel which is predicted by modeling to be on the exterior of the BMC (PubMed:25646976).
One side of the hexamer is concave which is lined by hydrophobic residues, the other side has a slightly protruding, 6-stranded beta-barrel which is occluded in PDB:3CGI by side chains.
Catalyzes the phosphorylation of riboflavin to FMN followed by the adenylation of FMN to FAD.
Catalyzes the hydrolysis of the ring A acetate delta-lactone of cobalt-precorrin-5A resulting in the loss of the C-20 carbon and its attached methyl group in the form of acetaldehyde.
An intermediate of this reaction is the autophosphorylated ppk in which a phosphate is covalently linked to a histidine residue through a N-P bond.
Belongs to the polyphosphate kinase 1 (PPK1) family.
Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP).
Belongs to the RNA methyltransferase RlmH family.
Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Involved in the degradation of phospho-AI-2, thereby terminating induction of the lsr operon and closing the AI-2 signaling cycle. Catalyzes the conversion of (4S)-4-hydroxy-5-phosphonooxypentane-2,3-dione (P-DPD) to 3-hydroxy-5-phosphonooxypentane-2,4-dione (P-HPD).
Component of the phosphoenolpyruvate-dependent nitrogen-metabolic phosphotransferase system (nitrogen-metabolic PTS), that seems to be involved in regulating nitrogen metabolism. Enzyme I-Ntr transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (NPr). Could function in the transcriptional regulation of sigma-54 dependent operons in conjunction with the NPr (PtsO) and EIIA-Ntr (PtsN) proteins. Enzyme I-Ntr is specific for NPr.
The EI 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 GAF domain is an important site of signal perception in prokaryotes and eukaryotes.
Belongs to the complex I subunit 4L family.
Belongs to the ETF beta-subunit/FixA family.
Belongs to the HAK/KUP transporter (TC 2.A.72) family.
Responsible for the low-affinity transport of potassium into the cell. Likely operates as a K(+):H(+) symporter.
Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Part of the ABC transporter complex PstSACB involved in phosphate import.
Dioxygenase that repairs alkylated DNA and RNA containing 3-methylcytosine or 1-methyladenine by oxidative demethylation. Has highest activity towards 3-methylcytosine. Has lower activity towards alkylated DNA containing ethenoadenine, and no detectable activity towards 1-methylguanine or 3-methylthymine. Accepts double-stranded and single-stranded substrates. Requires molecular oxygen, alpha-ketoglutarate and iron. Provides extensive resistance to alkylating agents such as MMS and DMS (SN2 agents), but not to MMNG and MNU (SN1 agents) (By similarity).
Belongs to the AB hydrolase superfamily. AB hydrolase 4 family.
Belongs to the ribonucleoside diphosphate reductase large chain family.
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R1 contains the binding sites for both substrates and allosteric effectors and carries out the actual reduction of the ribonucleotide.
S.typhimurium produces two separate class I enzymes. This one is the functional enzyme during growth.
Tetramer of two alpha (R1) and two beta (R2) subunits. The B1 protein is a dimer of alpha subunits. A radical transfer pathway occurs between 'Tyr-122' of R2 and R1.
Under complex allosteric control mediated by deoxynucleoside triphosphates and ATP binding to separate specificity and activation sites on the alpha subunit. 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. Stimulated by ATP and inhibited by dATP binding to the activity site (By similarity).
Catalyzes the transfer of an acetyl group from acetyl-CoA to the 6'-amino group of aminoglycoside molecules conferring resistance to antibiotics containing the purpurosamine ring.
Belongs to the aldolase class II family. RhaD subfamily.
Catalyzes the reversible cleavage of L-rhamnulose-1-phosphate to dihydroxyacetone phosphate (DHAP) and L-lactaldehyde.
Although this protein associates with the 30S subunit of the ribosome it is not considered to be a bona fide ribosomal protein.
Associates exclusively with the 30S subunit; there is 0.1 copy per ribosome in the exponential phase and 0.4 copies per ribosome in the stationary phase.
Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family. TrmL subfamily.
Methylates the ribose at the nucleotide 34 wobble position in the two leucyl isoacceptors tRNA(Leu)(CmAA) and tRNA(Leu)(cmnm5UmAA). Catalyzes the methyl transfer from S-adenosyl-L-methionine to the 2'-OH of the wobble nucleotide.
Cells lacking this gene are defective in aerobic degradation of propanediol (PubMed:9023178). Most cells lack BMCs, 22% have highly elongated internal structures, 20% have amorphous polar bodies. Grows in an interrupted manner on 1,2-PD and vitamin B12; grows for a while then stops, then restarts as if a toxic compound was accumulating and then decreases (PubMed:21239588). Grows faster under limiting vitamin B12 conditions, forms elongated BMCs (PubMed:24747050). A double pduJ-pduK strain grows in an interrupted manner on 1,2-PD and vitamin B12; grows for a while then stops, then restarts as toxic propionaldehyde accumulates and then decreases (PubMed:18296526). Makes elongated BMCs; this phenotype can be rescued by PduA or PduJ, but PduJ encoded on a plasmid cannot rescue a PduA deletion. When pduJ is cloned in the chromosomal position of pduA it substantially rescues the pduA deletion (PubMed:27561553, PubMed:33227310). Single pduA deletion makes BMCs but a double pduA-pduJ deletion does not (PubMed:33227310).
Homohexamer with a central pore of about 5.7 Angstroms in diameter (PubMed:27561553). Interacts with PduP, which targets PduP to the BMC (PubMed:22927404).
One of the major shell proteins of the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation. The isolated BMC shell component protein ratio for J:A:B':B:K:T:U is approximately 15:10:7:6:1:1:2 (PubMed:12923081). At least one of PduA or PduJ is required for BMC assembly; it must be encoded as the first gene in the pdu operon (PubMed:33227310, PubMed:27561553). Required for structural integrity of BMCs and to mitigate propionaldehyde toxicity, probably joins facets responsible for BMC closure (PubMed:21239588). Edge residues (particularly Lys-25) are important for function and assembly of the BMC (PubMed:24747050). 80% identical to PduA; although their pore regions appear structurally identical, unlike PduA plays no role in 1,2-PD diffusion into or out of the BMC shell. If pduJ is cloned in the chromosomal position of pduA it is able to complement a pduA deletion; it then has a functional pore as it assumes the transport functions of PduA (PubMed:27561553). Overexpression of this protein leads to aberrant filaments that extend the length of the cell, cross the cleavage furrow and impair division. The filaments form nanotubes with a hollow center (PubMed:33227310). Modeling suggests PduJ is probably the hub for binding multiple enzymes to the interior of the BMC; modeling suggests PduC, PduD, PduG and PduM are targeted to PduJ (Probable).
Belongs to the mandelate racemase/muconate lactonizing enzyme family. GalD subfamily.
Catalyzes the dehydration of D-galactonate to 2-keto-3-deoxy-D-galactonate.
Reaction proceeds via an anti dehydration.
Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
Belongs to the transferase hexapeptide repeat family. LpxA subfamily.
Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Exported via the flagellum-specific export pathway.
Flagellum-specific muramidase which hydrolyzes the peptidoglycan layer to assemble the rod structure in the periplasmic space.
In the C-terminal section; belongs to the glycosyl hydrolase 73 family.
In the N-terminal section; belongs to the FlgJ family.
Probably part of the PhnSTUV complex (TC 3.A.1.11.5) involved in 2-aminoethylphosphonate import. Probably responsible for the translocation of the substrate across the membrane.
Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. Involved in the aerobic and anaerobic degradation of long-chain fatty acids (By similarity).
Required for disulfide bond formation in some periplasmic proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by a yet uncharacterized protein. Also acts as a disulfide isomerase.
Is an L-glutamate ligase that catalyzes the ATP-dependent post-translational addition of glutamate residues to the C-terminus of ribosomal protein S6 (RpsF). Is also able to catalyze the synthesis of poly-alpha-glutamate in vitro, via ATP hydrolysis from unprotected glutamate as substrate. The number of glutamate residues added to either RpsF or to poly-alpha-glutamate changes with pH.
Belongs to the bacterial reverse transcriptase family.
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.
Mutants accumulate unmodified prolipoprotein due to a defect in the activity of prolipoprotein glyceryl transferase.
Responsible for synthesis of pseudouridine from uracil-516 in 16S ribosomal RNA.
Post-translationally modifies flagellin by methylation of epsilon amino group of surface-exposed lysine residues.
Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon.
Belongs to the biotin--protein ligase family.
Belongs to the DapA family. NanA subfamily.
Catalyzes the reversible aldol cleavage of N-acetylneuraminic acid (sialic acid; Neu5Ac) to form pyruvate and N-acetylmannosamine (ManNAc) via a Schiff base intermediate.
Regulation of the glyoxylate bypass operon, which encodes isocitrate lyase, malate synthase as well as isocitrate dehydrogenase kinase/phosphorylase.
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 UDP-glucose/GDP-mannose dehydrogenase family.
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.
FliM is one of three proteins (FliG, FliN, FliM) that forms 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 (By similarity).
Part of a tripartite efflux system composed of MdtA, MdtB and MdtC.
Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
By proline, autorepression and catabolite repression, and is potentially nitrogen controlled.
In the C-terminal section; belongs to the aldehyde dehydrogenase family.
In the N-terminal section; belongs to the proline dehydrogenase family.
Oxidizes proline to glutamate for use as a carbon and nitrogen source and also function as a transcriptional repressor of the put operon.
BMC production is induced by growth on 1,2-PD vitamin B12 medium (PubMed:10498708). By either propanediol or glycerol (PubMed:1312999).
Belongs to the diol/glycerol dehydratase large subunit family.
Cells lacking this gene are defective in aerobic degradation of propanediol and display no propanediol dehydratase activity (PubMed:9023178). A triple pduC-pduD-pduE deletion releases no acetaldehyde when grown on propanediol (PubMed:16585748).
Part of the PduCDE complex that catalyzes the dehydration of 1,2-propanediol (1,2-PD) to propionaldehyde. Required for S.typhimurium growth on 1,2-PD as the sole carbon and energy source (Probable) (PubMed:9023178). This subunit is directly targeted to the BMC (By similarity).
Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. 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.
Bifunctional enzyme that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides (By similarity).
Homohexamer, formed by a dimer of trimers.
In the C-terminal section; belongs to the NAD(P)-dependent epimerase/dehydratase family. UDP-glucuronic acid decarboxylase subfamily.
In the N-terminal section; belongs to the Fmt family. UDP-L-Ara4N formyltransferase subfamily.
Involved in resistance toward heavy metals.
Catalyzes the transfer of CDP-abequose on D-mannosyl-L-rhamnosyl-D-galactose-1-diphospholipid to yield D-abequosyl-D-mannosyl-rhamnosyl-D-galactose-1-diphospholipid.
Belongs to the inositol monophosphatase superfamily.
Homodimer. The rRNA transcription and antitermination complex (rrnTAC) consists of RNA polymerase (RNAP), NusA, NusB, NusE (rpsJ), NusG, SubB, ribosomal protein S4, DNA and precursor rRNA; S4 is more flexible than other subunits.
Part of the processive rRNA transcription and antitermination complex (rrnTAC). The complex forms an RNA-chaperone ring around the RNA exit tunnel of RNA polymerase (RNAP). It supports rapid transcription and antitermination of rRNA operons, cotranscriptional rRNA folding, and annealing of distal rRNA regions to allow correct ribosome biogenesis. This subunit may play a central role in organizing the structure.
Oxygen-regulated protein required for bacterial internalization.
Belongs to the chloride channel (TC 2.A.49) family. ClcB subfamily.
Probably acts as an electrical shunt for an outwardly-directed proton pump that is linked to amino acid decarboxylation, as part of the extreme acid resistance (XAR) response.
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.
Belongs to the ABC transporter superfamily. Lipid exporter (TC 3.A.1.106) family.
In MsbA the ATP-binding domain (NBD) and the transmembrane domain (TMD) are fused.
Involved in lipopolysaccharide (LPS) biosynthesis. Translocates lipid A-core from the inner to the outer leaflet of the inner membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Belongs to the P-Pant transferase superfamily. Gsp/Sfp/HetI/AcpT family.
May be involved in an alternative pathway for phosphopantetheinyl transfer and holo-ACP synthesis. The native apo-protein substrate is unknown.
Binds tightly to dsDNA (PubMed:10844682). Acts as a global transcriptional regulator through its ability to bind to AT-rich DNA sequences (PubMed:1423593, PubMed:16933988, PubMed:21673140). Binds in the minor groove of AT-rich DNA (PubMed:21673140). Was found to bind 746 genes, about half of which show no change in expression in disruption experiments suggesting these sites are important for nucleoid structure (PubMed:16933988). On a global level genes bound by H-NS are expressed at a lower than average level; H-NS is excluded from binding to highly transcribed genes and does not co-localize with RNA polymerase in DNA-binding studies during exponential growth in rich medium (PubMed:16933988). The best correlation for H-NS binding is AT-content rather than predicted DNA curvature (PubMed:16933988). Has a strong preference for DNA that has been recently acquired by horizontal gene transfer, binding strongly to Salmonella pathogenicity islands 1 and 2 (SPI1 and SPI2); this offers the selective advantage of silencing foreign DNA while keeping it in the genome in case of need (PubMed:16933988). DNA-binding influences plasmid DNA topology (PubMed:1423593). For the proU locus (the proV-proW-proX operon) inhibits transcription at low osmolarity by binding to AT-rich, curved, DNA downstream of the transcription start site of proV; repression is greater when more than 1 curved DNA sequence is present (PubMed:1423593). It plays a role in the thermal control of pili production (By similarity). It is subject to transcriptional auto-repression (By similarity). It binds preferentially to the upstream region of its own gene recognizing two segments of DNA on both sides of a bend centered around -150 (By similarity).
Composed of 2 domains (approximately residues 1-64 and 89-136) joined by a flexible linker. The isolated N-terminus (1-64) forms a trimer, probably via coiled-coil interactions (PubMed:10844682, PubMed:11237622). The isolated N-terminus plus linker fragment (residues 1-89) forms homooligomers of increasing size with increasing protein concentration, while the isolated C-terminus fragment is a monomer (PubMed:10844682). A shorter fragment (residues 1-46) interacts with Hha (PubMed:23515315).
Forms oligomers of increasing size with increasing protein concentration (PubMed:10844682, PubMed:23515315). The fragment of 1-83 probably forms oligomers of 4 dimeric units at 10 degrees Celsius, at 40 degrees Celsius only dimers are formed (PubMed:20798056). Binds Hha and YdgT (also known as cnu); crystal structures suggest each H-NS dimer could bind 2 Hha monomers on opposites sides (PubMed:23515315). Probably also binds StpA (By similarity).
Loss of osmotic regulation of the proU locus, loss of changes in plasmid linking number (PubMed:1423593). 2X decreased growth rate, which is partially restored by a mutation preventing expression of SPI2, increased expression of about half of the genes to which H-NS binds (PubMed:16933988). Note strain LT2 has point mutation in rpoS which decreases its translation efficiency, in the presence of wild-type rpoS, deletion of hns is lethal (PubMed:16933988).
Part of the ABC transporter complex CysAWTP (TC 3.A.1.6.1) involved in sulfate/thiosulfate import. Probably responsible for the translocation of the substrate across the membrane.
Belongs to the multicopper oxidase family.
By CueR, at increased levels of cytoplasmic cuprous ions.
Multicopper oxidase involved in copper homeostasis and copper tolerance under both aerobic and anaerobic conditions (PubMed:12442888, PubMed:17768242). Is responsible for the oxidation of Cu(+) to the less harmful Cu(2+) in the periplasm, thereby preventing Cu(+) from entering the cytoplasm (By similarity).
Mutant is very sensitive to copper after copper shock (PubMed:12442888). Causes a moderate defect in aerobic growth on CuSO(4), strongly impairs survival during anaerobic growth on CuSO(4) (PubMed:17768242).
Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.
Mutants have a reduced pyruvate oxidase activity and a reduced growth rate, and are highly attenuated for virulence in mouse models of infection. Salmonella epmA and epmB mutants share extensive phenotypic pleiotropy, including an increased ability to respire under nutrient-limiting conditions, hypersusceptibility to a variety of diverse growth inhibitors, and altered expression of multiple proteins, including several encoded on the SPI-1 pathogenicity island.
With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of EF-P 'Lys-34' (Probable). Can also use L-alpha-lysine as a substrate, but probably with lower efficiency. Cannot aminoacylate tRNA(Lys) with lysine.
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.
Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfB subfamily.
Belongs to the major facilitator superfamily. Proton-dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family.
Involved in muropeptide degradation. Catalyzes the hydrolysis of the gamma-D-glutamyl-diaminopimelic acid (gamma-D-Glu-Dap) amide bond in the murein tripeptide L-alanyl-gamma-D-glutamyl-meso-diaminopimelic acid, leading to the formation of L-Ala-gamma-D-Glu and Dap.
Cleaves the N-terminal amino acid of tripeptides. Hydrolyzes tripeptides containing N-terminal methionine, leucine, or phenylalanine. Displays little or no activity against dipeptides, N-blocked or C-blocked tripeptides, and tetrapeptides.
Belongs to the metallo-dependent hydrolases superfamily. Uronate isomerase family.
Belongs to the glucose-6-phosphate dehydrogenase family.
Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone.
1.5-fold induced in nutrient-poor medium.
Functions in complex with FlhC as a master transcriptional regulator that regulates transcription of several flagellar and non-flagellar operons by binding to their promoter region. Activates expression of class 2 flagellar genes, including fliA, which is a flagellum-specific sigma factor that turns on the class 3 genes. Also regulates genes whose products function in a variety of physiological pathways (Probable).
Homodimer; disulfide-linked. Forms a heterohexamer composed of two FlhC and four FlhD subunits. Each FlhC binds a FlhD dimer, forming a heterotrimer, and a hexamer assembles by dimerization of two heterotrimers (Probable). This subunit binds DNA and interacts with YdiV, which decreases its ability to bind DNA.
The C-terminal region contains a putative helix-turn-helix (HTH) motif, suggesting that this region may bind DNA.
Belongs to the phospholipase D family. Cardiolipin synthase subfamily. ClsA sub-subfamily.
Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol.
Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.
Belongs to the dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family. GltP subfamily.
Catalyzes the proton-dependent transport of glutamate and aspartate.
Belongs to the SMC family. SbcC subfamily.
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.
Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. Epd subfamily.
Catalyzes the NAD-dependent conversion of D-erythrose 4-phosphate to 4-phosphoerythronate.
FliG is one of three proteins (FliG, FliN, FliM) that forms 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 (By similarity).
Belongs to the ABC transporter superfamily. Zinc importer (TC 3.A.1.15.5) family.
Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system (Probable). Seems to be important for the virulence.
The complex is composed of two ATP-binding proteins (ZnuC), two transmembrane proteins (ZnuB) and a solute-binding protein (ZnuA).
Transcriptionally repressed by zur (zinc uptake regulator), in response to high extracellular zinc concentrations.
Belongs to the methyltransferase superfamily. RlmKL family.
Specifically methylates the guanine in position 2445 (m2G2445) and the guanine in position 2069 (m7G2069) of 23S rRNA.
Binds 1 heme b (iron(II)-protoporphyrin IX) group per molecule.
Electron-transport protein of unknown function.
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).
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 (By similarity).
Probably acts on the acetaldehyde produced by the degradation of ethanolamine, producing ethanol.
Unable to grow with ethanolamine (EA) as sole carbon source. Slightly attenuated in a mouse model of infection (PubMed:7868611). Not required for aerobic growth on EA supplemented with cobalamin (vitamin B12). A double eutJ-eutG deletion is not required for growth on EA supplemented with vitamin B12 (PubMed:10464203). A non-polar deletion mutant grows on EA at pH 5.5 to pH 7.0 but not at pH 8.0 or pH 8.5, releases increased amounts of acetaldehyde on EA plus vitamin B12. Preventing acetaldehyde vapor loss allow growth up to pH 8.5 (PubMed:16585748).
Belongs to the YigI thioesterase family.
Displays thioesterase activity against medium- to long-chain acyl-CoA substrates (By similarity). Is involved in the thioesterase-dependent beta-oxidation pathway of (9Z,11E)-octadecadienoate (conjugated linoleic acid or CLA), along with TesB and FadM (By similarity).
Belongs to the AFG1 ATPase family. ZapE subfamily.
Reduces the stability of FtsZ polymers in the presence of ATP.
Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Binds maltose and higher maltodextrins.
Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either CheB or CheY.
May have three functional domains: one for interaction with CheB and CheY, a second for regulating phosphorylation and controlling the stability of the protein, and a third for receiving input signals regulating CheA activity.
Chaperone for NapA, the catalytic subunit of the periplasmic nitrate reductase. It binds directly and specifically to the twin-arginine signal peptide of NapA, preventing premature interaction with the Tat translocase and premature export.
Belongs to the PHP family. TrpH/YciV subfamily.
Exoribonuclease that catalyzes the last steps of 5S, 16S and 23S rRNA 5'-end maturation. Removes 3 nucleotides (nt) from the 5' end of 5S, 16S and 23S rRNA precursors to generate the mature 5' ends. 5S and 23S rRNA maturation occurs more efficiently and accurately on ribosomal particles as compared to free RNA. Efficiently catalyzes the hydrolysis of the 3'-phosphate from 3',5'-bis-phosphonucleotides as well as the successive hydrolysis of 5'-phosphomononucleotides from the 5'-end of short pieces of RNA and DNA, with no specificity toward the identity of the nucleotide base. Is more efficient at hydrolyzing RNA oligonucleotides than DNA oligonucleotides. This enzyme can also hydrolyze annealed DNA duplexes, albeit at a catalytic efficiency lower than that of the corresponding single-stranded oligonucleotides.
A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and facilitates RecA-binding to the ssDNA for homologous DNA recombination and repair. Holoenzyme degrades any linearized DNA that is unable to undergo homologous recombination. In the holoenzyme this subunit has ssDNA-dependent ATPase and 5'-3' helicase activity. When added to pre-assembled RecBC greatly stimulates nuclease activity and augments holoenzyme processivity. Negatively regulates the RecA-loading ability of RecBCD.
Belongs to the NAD(P)-dependent epimerase/dehydratase family. Fucose synthase subfamily.
Catalyzes the two-step NADP-dependent conversion of GDP-4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction.
Belongs to the outer membrane OOP (TC 1.B.6) superfamily. Ail family.
Essential for full virulence and survival within macrophages.
Responsible for synthesis of pseudouridine from uracil-65 in transfer RNAs.
Belongs to the formate dehydrogenase gamma subunit family.
A key translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability. Mediates global changes in gene expression, shifting from rapid growth to stress survival by linking envelope stress, the stringent response and the catabolite repression systems. Usually binds in the 5'-UTR; binding at or near the Shine-Dalgarno sequence prevents ribosome-binding, repressing translation, binding elsewhere in the 5'-UTR can activate translation and/or stabilize the mRNA. Its function is antagonized by small RNA(s).
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.
Deletion mutants display increased resistance to oxidative stress, increased catalase activity and increased survival in macrophage cells. Deletion results in the altered expression of 82 and 56 genes in log and stationary phase, respectively.
Deletion of the N- or the C-terminal 10 amino acids abolishes activity, while a region that includes amino acids 56 to 80 is dispensable for activity. Contains a predicted HTH motif, which may bind DNA.
Involved in oxidative stress resistance.
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).
HIU hydrolysis also occurs spontaneously, but more slowly.
A component of the bacterial microcompartment (BMC) shell dedicated to ethanolamine degradation. Expression of eutK, eutL, eutM, eutN, eutS (eutSMNLK) in E.coli leads to formation of a single BMC (PubMed:22428024, PubMed:27063436). Coexpression of eutQ with eutSMNLK permits E.coli to make cells with more than one mobile BMC, as is usual in vivo (PubMed:27063436).
Artificial BMCs can be made in E.coli by expressing eutK, eutL, eutM, eutN, eutS (eutSMNLK) or eutS alone. Cargo proteins can be targeted to them and beta-galactosidase (lacZ) was active within the BMC, showing the BMC allows passage of substrate into the interior. This can lead to the development of tailored BMCs for specific metabolic reactions (PubMed:22428024, PubMed:27063436). The addition of eutQ to the eutSMNLK construct results in biogenesis of multiple BMCs (PubMed:27063436).
Involved in the biosynthesis of 3-deoxy-D-manno-octulosonate (KDO), a unique 8-carbon sugar component of lipopolysaccharides (LPSs). Catalyzes the reversible aldol-ketol isomerization between D-ribulose 5-phosphate (Ru5P) and D-arabinose 5-phosphate (A5P) (By similarity).
Rhomboid-type serine protease that catalyzes intramembrane proteolysis.
Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. Required, with TolQ, for the proton motive force-dependent activation of TolA and for TolA-Pal interaction.
Binds two Mg(2+) per subunit. The active form of the enzyme binds two Mg(2+) ions in its active site. The first Mg(2+) forms only one salt bridge with the protein.
Trims short 3' overhangs of a variety of RNA species, leaving a one or two nucleotide 3' overhang. Responsible for the end-turnover of tRNA: specifically removes the terminal AMP residue from uncharged tRNA (tRNA-C-C-A). Also appears to be involved in tRNA biosynthesis.
Involved in negative control of bacterial proliferation within fibroblasts.
Induced in response to increased extracellular osmolarity, this is the third gene of the proU operon (proV-proW-proX). Osmoregulation requires curved DNA downstream of the transcription start site in proV, which is repressed when bound by H-NS. H-NS may act indirectly to influence the local topology of the promoter (PubMed:1423593).
Part of the ProU ABC transporter complex involved in glycine betaine and proline betaine uptake. Binds glycine betaine and proline betaine with high affinity.
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.
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 (By similarity).
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.
Belongs to the TatA/E family. TatE subfamily.
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. TatE shares overlapping functions with TatA.
Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol, an intermediate step in ubiquinone biosynthesis.
For insertion of FliP into the membrane, cleavage of the signal peptide is important kinetically but not absolutely required.
Plays a role in the flagellum-specific transport system.
Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
Provides the cells with the ability to utilize trehalose at high osmolarity by splitting it into glucose molecules that can subsequently be taken up by the phosphotransferase-mediated uptake system.
Part of the binding-protein-dependent transport system for oligopeptides. Probably responsible for energy coupling to the transport system.
Belongs to the major facilitator superfamily. DHA1 family. MdtL (TC 2.A.1.2.22) subfamily.
Small subunit of the propanediol dehydratase-reactivating factor (DDR), which reactivates suicidally inhibited adenosylcobalamin-dependent propanediol dehydratase (diol dehydratase, DDH) found in the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation. Reactivates inactivated DDH in the presence of ATP, Mg(2+) and free adenosylcobalamin (AdoCbl), by mediating the exchange of the tightly bound damaged cofactor AdoCbl for a free intact one.
Belongs to the bacterial ribosomal protein bL28 family.
Involved in succinate export with YjjP. Both proteins are required for export.
The transporter is composed of YjjB and YjjP.
Component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (PubMed:28283062). Acts as a regulator of the InvC/SctN1 ATPase activity (By similarity). Required for invasion and secretion (PubMed:10816487).
Deletion of the gene disrupts proper SpaO/SctQ localization.
The core secretion machinery of the T3SS is composed of approximately 20 different proteins, including cytoplasmic components, a base, an export apparatus and a needle (PubMed:30107569, PubMed:28283062). This subunit is part of the cytosolic complex (PubMed:28283062, PubMed:31288030). Interacts directly with InvC/SctN1 (T3SS-1 ATPase) and SpaO/SctQ (the major sorting platform component) (PubMed:15060043, PubMed:25994170, PubMed:28283062, PubMed:31288030). Forms homodimers (PubMed:31288030).
More senstitive to protamine than wild-type cells, but not as sensitive as sapC, sapD or sapF deletions.
A site-2 regulated intramembrane protease (S2P) that cleaves the peptide bond between 'Ala-108' and 'Cys-109' in the transmembrane region of RseA. Part of a regulated intramembrane proteolysis (RIP) cascade. Acts on DegS-cleaved RseA to release the cytoplasmic domain of RseA. This provides the cell with sigma-E (RpoE) activity through the proteolysis of RseA (By similarity).
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 (By similarity).
The 2 circularly premutated PDZ domains act to negatively regulate protease action on intact RseA.
Belongs to the peptidase M24B family. Bacterial-type prolidase subfamily.
Splits dipeptides with a prolyl residue in the C-terminal position.
Sequence-specific endonuclease that cleaves unmethylated GATC sequences. It is involved in DNA mismatch repair.
Belongs to the LpxL/LpxM/LpxP family. LpxM subfamily.
Catalyzes the transfer of myristate from myristoyl-acyl carrier protein (ACP) to Kdo(2)-(lauroyl)-lipid IV(A) to form Kdo(2)-lipid A.
Component of the lipopolysaccharide transport and assembly complex. Interacts with LptE and LptA.
Contains two intramolecular disulfide bonds.
Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane.
Globally modulates RNA abundance by binding to RNase E (Rne) and regulating its endonucleolytic activity. Can modulate Rne action in a substrate-dependent manner by altering the composition of the degradosome.
Interacts with the C-terminal region of Rne.
Activation requires a sequential transfer of a phosphate group from a His in the primary transmitter domain, to an Asp in the receiver domain and to a His in the secondary transmitter domain.
Translation factor necessary for the incorporation of selenocysteine into proteins. It probably replaces EF-Tu for the insertion of selenocysteine directed by the UGA codon. SelB binds GTP and GDP.
Belongs to the glucose-1-phosphate cytidylyltransferase family.
Catalysis proceeds via a sequential rather than a ping-pong bi-bi reaction mechanism.
Involved in the biosynthesis of the tyvelose, a 3,6-dideoxyhexose found in the O-antigen of the surface lipopolysaccharides. It catalyzes the transfer of a CMP moiety from CTP to glucose 1-phosphate (By similarity).
Acts as an anti-FlhC(2)FlhD(4) factor by binding to FlhD, decreasing its ability to bind DNA, and thus negatively regulates expression of flagellar class II operons, decreasing motility in nutrient-poor medium. Required for resistance to host phagocyte oxidase. Suppresses killing of macrophages, while promoting resistance to hydrogen peroxide. Data regarding c-di-GMP is controversial; suppresses bacterial c-di-GMP levels (PubMed:15882417) but neither synthesizes nor degrades c-di-GMP (PubMed:19376870).
Decreased bacterial resistance to hydrogen peroxide and accelerated bacterial killing of macrophages. increased levels of c-di-GMP (PubMed:15882417). Down-regulation of rdar morphology, 50% reduction in CsgD expression, cellulose and curli fimbriae, increased swimming and swarming. Decrease in c-di-GMP levels (PubMed:19376870). Derepresses transcription of flagellar class II operons in nutrient-poor medium.
Has been proposed to be involved in c-di-GMP turnover (PubMed:15882417), but also not be involved in its turnover (PubMed:19376870). Mutagenesis of Glu-29 in the EAL domain suggests if this protein has c-di-GMP phosphdiesterase activity it is not involved in motility regulation (PubMed:21278297). Note that (PubMed:15882417) and (PubMed:19376870) experiments were done in strain 14028, which is not an LT2 derivative.
Induced in nutrient-poor medium (at protein level).
The multicellular rdar morphotype is characterized by the expression of the adhesive extracellular matrix components cellulose and curli fimbriae.
Belongs to the bacterial PQQ dehydrogenase family.
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.
This protein is a component of the leucine, isoleucine, valine, threonine transport system, which is one of the two periplasmic binding protein-dependent transport systems of the high-affinity transport of the branched-chain amino acids.
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).
Catalyzes the reduction of crotonobetainyl-CoA to gamma-butyrobetainyl-CoA.
Belongs to the YdjC deacetylase family. ChbG subfamily.
Involved in the degradation of chitin. ChbG is essential for growth on the acetylated chitooligosaccharides chitobiose and chitotriose but is dispensable for growth on cellobiose and chitosan dimer, the deacetylated form of chitobiose. Deacetylation of chitobiose-6-P and chitotriose-6-P is necessary for both the activation of the chb promoter by the regulatory protein ChbR and the hydrolysis of phosphorylated beta-glucosides by the phospho-beta-glucosidase ChbF. Catalyzes the removal of only one acetyl group from chitobiose-6-P to yield monoacetylchitobiose-6-P, the inducer of ChbR and the substrate of ChbF.
Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.
Catalyzes the reversible hydration of fumarate to (S)-malate. Functions as an aerobic enzyme in the direction of malate formation as part of the citric acid cycle. Accounts for about 80% of the fumarase activity when the bacteria grow aerobically. To a lesser extent, also displays D-tartrate dehydratase activity in vitro, but is not able to convert (R)-malate, L-tartrate or meso-tartrate. Can also catalyze the isomerization of enol- to keto-oxaloacetate.
Is expressed under aerobic conditions. Is repressed by glucose and anaerobiosis.
Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. May act as a translocator that mediates translocation of SPI-2 TTSS effector proteins from intraphagosomal bacterial cells into the host cells. SseB is required for correct localization of SseC and SseD on the bacterial cell surface.
May form a complex with SseC and SseD. Binds to the chaperone SseA.
Mutant is severely attenuated in virulence. Disruption prevents SpvB-induced F-actin depolymerization in human macrophages without affecting intra-bacterial SpvB protein levels.
Has an N-terminal adenylyltranferase and a C-terminal helical domain, with an ATP-binding cleft between them (PubMed:26527143, PubMed:29871922). Upon ATP binding the two domains reposition, antibiotics bind in this cleft (PubMed:29871922).
Induced by growth in minimal media (at protein level). Under positive control of the stringent response regulator guanosine 3',5'-bis(diphosphate) (ppGpp).
Loss of streptomycin and spectinomycin resistance.
Mediates bacterial resistance to the antibiotics streptomycin and spectinomycin, does not confer resistance to kanamycin (PubMed:26527143). Binds ATP first, then antibiotic (PubMed:26527143, PubMed:29871922).
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 1 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. Also shows phosphatase, 2'-nucleotidase and 2',3'-cyclic phosphodiesterase activities. These phosphohydrolase activities are probably involved in the repair of the tRNA 3'-CCA terminus degraded by intracellular RNases.
Comprises two domains: an N-terminal domain containing the nucleotidyltransferase activity and a C-terminal HD domain associated with both phosphodiesterase and phosphatase activities.
Magnesium is required for nucleotidyltransferase activity.
Monomer. Can also form homodimers and oligomers.
One of the proteins required for the normal export of preproteins out of the cell cytoplasm. It is a molecular chaperone that binds to a subset of precursor proteins, maintaining them in a translocation-competent state. It also specifically binds to its receptor SecA.
Belongs to the transaldolase family. Type 1 subfamily.
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Feed-back regulated by NAD. A high level of NAD causes NadR to lose enzymatic activity and repress several NAD synthetic genes; conversely, a low NAD level activates the assimilatory enzymatic activities and leads to derepression of biosynthetic genes.
In the C-terminal section; belongs to the bacterial RNK family.
In the central section; belongs to the bacterial NMN adenylyltransferase family.
This enzyme has three activities: DNA binding, nicotinamide mononucleotide (NMN) adenylyltransferase and ribosylnicotinamide (RN) kinase. The DNA-binding domain binds to the nadB operator sequence in an NAD- and ATP-dependent manner. As NAD levels increase within the cell, the affinity of NadR for the nadB operator regions of nadA, nadB, and pncB increases, repressing the transcription of these genes. The RN kinase activity catalyzes the phosphorylation of RN to form nicotinamide ribonucleotide. The NMN adenylyltransferase activity catalyzes the transfer of the AMP moiety of ATP to nicotinamide ribonucleotide to form NAD(+). The NMN adenylyltransferase domain also functions as the NAD and ATP sensor.
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 (By similarity).
Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Involved in allosteric regulation of aspartate carbamoyltransferase.
Belongs to the glycosyl hydrolase 3 family.
Proteolytic processing gives rise to the active protein.
Required for growth and/or survival at acidic conditions.
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.
Consists of a catalytic RNA component (M1 or rnpB) and a protein subunit.
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.
A peripheral cell membrane enzyme that catalyzes the oxidative decarboxylation of pyruvate to form acetate and CO(2). It channels electrons from the cytoplasm to the respiratory chain at the cell membrane via ubiquinone.
Has 4 domains; the Pyr domain which binds the pyrimidine moiety of the thiamine pyrophosphate cofactor, the FAD-binding domain, the PP-binding domain which binds the pyrophosphate portion of thiamine pyrophosphate and the C-terminal membrane binding region. The C-terminus is held closely against the rest of the protein and covers the active site; during activation it unfolds from the rest of the protein and forms an amphipathic helix upon membrane binding, exposing the active site.
The C-terminus inhibits activity; it has to move for the enzyme to be active. Activated by lipid-binding, which occurs via the C-terminus.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family. RlmC subfamily.
Catalyzes the formation of 5-methyl-uridine at position 747 (m5U747) in 23S rRNA.
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).
Isoleucine allosterically inhibits whereas valine allosterically activates this enzyme.
Binds single-stranded DNA at the primosome assembly site (PAS). During primosome assembly it facilitates the complex formation between PriA and DnaT.
Component of the preprimosomal complex composed of one monomer of PriC and DnaT, two monomers of PriA, two dimers of PriB and one hexamer of DnaB. Upon transient interaction with DnaG it forms the primosome.
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 enzymes involved in arginine catabolism. The open complex (sigma-54 and core RNA polymerase) serves as the receptor for the receipt of the melting signal from the remotely bound activator protein GlnG(NtrC).
Removes dipeptides from the C-termini of N-blocked tripeptides, tetrapeptides and larger peptides.
Unable to grow on N-acetyl-Ala-Ala-Ala as a nitrogen source.
Member of the two-component regulatory system TtrR/TtrS, which is required for synthesis of tetrathionate reductase. Positively regulates transcription of the ttrBCA operon. During mice infection, the ability to use tetrathionate as an electron acceptor is a growth advantage for S.typhimurium over the competing microbiota in the lumen of the inflamed gut.
Non-essential cell division protein that could be required for efficient cell constriction.
The SPOR domain binds septal peptidoglycans and is required to target DedD to the septal ring.
Binds 2 divalent metal cations. Magnesium or manganese.
DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contains the editing function and is a proofreading 3'-5' exonuclease (By similarity).
The DNA polymerase holoenzyme is a complex that contains 10 different types of subunits. These subunits are organized into 3 functionally essential subassemblies: the pol III core, the beta sliding clamp processivity factor and the clamp-loading complex. The pol III core (subunits alpha,epsilon and theta) contains the polymerase and the 3'-5' exonuclease proofreading activities. The polymerase is tethered to the template via the sliding clamp processivity factor. The clamp-loading complex assembles the beta processivity factor onto the primer template and plays a central role in the organization and communication at the replication fork. This complex contains delta, delta', psi and chi, and copies of either or both of two different DnaX proteins, gamma and tau. The composition of the holoenzyme is, therefore: (alpha,epsilon,theta)[2]-(gamma/tau)[3]-delta,delta', psi,chi-beta[4] (By similarity).
Probably functions as a manganese efflux pump.
Part of the constitutive potassium transport systems TrkG and TrkH. May regulate the transport activity of TrkG and TrkH systems. Binds to NAD(+) and NADH. In Salmonella it is required for resistance to antimicrobial peptides.
The RCK N-terminal domain binds NAD and possibly other effectors. This is expected to cause a conformation change that regulates potassium transport (By similarity).
Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily.
Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2-cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family. RlmD subfamily.
Catalyzes the formation of 5-methyl-uridine at position 1939 (m5U1939) in 23S rRNA.
Member of the two-component regulatory system EnvZ/OmpR involved in osmoregulation (particularly of genes ompF and ompC) as well as other genes (By similarity). Plays a central role in both acid and osmotic stress responses. Binds to the promoter of both ompC and ompF; at low osmolarity it activates ompF transcription, while at high osmolarity it represses ompF and activates ompC transcription (By similarity).
Phosphorylated by EnvZ; this stimulates its DNA-binding ability. Asp-55 is the primary phosphate acceptor site.
NADP-dependent dehydrogenase with broad substrate specificity acting on 3-hydroxy acids. Catalyzes the NADP-dependent oxidation of L-allo-threonine to L-2-amino-3-keto-butyrate, which is spontaneously decarboxylated into aminoacetone. Also acts on D-threonine, L-serine, D-serine, D-3-hydroxyisobutyrate, L-3-hydroxyisobutyrate, D-glycerate and L-glycerate. Able to catalyze the reduction of the malonic semialdehyde to 3-hydroxypropionic acid. YdfG is apparently supplementing RutE, the presumed malonic semialdehyde reductase involved in pyrimidine degradation since both are able to detoxify malonic semialdehyde.
Belongs to the aconitase/IPM isomerase family. LeuC type 1 subfamily.
Interacts with the SecY protein in vivo. May bind preferentially to an uncomplexed state of SecY, thus functioning either as a chelating agent for excess SecY in the cell or as a regulatory factor that negatively controls the translocase function.
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.
Composed of an N- and a C-terminal domain. The N-terminal domain carries the tetrahydrofolate (THF)-binding site and the C-terminal domain is presumably involved in positioning the Met-tRNA substrate for the formylation reaction.
Catalyzes the dehydrogenation of L-2-hydroxyglutarate (L2HG) to alpha-ketoglutarate and couples to the respiratory chain by feeding electrons from the reaction into the membrane quinone pool. Functions in a L-lysine degradation pathway that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate.
Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. Contributes to the formation of Salmonella-induced filaments (Sifs) in infected epithelial cells and to replication in macrophages.
Mutation leads to a prolonged survival of infected mice. Deletion blocks Sifs formation at an intermediate stage, before fusion of late endosome compartments with the SCV, and impairs bacterial replication in mouse macrophages but not in human epithelial cells.
The N-terminal domain mediates secretion by SPI-2 TTSS and targeting of late endocytic compartments in host cells.
Transcription is induced inside host cells and is dependent on the SsrA/SsrB and PhoP/PhoQ two-component systems.
Belongs to the glycosyl hydrolase 30 family.
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).
Belongs to the monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family. NhaP2 subfamily.
K(+)/H(+) antiporter that extrudes potassium in exchange for external protons and maintains the internal concentration of potassium under toxic levels.
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.
Belongs to the acyl carrier protein (ACP) family.
Carrier of the growing fatty acid chain in fatty acid biosynthesis.
Belongs to the TorD/DmsD family. DmsD subfamily.
Required for biogenesis/assembly of DMSO reductase, but not for the interaction of the DmsA signal peptide with the Tat system. May be part of a chaperone cascade complex that facilitates a folding-maturation pathway for the substrate protein.
Repressor of the galactose operon. Binds galactose as an inducer (By similarity).
Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
Impaired for BMC assembly, with a disrupted, unstable BMC shell.
Plays an essential role in assembly and/or stability of the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation. Overexpression impairs BMC formation.
Belongs to the SIS family. GmhA subfamily.
Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate.
The reaction produces a racemic mixture of D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate.
Belongs to the glutamate--cysteine ligase type 1 family. Type 1 subfamily.
Belongs to the class I-like SAM-binding methyltransferase superfamily. CmoB family.
Catalyzes carboxymethyl transfer from carboxy-S-adenosyl-L-methionine (Cx-SAM) to 5-hydroxyuridine (ho5U) to form 5-carboxymethoxyuridine (cmo5U) at position 34 in tRNAs.
Deletion results in tRNA having 5-hydroxyuridine (ho5U34) instead of cmo5U34.
In the N-terminal section; belongs to the CRISPR-associated nuclease Cas3-HD family.
In the central section; belongs to the CRISPR-associated helicase Cas3 family.
Belongs to the RbsD / FucU family. RbsD subfamily.
Catalyzes the interconversion of beta-pyran and beta-furan forms of D-ribose.
Belongs to the vitamin-B12 dependent methionine synthase family.
Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate (By similarity).
L-homocysteine is bound via the zinc atom.
Modular enzyme with four functionally distinct domains. The isolated Hcy-binding domain catalyzes methyl transfer from free methylcobalamin to homocysteine. The Hcy-binding domain in association with the pterin-binding domain catalyzes the methylation of cob(I)alamin by methyltetrahydrofolate and the methylation of homocysteine. The B12-binding domain binds the cofactor. The AdoMet activation domain binds S-adenosyl-L-methionine. Under aerobic conditions cob(I)alamin can be converted to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L-methionine and flavodoxin regenerates methylcobalamin (By similarity).
Catalyzes the reversible hydration of fumarate to (S)-malate.
Belongs to the HIBADH-related family. 3-sulfolactaldehyde reductase subfamily.
Reduces 3-sulfolactaldehyde (SLA) to 2,3-dihydroxypropane 1-sulfonate (DHPS).
Belongs to the methyltransferase superfamily. RlmG family.
Specifically methylates the guanine in position 1835 (m2G1835) of 23S rRNA.
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 universal ribosomal protein uL18 family.
Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S and 23S rRNAs.
This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.
May function as iron donor in the assembly of iron-sulfur clusters.
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.
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.
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.
Part of the OsmU ABC transporter complex, which is involved in the uptake of osmoprotectants such as choline-O-sulfate and glycine betaine.
In the C-terminal section; belongs to the imidazoleglycerol-phosphate dehydratase family.
In the N-terminal section; belongs to the histidinol-phosphatase family.
Belongs to the FtsQ/DivIB family. FtsQ subfamily.
Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. May control correct divisome assembly.
Belongs to the HpcH/HpaI aldolase family. Citrate lyase beta subunit subfamily.
Forms an efflux pump with AaeA. Could function as a metabolic relief valve, allowing to eliminate certain compounds when they accumulate to high levels in the cell.
Part of an enzyme complex containing four subunits: a flavoprotein, an iron-sulfur, cytochrome b-556, and a hydrophobic anchor protein.
Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth.
Belongs to the DNA gyrase inhibitor YacG family.
Inhibits all the catalytic activities of DNA gyrase by preventing its interaction with DNA. Acts by binding directly to the C-terminal domain of GyrB, which probably disrupts DNA binding by the gyrase.
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Positive regulator of the expression of the invasion-associated type III secretion system encoded within SPI-1 (pathogenicity island 1).
Belongs to the complex I subunit 6 family.
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Acts as a regulator of flagellar gene expression by modulating the protein level of the anti sigma factor FlgM upon sensing ring completion or hook elongation. Flk could inhibit FlgM secretion by acting as a braking system for the flagellar-associated type III secretion (T3S) system. Plays a role in hindering to flip the flagellar T3S specificity switch from the rod and hook-type substrates to filament-type substrates prior to hook-basal body (HBB) completion possibly by preventing interaction of FliK with FlhB.
Belongs to the purine/pyrimidine phosphoribosyltransferase family.
Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
O-acetyl-L-serine causes the CysE-CysK complex to dissociate in the absence of hydrogen sulfide.
Part of the cysteine synthase complex formed at a ratio of 2 copies of this protein and 1 copy of serine acetyltransferase (cysE). The complex reversibly dissociates in the presence of O-acetyl-L-serine but in the absence of hydrogen sulfide (PubMed:4977445). Homodimer (PubMed:10452898, PubMed:11023792, PubMed:9761678).
Two cysteine synthase enzymes are found, this enzyme and CysM; both catalyze the same reaction. Cysteine synthase B (CysM) can also use thiosulfate in place of sulfide to give cysteine thiosulfonate as a product.
Belongs to the concentrative nucleoside transporter (CNT) (TC 2.A.41) family.
Belongs to the monovalent cation:proton antiporter 2 (CPA2) transporter (TC 2.A.37) family. KefB subfamily.
Interacts with the regulatory subunit KefG.
A scaffold on which IscS assembles Fe-S clusters. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters.
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.
Binds GDP with a dissociation constant of 1.7 uM and GTP with a dissociation constant of 6.5 uM.
Monomer (By similarity). Binds RluD (AC P65836) as well as the 30S ribosomal subunit protein S9 (PubMed:17905831).
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.
Belongs to the GHMP kinase family. IspE subfamily.
Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Binds to the sigma-S subunit of RNA polymerase, activating expression of sigma-S-regulated genes, such as the csgBAC operon encoding the subunits of curli proteins, and BcsA, involved in cellulose biosynthesis.
Induced at late exponential and stationary phases, and at low temperatures.
Belongs to the anhydro-N-acetylmuramic acid kinase family.
Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling.
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.
Belongs to the glutaredoxin family. Monothiol subfamily.
Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters.
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.
ATP-dependent carboxylate-amine ligase which exhibits weak glutamate--cysteine ligase activity.
Belongs to the glutamate--cysteine ligase type 2 family. YbdK subfamily.
Belongs to the RNA cytidine acetyltransferase family. TmcA subfamily.
Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and ATP (or GTP).
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.
Binds 1 iron-sulfur cluster per subunit.
Required for insertion of 4Fe-4S clusters for at least IspG.
Belongs to the bacterial solute-binding protein PotD/PotF family.
Required for the activity of the bacterial periplasmic transport system of putrescine and spermidine. Polyamine binding protein.
Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group.
Belongs to the EPSP synthase family. MurA subfamily.
Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
Required for maximal bacterial cellulose synthesis.
Belongs to the Orn/Lys/Arg decarboxylase class-II family. LysA subfamily.
Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine.
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).
Cell division protein that is required for growth during stress conditions. May be involved in protecting or stabilizing the divisomal assembly under conditions of stress.
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 1 subfamily.
Belongs to the CRISPR-associated endonuclease Cas1 family.
CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Acts as a dsDNA endonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.
Homodimer, forms a heterotetramer with a Cas2 homodimer.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA methyltransferase RlmE family.
Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
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.
Belongs to the acetyltransferase YopJ family.
Belongs to the mannitol dehydrogenase family.
Belongs to the Dus family. DusB subfamily.
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.
Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme.
Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs 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. Required for acetate recapture but not for acetate excretion when this organism is grown on ethanolamine (PubMed:16272400).
Enables the cell to use acetate during aerobic growth to generate energy via the TCA cycle, and biosynthetic compounds via the glyoxylate shunt. Acetylates CheY, the response regulator involved in flagellar movement and chemotaxis.
In the C-terminal section; belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.
This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Belongs to the antirestriction protein family.
Belongs to the isocitrate lyase/PEP mutase superfamily. Methylisocitrate lyase family.
Cells lacking this gene are unable to accumulate 2-methylcitrate and 2-methyl-cis-aconitate.
In vitro, dithiothreitol (DTT) or reduced glutathione (GSH) are required for optimal activity.
Involved in the catabolism of short chain fatty acids (SCFA) via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the thermodynamically favored C-C bond cleavage of (2R,3S)-2-methylisocitrate to yield pyruvate and succinate via an alpha-carboxy-carbanion intermediate.
Belongs to the ABC transporter superfamily. Cobalt importer (TC 3.A.1.18.1) family.
Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import. The complex confers cobalt uptake upon expression in E.coli; can also transport nickel with a very low affinity. Presumably responsible for energy coupling to the transport system.
Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery.
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 this gene have an obligate requirement for diaminopimelic acid (DAP) and undergo lysis in environments deprived of DAP.
Vaccine strains for Salmonella typhimurium were successfully produced using strains with mutations in the asd gene.
Belongs to the universal ribosomal protein uS2 family.
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.
Belongs to the peptidase M20A family. DapE subfamily.
Binds 2 divalent cations per subunit, one with high affinity and the other with lower affinity. Zn(2+) and/or Co(2+) ions are used for desuccinylase activity. The form of DapE active as a peptidase contains Zn(2+) in the high-affinity site and Mn(2+) in the low-affinity site.
Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls. Can also hydrolyze all N-terminal Asp dipeptides except Asp-Pro. Asp-Ser is the best substrate, followed by Asp-Gly, Asp-Leu, and Asp-Cys.
Mn(2+)-activated peptidase is inhibited by Mn(2+) at concentration above 1 mM and by increasing concnentrations of Co(2+). There is a competitive inhibitor effect between the substrates. Hydrolysis of Asp-Leu by Mn(2+)-activated DapE is inhibited by SDAP, and hydrolysis of SDAP by Co(2+)-activated DapE is inhibited by Asp-Ser.
Zn(+2) is usually found in the tight binding site, but the nature of the second cation in the low affinity binding site is different according the activity.
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.
Catalyzes both the uptake and excretion of putrescine. The uptake of putrescine is dependent on the membrane potential and the excretion involves putrescine-ornithine antiporter activity.
Belongs to the ribosome association toxin RatA family.
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Belongs to the phD/YefM antitoxin family.
Putative antitoxin component of a toxin-antitoxin (TA) system; its cognate toxin is unknown.
YoeB, the specific toxin against which this antitoxin acts in E.coli, is not encoded in this genome.
4-aminobutanal can spontaneously cyclize to 1-pyrroline, and 5-aminopentanal to 1-piperideine.
Belongs to the aldehyde dehydrogenase family. Gamma-aminobutyraldehyde dehydrogenase subfamily.
Catalyzes the oxidation 4-aminobutanal (gamma-aminobutyraldehyde) to 4-aminobutanoate (gamma-aminobutyrate or GABA). This is the second step in one of two pathways for putrescine degradation, where putrescine is converted into 4-aminobutanoate via 4-aminobutanal. Also functions as a 5-aminopentanal dehydrogenase in a a L-lysine degradation pathway to succinate that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate.
Belongs to the acetyltransferase family. ArgA subfamily.
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 exoribonuclease that removes nucleotide residues following the -CCA terminus of tRNA and adds nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates.
Member of the two-component regulatory system PgtB/PgtA that regulates the inducible phosphoglycerate transport system. Activates PgtA by phosphorylation.
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.
Dicyclohexylcarbodiimide (DCDD) binding to the active aspartate residue inhibits ATPase in vitro.
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.
Catalyzes the synthesis of activated sulfate.
Acts as a repressor of mal genes. In absence of maltose, the C-terminus of MalK interacts with MalT, then MalT becomes inactive and the mal genes are not activated. In presence of maltose, MalK is tightly associated with the MalFG complex and has no affinity for MalT.
Belongs to the ABC transporter superfamily. Maltooligosaccharide importer (TC 3.A.1.1.1) family.
Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Responsible for energy coupling to the transport system.
Target for inducer exclusion, mediated by the unphosphorylated enzyme III of the phosphotransferase system for glucose and resulting in the inhibition of maltose transport.
The complex is composed of two ATP-binding proteins (MalK), two transmembrane proteins (MalG and MalK) and a solute-binding protein (MalE).
Involved in the efflux of threonine and homoserine.
Belongs to the RNA methyltransferase TrmD family.
Specifically methylates guanosine-37 in various tRNAs.
Consists of two structural and functional domains: an N-terminal DNA-binding domain, approximately the first 60 residues, and a larger C-terminal domain, approximately 280 residues, which imparts the function of corepressor binding and oligomerization.
Is the main repressor of the genes involved in the de novo synthesis of purine nucleotides, regulating purB, purC, purEK, purF, purHD, purL, purMN and guaBA expression. PurR is allosterically activated to bind its cognate DNA by binding the purine corepressors, hypoxanthine or guanine, thereby effecting transcription repression.
This protein specifically binds sulfate and is involved in its transmembrane transport.
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
B6-vitamer kinase involved in the salvage pathway of pyridoxal 5'-phosphate (PLP). Catalyzes the phosphorylation of pyridoxine (PN), pyridoxal (PL), and pyridoxamine (PM), forming their respective 5'-phosphorylated esters, i.e. PNP, PLP and PMP.
Belongs to the pyridoxine kinase family. PdxK subfamily.
Is repressed by the transcriptional regulator PtsJ.
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.
Cells lacking this gene are defective in aerobic degradation of propanediol.
Large subunit of the propanediol dehydratase-reactivating factor (DDR), which reactivates suicidally inhibited adenosylcobalamin-dependent propanediol dehydratase (diol dehydratase, DDH) found in the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation. Reactivates inactivated DDH in the presence of ATP, Mg(2+) and free adenosylcobalamin (AdoCbl), by mediating the exchange of the tightly bound damaged cofactor AdoCbl for a free intact one. This subunit contains the adenosine nucleotide binding site.
Originally suggested to encode a cobalamin adenosyl transferase.
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.
Homotetramer. Residues from neighboring subunits contribute catalytic and substrate-binding residues to each active site.
Catalyzes the transfer of an acyl group from acyl-ACP to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme can also utilize acyl-CoA as fatty acyl donor, but not acyl-PO(4).
Interacts (phosphorylated CheY) with CheZ (via C-terminus).
Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. In its active (phosphorylated or acetylated) form, CheY exhibits enhanced binding to a switch component, FliM, at the flagellar motor which induces a change from counterclockwise to clockwise flagellar rotation. Shows autophosphatase activity which is enhanced by CheZ.
Phosphorylated by CheA or acetylated by acetyl-CoA synthetase, depending on which acetate metabolism pathway is available (By similarity). Dephosphorylated (inactivated) by CheZ.
Belongs to the glycosyl hydrolase 1 family.
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.
Belongs to the DNA mismatch repair MutS family.
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.
In the C-terminal section; belongs to the anthranilate phosphoribosyltransferase family.
Monomer. Heterotetramer consisting of two non-identical subunits: a beta subunit (TrpG) and a large alpha subunit (TrpE) (Probable).
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. In addition to synthesizing anthranilate, it also catalyzes the second step of the pathway, the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate.
Essential for recycling GMP and indirectly, cGMP.
A minor shell protein of the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation. The isolated BMC shell component protein ratio for J:A:B':B:K:T:U is approximately 15:10:7:6:1:1:2 (PubMed:12923081). Not required for structural integrity of BMCs nor to mitigate propionaldehyde toxicity, it might be involved in spatial organization of BMCs (PubMed:21239588).
Interacts with shell proteins PduA and PduP and assembly protein PduM.
Releases increased amounts of acetaldehyde when grown on propanediol (PubMed:16585748). Half the cells seem to form BMC aggregates with visible shells, the other half have no BMCs. Grows normally on 1,2-PD and vitamin B12 (PubMed:21239588). A double pduJ-pduK strain grows in an interrupted manner on 1,2-PD and vitamin B12; grows for a while then stops, then restarts as toxic propionaldehyde accumulates and then decreases (PubMed:18296526).
The C-terminal 70 residues (positions 90-160) when overexpressed in E.coli bind Fe (PubMed:20870711). Might bind an [Fe-S] cluster in vivo (Probable).
The phosphoglycerate transporter protein is a part of the PGT transport system. It is the membrane bound transporter for phosphoglycerate into salmonella.
Belongs to the C/M/P thioester hydrolase family.
Functions as an ATPase. May play a role in metal insertion (metal-chelatase) or as a chaperone.
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.
Belongs to the phosphoglycerate mutase family.
Catalyzes the conversion of adenosylcobalamin 5'-phosphate to adenosylcobalamin (vitamin B12); involved in the assembly of the nucleotide loop of cobalamin. Also catalyzes the hydrolysis of the phospho group from alpha-ribazole 5'-phosphate to form alpha-ribazole.
Belongs to the DcuC/DcuD transporter (TC 2.A.61) family.
Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is required to maintain a long-term chronic systemic infection in mice. It inhibits normal cell migration of primary macrophages and dendritic cells, by a mechanism that involves interaction with the host factor IQGAP1, an important regulator of the cytoskeleton and cell migration. Also accelerates the systemic spread of infection from the gastrointestinal tract to the bloodstream, probably by interacting with host TRIP6.
Interacts with host IQGAP1 and host TRIP6 (thyroid receptor-interacting protein 6).
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.
Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily.
Belongs to the isocitrate lyase/PEP mutase superfamily. Isocitrate lyase family.
Involved in the metabolic adaptation in response to environmental changes. Catalyzes the reversible formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle during growth on fatty acid substrates.
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.
By propanediol aerobically and anaerobically, under control of PocR, Arc and Crp. Has 2 promoters.
No visible phenotype, not required for BMC formation (PubMed:8071226, PubMed:9352910). Reduced levels of PocR protein; pocR is transcribed in part from the pduF promoters (PubMed:7559322).
Probably facilitates diffusion of 1,2-propanediol (1,2-PD) into the cell (Probable). Modeling suggests active transport of 1,2-PD is required at low extracellular concentrations to allow maximal growth and saturation of PduP/PduQ within the bacterial microcompartment (BMC); this protein may be the cellular transporter (Probable).
Belongs to the LDH/MDH superfamily. MDH type 1 family.
Catalyzes the reversible oxidation of malate to oxaloacetate.
Belongs to the PpiC/parvulin rotamase family.
PPIases accelerate the folding of proteins. It prefers amino acid residues with hydrophobic side chains like leucine and phenylalanine in the P1 position of the peptides substrates (By similarity).
Belongs to the pseudouridine synthase TruD family.
Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate.
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).
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.
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.
Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Belongs to the P-Pant transferase superfamily. EntD family.
EntB, EntD, EntE, and EntF form a multienzyme complex called enterobactin synthase.
Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron(2+) atoms. Plays an essential role in the assembly of the enterobactin by catalyzing the transfer of the 4'-phosphopantetheine (Ppant) moiety from coenzyme A to the apo-domains of both EntB (ArCP domain) and EntF (PCP domain) to yield their holo-forms which make them competent for the activation of 2,3-dihydroxybenzoate (DHB) and L-serine, respectively.
Conversion of NADPH, generated by peripheral catabolic pathways, to NADH, which can enter the respiratory chain for energy generation.
Inactivated by D- and L-beta-fluoroalanine, D- and L-beta-chloroalanine, and O-acetyl-D-serine.
Isomerizes L-alanine to D-alanine which is then oxidized to pyruvate by DadA.
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 Dus family. DusA subfamily.
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. Specifically modifies U20 and U20a in tRNAs.
In the C-terminal section; belongs to the PRA-PH family.
In the N-terminal section; belongs to the PRA-CH 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. TdcB also dehydrates serine to yield pyruvate via analogous enamine/imine intermediates.
Each protein molecule can bind up to four molecules of AMP, which act as an allosteric activator to the enzyme. The enzyme is inhibited by alpha-keto acids and other catabolites.
In the native structure, TdcB is in a dimeric form, whereas in the TdcB-AMP complex, it exists in a tetrameric form (dimer of dimers).
Belongs to the ABC transporter superfamily. Vitamin B12 importer (TC 3.A.1.13.1) family.
Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Responsible for energy coupling to the transport system.
In classical PTS systems, the PTS EIIC type-2 domain forms the translocation channel and contains the specific substrate-binding site. UlaA does not exhibit the topological features of any recognized enzyme IIC.
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 arginine deiminase family.
Mutant is growth-deficient under aerobic conditions and is impaired to replicate at physiological and high temperatures (PubMed:21554724, PubMed:28559279). Mutant is defective for proliferation in macrophages and mice infection and has a severe attenuation in virulence in the murine model when inoculated both orally and intraperitoneally (PubMed:21554724, PubMed:28559279). Deletion inhibits colonization and invasion of four human cell lines, impairs flagella formation, activates the expression of type-1 fimbriae-like structures on the cell surface, enhances biofilm formation and reduces bacterial motility. The deletion mutant is menaquinone-deficient (PubMed:27777572).
Required for efficient ubiquinone (coenzyme Q) biosynthesis under aerobic conditions. UbiK is probably an accessory factor of Ubi enzymes and facilitates ubiquinone biosynthesis by acting as an assembly factor, a targeting factor, or both. Dispensable for ubiquinone biosynthesis under anaerobiosis (PubMed:28559279). Required for proliferation in macrophages and virulence in mice (PubMed:28559279, PubMed:21554724). Significantly contributes to colonization and invasion as well as host inflammation and innate immunity after infection (PubMed:27777572). In vitro, has membrane fusogenic activity at acidic pH (PubMed:21554724).
During aerobic growth, mutant is impaired for ubiquinone biosynthesis and for growth in rich medium, but it does not present any defect under anaerobic conditions. Mutant is also impaired for Salmonella intracellular proliferation in macrophages.
Required for ubiquinone (coenzyme Q) biosynthesis under aerobic conditions (PubMed:24142253). Binds hydrophobic ubiquinone biosynthetic intermediates via its SCP2 domain and is essential for the stability of the Ubi complex (By similarity). May constitute a docking platform where Ubi enzymes assemble and access their SCP2-bound polyprenyl substrates (By similarity). Required for intracellular proliferation in macrophages (PubMed:24142253).
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. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity.
Belongs to the bacterial ribosomal protein bL9 family.
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 LcrH/SycD chaperone family.
Type III secretion-associated chaperone required for SipB and SipC stabilization. Prevents premature association of SipB with SipC, which may lead to their targeting for degradation. Along with InvF, required for transcription activation of sigDE (sopB pipC), sicAsipBCDA, and sopE.
Functions as a type III secretion system (TTSS) chaperone, which is required for SseB and SseD accumulation and secretion. May have a direct role in secretion of SseB and SseD, or may facilitate their correct folding, for efficient secretion and function. Required for survival and replication within epithelial cells and macrophages.
Mutant is severely attenuated in virulence.
The N-terminal region is dispensable for binding and stabilizing SseB, but is essential for export of SseB to the surface of the bacterium.
Belongs to the ammonia transporter channel (TC 1.A.11.2) family.
Necessary for transcription of the csgAB operon. May have the capability to respond to starvation and/or high cell density by activating csgBA transcription (By similarity).
Probably catalyzes the hydrolysis of L-ascorbate-6-P into 3-keto-L-gulonate-6-P. Is essential for L-ascorbate utilization under anaerobic conditions.
Serine hydrolase involved in the detoxification of formaldehyde.
2 residues (Tyr-92 and Arg-95) present in a large hydrophobic pocket are probably involved in substrate specificity. They are important for desuccinylation activity, but dispensable for deacetylation activity.
5- to 20-fold higher levels of this protein are seen in rich and minimal media.
Belongs to the sirtuin family. Class III subfamily.
Both isoforms are monomers (PubMed:20889757).
Most expressed in mid- to late-log growth phases (at protein level) (PubMed:20889757). Has 3 promoters, P1 (upstream of nagK) gives rise to a nagK-cobB transcript, P2 (within the nagK coding region) gives rise to a transcript able to generate both CobB isoforms, while P3 (nucleotide 44 of the long isoform) can only give rise to the CobB-Short isoform (PubMed:20889757).
NAD-dependent lysine deacetylase that specifically removes acetyl groups on target proteins. Also acts as a protein-lysine deacylase by mediating protein desuccinylation and de-2-hydroxyisobutyrylation. Modulates the activities of several proteins which are inactive in their acylated form (By similarity). Activates the enzyme acetyl-CoA synthetase (acs) by deacetylating 'Lys-609' in the inactive, acetylated form of the enzyme (PubMed:12493915, PubMed:20889757, PubMed:12700259). May also modulate the activity of other propionyl-adenosine monophosphate (AMP)-forming enzymes such as propionate--CoA ligase (prpE) (PubMed:12493915, PubMed:12700259). Overexpression compensates for a cobT deletion, suggesting it may have N(1)-alpha-phosphoribosyltransferase activity; alternatively this protein may stimulate synthesis of an enzyme with the CobT activity (PubMed:9822644).
Originally isolated genetically as functioning in cobalamin biosynthesis and in propionate catabolism (PubMed:8206834, PubMed:8955330).
Single mutant grows on cobinamide (CBI), CBI plus 5,6-dimethylbenzimidazole (DMB) and cobalamin (CBL); double cobB-cobT deletion mutants do not grow on CBI plus DMB (PubMed:8206834). Single mutant does not grow on propionate (PubMed:8955330). Acetyl-CoA synthetase (acs) accumulates in an inactive, acetylated form (PubMed:12493915). Considerably decreased growth on 1,2-propanediol, cells do not excrete more propanediol than wild-type (PubMed:12700259).
In the N-terminal section; belongs to the NADH:flavin oxidoreductase/NADH oxidase family.
Belongs to the major facilitator superfamily. Proton-dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family. DtpA subfamily.
Proton-dependent permease that transports di- and tripeptides.
Transcriptionally activated by the EnvZ/OmpR regulatory system. Strongly stimulated under anaerobic conditions through an OmpR-independent mechanism.
Belongs to the shikimate kinase family. AroL subfamily.
The LID domain closes over the active site upon ATP binding.
Belongs to the GTP cyclohydrolase I type 2/NIF3 family.
Provides significant protection from radiation damage and may be involved in the degradation of radiation-damaged nucleotides.
Toroid-shaped homohexamer. In the hexamer, 3 dimers assemble to form a ring-like structure surrounding a central hole.
A probable alpha helix (residues 6-18) probably binds to cargo enzymes, attaching them to the shell.
Homotrimerizes to form a pseudohexamer with a central pore. The trimers pack into an array.
In purified BMCs seen as a 28.0 kDa and 25.0 kDa form, both of which have been N-terminally sequenced and whose N-fMet is removed; the smaller form is called PduB'.
Releases increased amounts of acetaldehyde when grown on propanediol (PubMed:16585748). Cells do not make BMCs, diol dehydratase is found in diffuse aggregates near the cell pole; it was later found this a double pduA-pduBB' deletion (PubMed:11844753). A deletion that prevents synthesis of both proteins makes no BMCs, about 20% of cells form amorphous polar bodies. Grows in an interrupted manner on 1,2-PD and vitamin B12; grows for a while then stops, then restarts as if a toxic compound was accumulating and then decreases (PubMed:21239588).
The two proteins produced are among the major shell proteins of the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation (PubMed:12923081, PubMed:21239588). Required for structural integrity of BMCs and to mitigate propionaldehyde toxicity (PubMed:21239588). The N-terminal 13 residues are important for correct assembly of the BMC shell (PubMed:28138097). The isolated BMC shell component protein ratio for J:A:B':B:K:T:U is approximately 15:10:7:6:1:1:2 (PubMed:12923081). The N-terminus of the long form (PduB) is required for correct formation of BMCs, deletions in the first 37 residues have substantially reduced levels of the major lumen enzymes. May play a major role in binding the enzyme contents to the shell (PubMed:28138097).
Upon overexpression of PduB or PduB' and mixing of the resulting purified sheets with 2-ethyl-1-hexanol, will form closed shells. Enzymes (tested with endogenous BMC enzyme DDH and the peroxidase activity of cytC) can be encapsulated in the shells; the enzyme is active in the shells. The shells are permeable to a variety of compounds, showing they could be used to make protein based synthetic bioreactors.
Belongs to the SEDS family. MrdB/RodA subfamily.
Peptidoglycan polymerase that is essential for cell wall elongation.
Belongs to the GTP cyclohydrolase I family. QueF type 2 subfamily.
Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
Belongs to the IUNH family. RihA subfamily.
Hydrolyzes cytidine or uridine to ribose and cytosine or uracil, respectively.
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.
Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors.
Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group. However, the true cosubstrate could be (R)-1-amino-2-propanol O-2-phosphate, leading to cobinamide phosphate.
Belongs to the universal ribosomal protein uS19 family.
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
Belongs to the quinolinate synthase family. Type 1 subfamily.
Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
Repressed by NadR and partially controlled by cAMP.
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).
Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
May protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition, may functin in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity (Probable). Overexpression of eutJ and eutS in E.coli leads to multiple BMC-like structures; eutS expression alone leads to 1 BMC-like structure per cell (PubMed:27063436).
Not required for aerobic growth on ethanolamine (EA) supplemented with cobalamin (vitamin B12). A double eutJ-eutG deletion is not required for growth in the above conditions. A double eutG-eutH deletion is not required for growth in the above conditions. Slightly attenuated in a mouse model of infection (PubMed:10464203). A non-polar deletion mutant grows on EA from pH 5.5 to pH 8.0, but does not grow at pH 8.5, no change in acetaldehyde release on EA plus vitamin B12 (PubMed:16585748).
Belongs to the DeoC/FbaB aldolase family.
Involved in the degradation of phospho-AI-2, thereby terminating induction of the lsr operon and closing the AI-2 signaling cycle. Catalyzes the transfer of an acetyl moiety from 3-hydroxy-5-phosphonooxypentane-2,4-dione to CoA to form glycerone phosphate and acetyl-CoA.
Interacts, and probably forms a ternary complex, with MukF and MukB. The complex formation is stimulated by calcium or magnesium.
Involved in chromosome condensation, segregation and cell cycle progression. May participate in facilitating chromosome segregation by condensation DNA from both sides of a centrally located replisome during cell division. Probably acts via its interaction with MukB and MukF.
Regulatory DnaK co-chaperone. Direct interaction between DnaK and DjlA is needed for the induction of the wcaABCDE operon, involved in the synthesis of a colanic acid polysaccharide capsule, possibly through activation of the RcsB/RcsC phosphotransfer signaling pathway. The colanic acid capsule may help the bacterium survive conditions outside the host.
The transmembrane domain is a dimerization domain.
Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. PdxB subfamily.
Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate.
Belongs to the DEAD box helicase family. RhlE subfamily.
DEAD-box RNA helicase involved in ribosome assembly. Has RNA-dependent ATPase activity and unwinds double-stranded RNA.
Belongs to the band 7/mec-2 family. HflK subfamily.
HflC and HflK could encode or regulate a protease.
HflC and HflK may interact to form a multimeric complex.
Part of the ABC transporter complex GltIJKL involved in glutamate and aspartate uptake. Binds to both glutamate and aspartate.
The complex is composed of two ATP-binding proteins (GltL), two transmembrane proteins (GltJ and GltK) and a solute-binding protein (GltI).
Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemW subfamily.
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 band 7/mec-2 family. Flotillin subfamily.
Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein includes tyrosine phosphatase and GTPase activating protein (GAP) activities. After bacterial internalization, GAP mediates the reversal of the cytoskeletal changes induced by SopE. This function is independent of its tyrosine phosphatase activity, which remains unclear.
Forms a complex with SicP. Binds host RAC1.
In the N-terminal section; belongs to the YopE family.
Requires SicP as a chaperone for its stability and for secretion. The structure of the SptP-SicP complex contains four molecules of the chaperone SicP, aligned in a linear fashion and arranged in two sets of tightly bound homodimers that bind two SptP molecules. The SicP homodimers do not interact with each other, but are held together by a molecular interface formed between two SptP molecules. The chaperone-binding domain of SptP does not adopt a globular fold for interaction with SicP. Each SptP molecule is wrapped around by three SicP chaperones (two chaperones from one homodimer and a third one from the opposite homodimer pair). SptP interacts with SicP chaperone dimers mainly through four regions of its chaperone-binding domain.
The tyrosine phosphatase activity is inhibited by sodium vanadate.
Adenine glycosylase active on G-A mispairs. MutY also corrects error-prone DNA synthesis past GO lesions which are due to the oxidatively damaged form of guanine: 7,8-dihydro-8-oxoguanine (8-oxo-dGTP).
Binds 1 [4Fe-4S] cluster. The cluster does not appear to play a role in catalysis, but is probably involved in the proper positioning of the enzyme along the DNA strand.
Belongs to the type-I 3-dehydroquinase family.
Inhibited by (2R)-2-methyl-3-dehydroquinic acid.
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. The reaction involves the formation of an imine intermediate between the keto group of 3-dehydroquinate and the epsilon-amino group of a Lys-170 at the active site.
Belongs to the ATP-dependent AMP-binding enzyme family. MenE subfamily.
Converts 2-succinylbenzoate (OSB) to 2-succinylbenzoyl-CoA (OSB-CoA).
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 (By similarity).
Some 20 DnaA protein molecules bind their sites in oriC.
Required for the activity of the bacterial periplasmic transport system of putrescine.
Belongs to the phosphoglycerate kinase family.
Belongs to the ACC deaminase/D-cysteine desulfhydrase family.
Catalyzes the alpha,beta-elimination reaction of D-cysteine and of several D-cysteine derivatives. It could be a defense mechanism against D-cysteine.
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.
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.
Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
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 universal ribosomal protein uL29 family.
Catalyzes nitrate uptake, nitrite uptake and nitrite export across the cytoplasmic membrane.
In the presence of manganese, represses expression of mntH and mntS. Up-regulates expression of mntP (By similarity).
It contains an N-terminal DNA-binding domain and a metal-binding domain.
Transcriptional repressor that controls expression of the genes required for the catabolism of sialic acids.
Belongs to the major facilitator superfamily. Proton-dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family. DtpB subfamily.
Has several major domains; the N-terminal cytoplasmic domain is followed by 2 transmembrane helices that anchor the protein in the membrane; the periplasmic domain between the helices interacts with MrzA. The cytoplasmic C-terminal domain has a HAMP domain joined by a flexible linker to a histidine kinase domain. The HAMP domain by itself is intrinsically disordered. The cytoplasmic dimerization domain (CDD) forms an osmosensitive core and includes the autophosphorylated histidine residue.
Member of the two-component regulatory system EnvZ/OmpR involved in osmoregulation (particularly of genes ompF and ompC) as well as other genes (By similarity). EnvZ functions as a membrane-associated protein kinase that phosphorylates OmpR in response to environmental signals; at low osmolarity OmpR activates ompF transcription, while at high osmolarity it represses ompF and activates ompC transcription (By similarity).
Belongs to the NAD(P)-dependent epimerase/dehydratase family. HldD subfamily.
Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose.
Contains a large N-terminal NADP-binding domain, and a smaller C-terminal substrate-binding domain.
Carbamylation allows a single lysine to coordinate two zinc ions.
Catalyzes the hydrolytic cleavage of a subset of L-isoaspartyl (L-beta-aspartyl) dipeptides. Used to degrade proteins damaged by L-isoaspartyl residues formation.
Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. May act as a translocator that mediates translocation of SPI-2 TTSS effector proteins from intraphagosomal bacterial cells into the host cells.
May form a complex with SseB and SseD. SseB is required for correct localization of SseC on the bacterial cell surface.
Belongs to the phospholipase D family. Cardiolipin synthase subfamily. ClsC sub-subfamily.
Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) from phosphatidylglycerol (PG) and phosphatidylethanolamine (PE).
Belongs to the mannose-6-phosphate isomerase type 1 family.
Involved in the conversion of glucose to GDP-L-fucose, which can be converted to L-fucose, a capsular polysaccharide.
Belongs to the KHG/KDPG aldolase family.
Belongs to the MenA family. Type 1 subfamily.
Conversion of 1,4-dihydroxy-2-naphthoate (DHNA) to demethylmenaquinone (DMK).
Allosterically inhibited by NADPH and NADH. NADPH is the primary inhibitor during aerobic growth and NADH during anaerobic growth.
Equilibrium mixture of dimer and tetramer. It is converted entirely to tetramer in the presence of the inhibitor NADPH.
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 as a source of phosphorus. NADH cannot replace NAD as a substrate.
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 glycosyl hydrolase 5 (cellulase A) family.
Part of the UhpABC signaling cascade that controls the expression of the hexose phosphate transporter UhpT. Activates the transcription of the uhpT gene. Acts by binding specifically to the uhpT promoter region.
Phosphorylated and dephosphorylated by UhpB.
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.
There are 3 DAHP synthases, AroF is feedback-inhibited by Tyr. The other 2 DAHP synthases are Phe- and Trp-sensitive, respectively.
Binds 2 iron ions per subunit. The catalytic dinuclear iron-binding site within each subunit is known as the ferroxidase center.
Homooligomer of 24 subunits, arranged as 12 dimers, that are packed together to form an approximately spherical molecule with a central cavity, in which large amounts of iron can be deposited.
Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.
Required for spatial organization of the terminus region of the chromosome (Ter macrodomain) during the cell cycle. Prevents early segregation of duplicated Ter macrodomains during cell division. Binds specifically to matS, which is a 13 bp signature motif repeated within the Ter macrodomain.
Belongs to the glycosyltransferase 26 family.
Catalyzes the synthesis of Und-PP-GlcNAc-ManNAcA (Lipid II), the second lipid-linked intermediate involved in enterobacterial common antigen (ECA) synthesis.
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R1E contains the binding sites for both substrates and allosteric effectors and carries out the actual reduction of the ribonucleotide.
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. Lacks the N-terminal activity site.
Belongs to the class I-like SAM-binding methyltransferase superfamily. CmoM family.
Catalyzes the methylation of 5-carboxymethoxyuridine (cmo5U) to form 5-methoxycarbonylmethoxyuridine (mcmo5U) at position 34 in tRNAs.
Belongs to the DeoC/FbaB aldolase family. DeoC type 2 subfamily.
Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Part of the yceD-rpmF operon, which may continue into downstream genes.
Plays a role in synthesis, processing and/or stability of 23S rRNA.
Not known; mutations in apaG/corD give a phenotype of low-level Co(2+) resistance. They also decrease Mg(2+) efflux but not influx via the CorA Mg(2+) transport system.
Belongs to the methyltransferase superfamily. L-isoaspartyl/D-aspartyl protein methyltransferase family.
Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Belongs to the catalase family. HPII subfamily.
Serves to protect cells from the toxic effects of hydrogen peroxide.
Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
Cleavage and activation of PanD is accelerated by PanM.
Heterooctamer of four alpha and four beta subunits (By similarity). Interacts with PanM (PubMed:22497218, PubMed:22782525).
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.
Belongs to the DNA polymerase type-C family. DnaE subfamily.
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.
The DNA polymerase holoenzyme is a complex that contains 10 different types of subunits. These subunits are organized into 3 functionally essential subassemblies: the pol III core, the beta sliding clamp processivity factor and the clamp-loading complex. The pol III core (subunits alpha,epsilon and theta) contains the polymerase and the 3'-5' exonuclease proofreading activities. The polymerase is tethered to the template via the sliding clamp processivity factor. The clamp-loading complex assembles the beta processivity factor onto the primer template and plays a central role in the organization and communication at the replication fork. This complex contains delta, delta', psi and chi, and copies of either or both of two different DnaX proteins, gamma and tau. The composition of the holoenzyme is, therefore: (alpha,epsilon,theta)[2]-(gamma/tau)[3]-delta,delta', psi,chi-beta[4].
Belongs to the L-ribulose-5-phosphate 3-epimerase family.
Catalyzes the isomerization of L-xylulose-5-phosphate to L-ribulose-5-phosphate. Is involved in the anaerobic L-ascorbate utilization.
A protein kinase that (auto)phosphorylates on Ser and Thr residues, probably involved in the extracytoplasmic stress response (PubMed:12511488). Probably acts to suppress the effects of stress linked to accumulation of reactive oxygen species (By similarity).
Belongs to the SrkA/RdoA protein kinase family.
Decreases long-term survival (1000-fold decrease after 20 days in liquid culture), derepresses curli production under non-curli-inducing growth conditions.
Expression is growth phase dependent and sensitive to the media conditions reaching high levels in stationary phase (at protein level) (PubMed:17302814). It is probably regulated by the CpxRA two-component regulatory system (PubMed:12511488).
Not known. This protein is involved in the virulence of salmonellas.
Belongs to the amino acid/polyamine transporter 2 family. Mtr/TnaB/TyrP permease subfamily.
Involved in transporting aromatic amino acids across the cytoplasmic membrane.
Individual Salmonella serotypes usually alternate between the production of 2 antigenic forms of flagella, termed phase 1 and phase 2, each specified by separate structural genes, fliC and fljB.
Inhibited in nutrient-poor medium (at protein level).
Catalyzes the isomerization of 5-dehydro-4-deoxy-D-glucuronate to 3-deoxy-D-glycero-2,5-hexodiulosonate.
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. Forms a bridge to the 50S subunit in the 70S ribosome, contacting the 23S rRNA.
Belongs to the nicotinamide ribonucleoside (NR) uptake permease (TC 4.B.1) family.
Required for nicotinamide riboside transport across the inner membrane.
Autophosphorylated. Seems to be phosphorylated through a cooperative two-step mechanism. First, Tyr-568 is phosphorylated in an intramolecular reaction that generates a significant increase of protein kinase activity. Then Tyr-707, Tyr-709, Tyr-710, Tyr-712 and Tyr-714 are phosphorylated in an intermolecular Tyr-568-dependent reaction (By similarity).
Required for the extracellular polysaccharide colanic acid synthesis. The autophosphorylated form is inactive. Probably involved in the export of colanic acid from the cell to medium (By similarity).
Activates ribosomal RNA transcription. Plays a direct role in upstream activation of rRNA promoters.
Belongs to the transcriptional regulatory Fis family.
In the C-terminal section; belongs to the precorrin methyltransferase family.
In the N-terminal section; belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family.
Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme.
Belongs to the mandelate racemase/muconate lactonizing enzyme family. MenC type 1 subfamily.
Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 2-succinylbenzoate (OSB).
Involved in control of the biosynthesis of leucine.
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.
Required for the efficient initiation of filament assembly.
Belongs to the phosphothreonine lyase family.
Secreted effector that irreversibly inactivates host MAP kinases by catalyzing the dephosphorylation of the phosphothreonine residue in the pT-X-pY motif in MAPK2/ERK2, MAPK3/ERK1, and p38, via a beta-elimination reaction leading to a dehydrobutyrine residue. Is also able to remove the phosphate group from phospho-JNK in vitro, but JNK may not be a substrate in vivo. Could help suppress localized pro-inflammatory responses at infection foci in the spleen and liver, and thereby facilitate bacterial growth.
Strains lacking this gene are attenuated for systemic virulence in mice.
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Catalyzes the deamination of adenosine to inosine at the wobble position 34 of tRNA(Arg2).
Belongs to the bacterial ribosomal protein bL21 family.
Part of the 50S ribosomal subunit. Contacts protein L20.
This protein binds to 23S rRNA in the presence of protein L20.
Purine salvage pathway enzyme which catalyzes the transfer of the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to the N9 position of hypoxanthine to yield IMP (inosine 5'-monophosphate). To a lesser extent, can also act on guanine leading to GMP, but shows a highly less efficient activity with xanthine.
In the C-terminal section; belongs to the complex I 49 kDa subunit family.
In the N-terminal section; belongs to the complex I 30 kDa subunit family.
Associates with aggregated proteins, together with IbpB, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent.
Monomer. Forms homomultimers of about 100-150 subunits at optimal growth temperatures. Conformation changes to monomers at high temperatures or high ionic concentrations.
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).
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.
Belongs to the methyltransferase superfamily. PrmA family.
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.
Adds a galactose goup to a glucose group of LPS.
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.
Part of the 50S ribosomal subunit. Forms a cluster with proteins L14 and L19.
In the C-terminal section; belongs to the MGMT family.
The methylated ADA protein acts as a positive regulator of its own synthesis, as well as that of other proteins. The transcription-activating function of the ADA protein resides in its N-terminus. It activates the transcription of alkA, alkB and aidB.
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, and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings. Replenishes negative supercoiling downstream of highly transcribed genes to help control overall chromosomal supercoiling density (PubMed:22916023). E.coli makes 15% more negative supercoils in pBR322 plasmid DNA than S.typhimurium; the S.typhimurium GyrB subunit is toxic in E.coli, while the E.coli copy can be expressed in S.typhimurium even though the 2 subunits have 777/804 residues identical (PubMed:17400739).
Belongs to the type II topoisomerase GyrA/ParC subunit family.
Involved in the degradation and recycling of damaged RNA. It is itself a target for degradation by the ATP-dependent protease Lon.
Converts alpha-N-acetylneuranimic acid (Neu5Ac) to the beta-anomer, accelerating the equilibrium between the alpha- and beta-anomers. Probably facilitates sialidase-negative bacteria to compete sucessfully for limited amounts of extracellular Neu5Ac, which is likely taken up in the beta-anomer. In addition, the rapid removal of sialic acid from solution might be advantageous to the bacterium to damp down host responses.
Acts as the second step in ethanolamine degradation by converting acetaldehyde into acetyl-CoA (Probable) (PubMed:21803884). Has a very strong preference for NAD(+) over NADP(+) in both catalytic directions (PubMed:21803884). May play a role in bacterial microcompartment (BMC) assembly or maintenance (Probable). Directly targeted to the BMC (PubMed:27450681).
Artificial BMCs can be made in E.coli by expressing eutK, eutL, eutM, eutN, eutS (eutSMNLK) or eutS alone. Cargo proteins can be targeted to them using the first 21 residues of this protein. This can lead to the development of tailored BMCs for specific metabolic reactions.
Can use ethanolamine (EA) as a nitrogen source but not as a carbon source. Slightly attenuated in a mouse model of infection (PubMed:7868611, PubMed:2656649). No aerobic growth on EA supplemented with cobalamin (vitamin B12) (PubMed:10464203, PubMed:16272400). A non-polar deletion mutant does not grow on EA between pH 5.5 and pH 8.5, releases increased amounts of acetaldehyde on EA plus vitamin B12 (PubMed:16585748). A deletion allows growth on acetate, suggesting BMC assembly or maintenance is impaired (PubMed:23585538).
Has been used to coproduce acetaldehyde and hydrogen in E.coli.
Interacts with EutS, which targets it to the interior of the BMC.
The first 21 residues target foreign proteins (tested with eGFP) to the BMC in E.coli. The cargo is only detected by Western blot in broken shells, strongly suggesting this protein is normally found inside the BMC and not on its exterior.
Member of the two-component regulatory system PhoR/PhoB involved in the phosphate regulon genes expression. PhoR may function as a membrane-associated protein kinase that phosphorylates PhoB in response to environmental signals.
Belongs to the dGTPase family. Type 1 subfamily.
dGTPase preferentially hydrolyzes dGTP over the other canonical NTPs.
Causes a mild defect in aerobic growth on CuSO(4), strongly impairs survival during anaerobic growth on CuSO(4).
Expression of the CopA(Z) soluble copper chaperone isoform requires a -1 programmed ribosomal frameshift (PRF) at the 70th codon. A nucleotide 'slippery sequence' that promotes PRF is found just downstream of the frameshifted site.
Involved in Cu(+) export (By similarity). Essential for copper tolerance under both aerobic and anaerobic conditions (PubMed:17768242).
Probably also encodes a cytoplasmic copper chaperone CopA(Z) that is produced by programmed ribosomal frameshifting (Probable).
Transcriptionally up-regulated by CueR in response to copper ions.
Controls the rotational direction of flagella during chemotaxis.
Belongs to the sigma-70 factor family. RpoH subfamily.
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 expression of heat shock genes.
Belongs to the TACO1 family. YeeN subfamily.
Induced in response to increased extracellular osmolarity, this is the first gene of the proU operon (proV-proW-proX). Osmoregulation requires curved DNA downstream of the transcription start site in this gene, which is repressed when bound by H-NS. H-NS may act indirectly to influence the local topology of the promoter (PubMed:1423593).
Part of the ProU ABC transporter complex involved in glycine betaine and proline betaine uptake. Probably responsible for energy coupling to the transport system.
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.
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).
Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA methyltransferase RlmE family. RlmM subfamily.
Catalyzes the 2'-O-methylation at nucleotide C2498 in 23S rRNA.
Component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (PubMed:24722491). Acts as a regulator of the SsaN/SctN2 ATPase activity (By similarity).
The core secretion machinery of the T3SS is composed of approximately 20 different proteins, including cytoplasmic components, a base, an export apparatus and a needle (PubMed:30107569). This subunit is part of the cytosolic complex (PubMed:24722491). Interacts directly with SsaN/SctN2 (T3SS-2 ATPase) (PubMed:24722491).
Belongs to the peptidase U32 family. UbiV subfamily.
Required for O(2)-independent ubiquinone (coenzyme Q) biosynthesis. Together with UbiU, is essential for the C6-hydroxylation reaction in the oxygen-independent ubiquinone biosynthesis pathway.
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. 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. Interacts with FliE and peptidoglycan hydrolase FlgJ (via N-terminus), which seems to function as a scaffold or cap for rod assembly.
Probable regulatory protein. Its target is not known.
Responsible for synthesis of pseudouridine from uracil at positions 955, 2504 and 2580 in 23S ribosomal RNA.
Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3-hydroxyacyl-CoA dehydrogenase activities.
In the central section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
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).
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
Belongs to the bacterial ribosomal protein bL31 family. Type B subfamily.
Belongs to the universal ribosomal protein uS10 family.
Involved in the binding of tRNA to the ribosomes.
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).
Activates the small RNA gene sgrS under glucose-phosphate stress conditions as well as yfdZ. Represses its own transcription under both stress and non-stress conditions. Might act as a sensor of the intracellular accumulation of phosphoglucose by binding these molecules in its C-terminal solute-binding domain.
Belongs to the HIBADH-related family. 2-hydroxy-3-oxopropionate reductase subfamily.
Catalyzes the reduction of tatronate semialdehyde to D-glycerate.
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 pyruvate:ferredoxin/flavodoxin oxidoreductase family.
Could be part of an electron transfer system required for anaerobic carnitine reduction.
Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes.
Belongs to the bacterial diacylglycerol kinase family.
Catalyzes the ATP-dependent phosphorylation of sn-l,2-diacylglycerol (DAG) to phosphatidic acid. Involved in the recycling of diacylglycerol produced as a by-product during membrane-derived oligosaccharide (MDO) biosynthesis.
Belongs to the mandelate racemase/muconate lactonizing enzyme family. RhamD subfamily.
Catalyzes the dehydration of L-rhamnonate to 2-keto-3-deoxy-L-rhamnonate (KDR). Can also dehydrate L-lyxonate and L-mannonate, although less efficiently, but not 2-keto-4-hydroxyheptane-1,7-dioate.
Reaction proceeds via a syn dehydration.
Represses the transcription of fabB, involved in unsaturated fatty acid (UFA) biosynthesis. By controlling UFA production, FabR directly influences the physical properties of the membrane bilayer.
Catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis (By similarity).
Component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (PubMed:9786184, PubMed:27974800, PubMed:30242280). Forms a ring-shaped multimeric structure with an apparent central pore in the outer membrane (PubMed:9786184, PubMed:21385715, PubMed:27974800, PubMed:30242280).
Insertion mutants are hypoinvasive in the HEp-2 cell assay.
The core secretion machinery of the T3SS is composed of approximately 20 different proteins, including cytoplasmic components, a base, an export apparatus and a needle (PubMed:30107569). This subunit is part of the base, which anchors the injectisome in the bacterial cell envelope (PubMed:21385715, PubMed:23633951, PubMed:27974800, PubMed:30242280). Forms a stable homooligomeric complex (PubMed:9786184, PubMed:21385715, PubMed:23633951, PubMed:27974800, PubMed:30242280). The complex is composed of 15 subunits (PubMed:21385715, PubMed:23633951, PubMed:27974800).
Possible endonuclease which induces a single-strand cut and initiates DNA replication.
Part of the ABC transporter complex CysAWTP (TC 3.A.1.6.1) involved in sulfate/thiosulfate import. Probably responsible for the translocation of the substrate across the membrane (By similarity).
Adds poly(A) tail to the 3' end of many RNAs, which usually targets these RNAs for decay. Plays a significant role in the global control of gene expression, through influencing the rate of transcript degradation, and in the general RNA quality control.
Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family.
Belongs to the arginase family. Agmatinase subfamily.
Catalyzes the formation of putrescine from agmatine.
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. Also cleaves 5'-deoxyadenosine, a toxic by-product of radical S-adenosylmethionine (SAM) enzymes, into 5-deoxyribose and adenine. Thus, is required for in vivo function of the radical SAM enzymes biotin synthase and lipoic acid synthase, that are inhibited by 5'-deoxyadenosine accumulation.
Belongs to the phage antitermination Q type 1 family.
Negative regulator of allantoin and glyoxylate utilization operons. Binds to the gcl promoter and to the allS-allA intergenic region (By similarity).
Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. EngB GTPase family.
Necessary for normal cell division and for the maintenance of normal septation.
Electron transport system for the ribonucleotide reductase system NrdEF.
Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids.
Exporter of O-acetylserine (OAS) and cysteine.
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 and to avoid they are captured by anthranilate phosphoribosyltransferase (TrpD) to generate PRA, an intermediate in the alternative pyrimidine biosynthetic (APB) pathway. Also required for full activity of IlvE which is involved in the isoleucine biosynthesis. RidA also accelerates the release of pyruvate produced by IlvA from L-serine.
Cells lacking this gene appear to be compromised in their ability to synthesize isoleucine. Mutation results in the partial block of at least one step in isoleucine biosynthesis subsequent to the reaction catalyzed by threonine deaminase (IlvA). Mutation is required for the dependence of the PurF-independent alternative pyrimidine biosynthesis (APB) pathway of thiamine upon the oxidative pentose phosphate pathway.
Belongs to the trehalose phosphatase family.
Removes the phosphate from trehalose 6-phosphate to produce free trehalose.
Required for the activity of the bacterial periplasmic transport system of putrescine and spermidine.
Can use ethanolamine (EA) as a nitrogen source when AdoCbl but not cyano-B12 or hydroxy-B12 is provided; cannot use EA as a carbon source (PubMed:2656649, PubMed:15516577). Required for aerobic growth on ethanolamine supplemented with cobalamin (vitamin B12) (PubMed:10464203). A non-polar deletion mutant does not grow on EA between pH 5.5 and pH 8.5 (PubMed:16585748).
Reactivates suicidally inhibited ethanolamine ammonia-lyase (EAL), cyanocobalamin-inactivated EAL and O(2)-inactivated EAL; requires Mg(2+), ATP and adenosylcobalamin. Reactivation probably occurs by the ATP-dependent exchange of cobalamin (By similarity). Protects EAL from inhibition by CN-B12, does not have adenosylation activity (PubMed:15516577) (Probable).
Belongs to the cytidylate kinase family. Type 1 subfamily.
Belongs to the type II topoisomerase family. ParE type 1 subfamily.
This protein is a positive regulator of gene expression for the cysteine regulon, a system of 10 or more loci involved in the biosynthesis of L-cysteine from inorganic sulfate. The inducer for CysB is N-acetylserine. CysB inhibits its own transcription.
Belongs to the SecD/SecF family. SecF subfamily.
Forms a complex with SecD. Part of the essential Sec protein translocation apparatus which comprises SecA, SecYEG and auxiliary proteins SecDF-YajC and YidC.
Modulates the activity of the EnvZ/OmpR two-component regulatory system, probably by directly modulating EnvZ enzymatic activity and increasing stability of phosphorylated OmpR.
Belongs to the Cob(I)alamin adenosyltransferase family.
Mild growth defect on 1,2-propanediol-cyanocobalamin medium; no growth is seen in a double cobA-pduO deletion.
Required for both de novo synthesis of the corrin ring for the assimilation of exogenous corrinoids. Participates in the adenosylation of a variety of incomplete and complete corrinoids.
May form a complex with SseB and SseC. SseB is required for correct localization of SseD on the bacterial cell surface. Binds to the chaperone SseA.
Activation of pyruvate formate-lyase 1 under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine.
Activation of pyruvate formate-lyase under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine.
To bacterial alkanal monooxygenase alpha and beta chains.
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.
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) (By similarity).
Belongs to the HpcH/HpaI aldolase family. KDGluc aldolase subfamily.
Catalyzes the reversible retro-aldol cleavage of both 5-keto-4-deoxy-D-glucarate and 2-keto-3-deoxy-D-glucarate to pyruvate and tartronic semialdehyde.
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.
Catalyzes the 6-electron oxidation of protoporphyrinogen IX to form protoporphyrin IX; under anaerobic conditions uses menaquinone as an electron acceptor, under aerobic condition uses ubiquinone as an electron acceptor.
Involved in the synthesis of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (PubMed:9680224, PubMed:9786184). Pilot protein that is required for the proper localization of the secretin InvG/SctC in the outer membrane (PubMed:9680224, PubMed:9786184). Required for the secretion of the Sip virulence factors (PubMed:9680224, PubMed:23159244).
Mutant shows decreased levels of InvG/SctC (PubMed:9786184). Deletion of the gene reduces the invasion efficiency of the bacterium to 70-80% as compared to wild-type in vitro (PubMed:23159244). SctG/invH-ssaV double mutant shows reduced secretion of Sip effector proteins (SipA, SipB, SipC and SipD) (PubMed:23159244).
Belongs to the MsrB Met sulfoxide reductase family.
Binds 1 zinc ion per subunit. The zinc ion is important for the structural integrity of the protein.
Belongs to the Pcp/SlyB lipoprotein family.
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.
Belongs to the transferase hexapeptide repeat family. LpxD subfamily.
Catalyzes the N-acylation of UDP-3-O-(hydroxytetradecanoyl)glucosamine using 3-hydroxytetradecanoyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
The SS-C mutant is antibiotic supersensitive; its outer membrane permeability barrier against hydrophobic antibiotics is severely deficient.
Was originally thought to be involved in transcription.
Catalyzes the efficient dehydration of both L-talarate (also called L-altrarate) and galactarate to 5-keto-4-deoxy-D-glucarate (5-KDG) (PubMed:17649980, PubMed:29248502). Also catalyzes the epimerization of L-talarate to galactarate; epimerization occurs in competition with dehydration. Is required for the utilization of L-talarate as a carbon source. Also functions in galactarate utilization. Is not active on other acid sugars (PubMed:17649980).
Cells lacking this gene lose the ability to grow on L-talarate as carbon source, and are impaired in the ability to utilize galactarate as carbon source.
The enzyme product is the enantiomer of the product obtained in the galactarate dehydratase reaction catalyzed by OB2843; the enzymes thus differ in their regiochemistry of dehydration.
Belongs to the Dus family. DusC subfamily.
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. Specifically modifies U16 in tRNAs.
Has been reported to be located in the outer membrane.
Molecular chaperone that interacts specifically with outer membrane proteins, thus maintaining the solubility of early folding intermediates during passage through the periplasm.
Associates exclusively with 100S ribosomes, which are dimers of 70S ribosomes.
Belongs to the HPF/YfiA ribosome-associated protein family. Short HPF subfamily.
During stationary phase, promotes and stabilizes dimerization of 70S ribosomes by the ribosome modulation factor (RMF), leading to the formation of inactive 100S ribosomes.
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.
Belongs to the DNA gyrase inhibitor family.
Inhibits the supercoiling activity of DNA gyrase. Acts by inhibiting DNA gyrase at an early step, prior to (or at the step of) binding of DNA by the gyrase. It protects cells against toxins that target DNA gyrase, by inhibiting activity of these toxins and reducing the formation of lethal double-strand breaks in the cell.
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.
Belongs to the UDP-N-acetylglucosamine 2-epimerase family.
Catalyzes the reversible epimerization at C-2 of UDP-N-acetylglucosamine (UDP-GlcNAc) and thereby provides bacteria with UDP-N-acetylmannosamine (UDP-ManNAc), the activated donor of ManNAc residues.
Catalyzes the ATP-dependent phosphorylation of D-threonate to D-threonate 4-phosphate (PubMed:27402745). Can also phosphorylate 4-hydroxy-L-threonine, with lower efficiency. This side reaction may serve to deal with the toxicity of 4-hydroxy-L-threonine by converting it into 4-hydroxy-L-threonine 4-phosphate, a useful product that can be used by PdxA2 (PubMed:27402745, PubMed:27294475).
Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
TctD expression is regulated by catabolite repression.
Transcriptional activator of the tctI tricarboxylate transport system operon.
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 exact function of the psi subunit is unknown.
Catalyzes the methylation of C-11 in cobalt-precorrin-4 to form cobalt-precorrin-5A.
Probably involved in ribonucleotide reductase function.
Globally modulates RNA abundance by binding to RNase E (Rne) and regulating its endonucleolytic activity. Can modulate Rne action in a substrate-dependent manner by altering the composition of the degradosome. Modulates RNA-binding and helicase activities of the degradosome.
Homotrimer. Binds to both RNA-binding sites in the C-terminal region of Rne and to RhlB.
Belongs to the LysE/ArgO transporter (TC 2.A.75) family.
Involved in the export of arginine. Important to control the intracellular level of arginine and the correct balance between arginine and lysine.
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.
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 (By similarity).
Protein L10 is also a translational repressor protein. It controls the translation of the rplJL-rpoBC operon by binding to its mRNA.
Ribosomal protein L8 appears to be an aggregate of ribosomal proteins L7/L12 and L10.
Belongs to the FAD-dependent oxidoreductase family.
One of at least two accessory proteins for anaerobic nitric oxide (NO) reductase. Reduces the rubredoxin moiety of NO reductase.
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.
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.
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 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).
Transcriptional activator of csgD, which is required for production of the curli (AgF).
Catalyzes the transfer of CoA to carnitine, generating the initial carnitinyl-CoA needed for the CaiB reaction cycle. Also has activity toward crotonobetaine and gamma-butyrobetaine.
Part of the histidine permease ABC transporter. Binds histidine. Interacts with HisQMP and stimulates ATPase activity of HisP, which results in histidine translocation. May have some additional function(s) in translocation that is independent of the stimulation of ATP hydrolysis.
The complex is composed of two ATP-binding proteins (HisP), two transmembrane proteins (HisM and HisQ) and a solute-binding protein (HisJ).
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.
Is critically involved in promoting the replication of S.typhimurium cells inside host macrophages, suggesting a role in the establishment of bacterial colonization within macrophages. May be involved in the biosynthesis and modification of the peptidoglycan layer of the cell wall.
Up-regulated following infection of host macrophages.
ATPase component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (PubMed:24722491). Acts as a molecular motor to provide the energy that is required for the export of proteins (By similarity). Required for type III secretion apparatus (T3SA) formation, secretion of a subset of SPI-2 effectors and virulence (PubMed:24722491, PubMed:25035427). May play a critical role in T3SS substrate recognition, disassembly of the effector/chaperone complex and unfolding of the effector in an ATP-dependent manner prior to secretion (Probable). Releases the effector protein SseB from the T3SS-2 specific chaperone SsaE in an ATP-dependent manner (PubMed:24722491).
Deletion mutant cannot secrete the effector proteins SseB, SseC, SseD, SseF, SseG and SseJ (PubMed:24722491, PubMed:25035427). Mutant is also defective for the secretion of the translocon proteins SseC/SctE and SseD/SctB (PubMed:25035427). Mutant shows decreased virulence in the mouse model of systemic infection (PubMed:24722491).
The core secretion machinery of the T3SS is composed of approximately 20 different proteins, including cytoplasmic components, a base, an export apparatus and a needle (PubMed:30107569). This subunit is part of the cytosolic complex (PubMed:24722491). Forms homohexamers (PubMed:25035427). Forms a complex with SsaK/SctL (stator protein) and SsaQ/SctQ (the major sorting platform component) (PubMed:24722491). Interacts with the T3SS-2 specific chaperones SsaE, SseA, SscA, SscB, and SrcA (PubMed:24722491, PubMed:25035427).
Belongs to the EcnA/EcnB lipoprotein family.
Belongs to the methyltransferase superfamily. UbiG/COQ3 family.
O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
Interacts directly with the RNA polymerase.
Transcription factor that acts by binding directly to the RNA polymerase (RNAP). Required for negative regulation of rRNA expression and positive regulation of several amino acid biosynthesis promoters. Also required for regulation of fis expression.
Negatively regulates the transcription of the flagellar master operon flhDC by binding to the upstream region of the operon.
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. 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. 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).
Belongs to the ureidoglycolate lyase family.
Catalyzes the catabolism of the allantoin degradation intermediate (S)-ureidoglycolate, generating urea and glyoxylate. Involved in the utilization of allantoin as nitrogen source.
Involved in the export and assembly of LpfA fimbrial subunits across the outer membrane.
Belongs to the thioredoxin family. DsbD subfamily.
Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps.
Uptake of L-lactate across the membrane (By similarity). Can also transport D-lactate and glycolate (By similarity). Seems to be driven by a proton motive force (By similarity).
Belongs to the diaminopropionate ammonia-lyase family.
Catalyzes the alpha,beta-elimination reaction of both L- and D-alpha,beta-diaminopropionate (DAP) to form pyruvate and ammonia. In vitro L- and D-isomers of serine are also degraded, though slowly; it is the only serine dehydratase which can eliminate an amino group at the beta-carbon position. In vivo L-, D- and a mixure of DL-DAP allow growth. DL-DAP is toxic in the absence of this enzyme, it may inhibit enzymes involved in the synthesis of pyruvate and aspartate, as well as amino acids derived from them.
Competitively inhibited by L- and D-alanine.
No growth on minimal medium plus DL-DAP; growth can be restored by a mix of 8 amino acids (Arg, Asn, Cys, Glu, Ile, Leu, Met and Thr).
Belongs to the 'GDSL' lipolytic enzyme family.
Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is required for endosomal tubulation and negatively regulates the formation of Salmonella-induced filaments (Sifs) in epithelial cells. Has both deacylase and esterification activities in vitro, but esterification is probably the dominant activity in host cells. Significantly contributes to cholesterol esterification, which reduces cellular cholesterol in cells and abrogates the ability of SifA to associate with cholesterol and LAMP-1 vesicles.
Interacts with RhoA and indirectly with SifA.
Mutants have reduced cholesterol esterification activity as well as reduced lipid droplets.
Responsible for synthesis of pseudouridine from uracil at positions 1911, 1915 and 1917 in 23S ribosomal RNA.
Activity of this regulatory enzyme is affected by several metabolites. Allosterically and non-competitively inhibited by fructose 1,6-bisphosphate (FBP) and unphosphorylated phosphocarrier protein EIIA-Glc (III-Glc), an integral component of the bacterial phosphotransferase (PTS) system.
Homotetramer and homodimer (in equilibrium). Heterodimer with EIIA-Glc. Binds 1 zinc ion per glycerol kinase EIIA-Glc dimer. The zinc ion is important for dimerization.
Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
This bifunctional enzyme catalyzes two consecutive reactions during ribonucleic acid degradation. Converts a 2',3'-cyclic nucleotide to a 3'-nucleotide and then the 3'-nucleotide to the corresponding nucleoside and phosphate.
Two kinetically distinguishable active sites for the two substrates (2',3'-cyclic nucleotides and 3'-nucleotides) have been identified.
Belongs to the NhaB Na(+)/H(+) (TC 2.A.34) antiporter family.
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 (By similarity).
Part of the 30S ribosomal subunit. Forms a tight complex with proteins S10 and S14. Some nascent polypeptide chains are able to cross-link to this protein in situ (By similarity).
Catalyzes the 2'-O methylation of guanosine at position 18 in tRNA.
Belongs to the bacterial ribosomal protein bS21 family.
Belongs to the HpcH/HpaI aldolase family. KDR aldolase subfamily.
Catalyzes the reversible retro-aldol cleavage of 2-keto-3-deoxy-L-rhamnonate (KDR) to pyruvate and lactaldehyde.
Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
By nickel and cobalt. Transcriptionally repressed by RcnR (By similarity).
Part of a sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions. Accepts sulfur from TusA and transfers it in turn to TusE.
The beta chain is an electron transfer unit containing 4 cysteine clusters involved in the formation of iron-sulfur centers.
Not essential for flagellar formation and function.
Dual-function protein that regulates the transcription of class 2 flagellar operons and that also acts as an export chaperone for the filament-capping protein FliD. As a transcriptional regulator, acts as an anti-FlhDC factor; it directly binds FlhC, thus inhibiting the binding of the FlhC/FlhD complex to class 2 promoters, resulting in decreased expression of class 2 flagellar operons. As a chaperone, effects FliD transition to the membrane by preventing its premature polymerization, and by directing it to the export apparatus.
Homodimer. Interacts with FliD and FlhC.
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.
Acts as transcriptional repressor of the pdxK gene, encoding a pyridoxal kinase involved in the vitamin B6 salvage pathway. Also represses transcription of its own gene. Binds to the ptsJ-pdxK intergenic region, but does not bind pdxY and pdxH promoters. Among all six B6 vitamers, only pyridoxal 5'-phosphate (PLP) clearly binds to the protein and acts as an effector molecule for PtsJ, inducing a protein conformational change that increases affinity for DNA. Thus, PLP stabilizes protein-DNA interactions, reinforcing repression.
Cells lacking this gene display a 80-fold increase in pdxK expression with respect to wild-type when grown in minimal medium. A much lower but significant 2/3-fold increase of expression is also observed for pdxY and pdxH.
Binds 2 iron ions per dimer. The dimer may bind additional iron ions.
Homodimer; may form tetramers and higher multimers.
Is able to transfer iron-sulfur clusters to apo-ferredoxin. Multiple cycles of [2Fe2S] cluster formation and transfer are observed, suggesting that IscA acts catalytically. Recruits intracellular free iron so as to provide iron for the assembly of transient iron-sulfur cluster in IscU in the presence of IscS, L-cysteine and the thioredoxin reductase system TrxA/TrxB.
Belongs to the drug/metabolite transporter (DMT) superfamily. Small multidrug resistance (SMR) (TC 2.A.7.1) family. Gdx/SugE subfamily.
Guanidinium ion exporter. Couples guanidinium export to the proton motive force, exchanging one guanidinium ion for two protons.
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).
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
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.
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. 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.
Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
Responsible for synthesis of pseudouridine from uracil-2457 in 23S ribosomal RNA.
Belongs to the metallo-dependent hydrolases superfamily. NagA family.
Belongs to the KAE1 / TsaD family. TsaB subfamily.
Has been identified as the first Gram-negative bacterial RPF (Resuscitation-Promoting Factor) capable of reviving VNC (viable but non-culturable) cells when added externally, but the million-fold lower activity as compared to Gram-positive bacterial RPFs may indicate a lack of physiological relevance.
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 (By similarity). Neither binds polyphosphates nor a wide range of nucleotides on its own. Does not show O-sialoglycoprotein endopeptidase activity.
Belongs to the GTP-binding SRP family. FtsY subfamily.
Contains an acidic N-terminal A domain, a central N domain and a C-terminal GTPase G domain that can bind and hydrolyze GTP. Contains at least two lipid-binding sites. The first site contains the first 14 amino acids (helix 1) and the second binding site is an amphipathic alpha-helix located at the interface between the A- and the N-domain (helix 2).
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). Interaction with SRP-RNC 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.
Belongs to the universal ribosomal protein uS9 family.
Belongs to the radical SAM superfamily. KamA family.
Cells lacking this gene are highly attenuated for virulence in mouse models of infection. Salmonella epmA and epmB mutants share extensive phenotypic pleiotropy, including an increased ability to respire under nutrient-limiting conditions, hypersusceptibility to a variety of diverse growth inhibitors, and altered expression of multiple proteins, including several encoded on the SPI-1 pathogenicity island.
With EpmA is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. EpmB appears to act before EpmA. Displays lysine 2,3-aminomutase activity, producing (R)-beta-lysine from (S)-alpha-lysine (L-lysine) (By similarity).
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. Interacts directly with several other division proteins.
Belongs to the ROK (NagC/XylR) family. NagK subfamily.
Catalyzes the phosphorylation of N-acetyl-D-glucosamine (GlcNAc) derived from cell-wall degradation, yielding GlcNAc-6-P.
Expressed in mid-log phase, part of the nagK-cobB operon (PubMed:20889757).
Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA.
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).
Is the dominant magnesium transport system under laboratory growth conditions.
Mediates both influx and efflux of magnesium ions (PubMed:3536881, PubMed:2548998, PubMed:2670893, PubMed:9786860, PubMed:10601252, PubMed:10748031). Can also mediate cobalt and nickel uptake, albeit only at extracellular concentrations that are toxic to the cell (PubMed:3536881, PubMed:2670893). Does not transport iron (PubMed:15516579). Alternates between open and closed states. Activated by low cytoplasmic Mg(2+) levels. Inactive when cytoplasmic Mg(2+) levels are high (By similarity).
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. Co(2+) binding also induces a conformation change. 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.
Belongs to the calycin superfamily. Lipocalin family.
Involved in the storage or transport of lipids necessary for membrane maintenance under stressful conditions. Displays a binding preference for lysophospholipids.
Belongs to the class-II fumarase/aspartase family. Aspartase subfamily.
Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. Required, with TolR, for the proton motive force-dependent activation of TolA and for TolA-Pal interaction.
Regulates the transcription of several operons and genes involved in the biogenesis of Fe-S clusters and Fe-S-containing proteins.
Belongs to the CN hydrolase family. Apolipoprotein N-acyltransferase subfamily.
Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
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.
Belongs to the Mg-chelatase subunits D/I family. ComM subfamily.
Involved in the stabilization of the sigma stress factor RpoS.
Belongs to the NhaA Na(+)/H(+) (TC 2.A.33) antiporter family.
Antitoxin component of a type II toxin-antitoxin (TA) system. Upon expression in E.coli neutralizes the effect of cognate toxin VapC.
One of the components on the FinOP fertility inhibition complex, which inhibits the expression of traJ gene, which in turn regulates the expression of some 20 transfer genes. The transfer genes are responsible for the process, called conjugal transfer, in which DNA is transmitted from one bacterial host to another. RNA-binding that interacts with the traJ mRNA and its antisense RNA, finP, stabilizing finP against endonucleolytic degradation and facilitating sense-antisense RNA recognition.
Was originally thought to be a UDP-sugar hydrolase.
Part of a membrane-bound tetrathionate reductase that catalyzes the reduction of tetrathionate to thiosulfate. TtrB is probably involved in transfer of electrons from TtrC to TtrA. During mice infection, the ability to use tetrathionate as an electron acceptor is a growth advantage for S.typhimurium over the competing microbiota in the lumen of the inflamed gut.
Belongs to the methylglyoxal synthase family.
Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate.
Belongs to the glutamine synthetase family.
Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia.
Oligomer of 12 subunits arranged in the form of two hexameric ring.
When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) of GlnE inhibits GlnA by covalent transfer of an adenylyl group from ATP to Tyr-398. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) of GlnE activates GlnA by removing the adenylyl group by phosphorolysis. The fully adenylated enzyme complex is inactive.
Belongs to the HPS/KGPDC family. HPS subfamily.
Belongs to the methyltransferase superfamily. METTL16/RlmF family.
Specifically methylates the adenine in position 1618 of 23S rRNA.
Forms a 24-polypeptide structural core with octahedral symmetry.
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 resistance-nodulation-cell division (RND) (TC 2.A.6) family. MdtC subfamily.
Part of a tripartite efflux system composed of MdtA, MdtB and MdtC. MdtC forms a heteromultimer with MdtB.
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.
Belongs to the sodium:citrate (SCF) symporter family.
Uptake of citrate across the boundary membrane with the concomitant uptake of a sodium ion (symport system).
Essential cell division protein that activates septal peptidoglycan synthesis and constriction of the cell. Acts on both sides of the membrane, via interaction with FtsA in the cytoplasm and interaction with the FtsQBL complex in the periplasm. These interactions may induce a conformational switch in both FtsA and FtsQBL, leading to septal peptidoglycan synthesis by FtsI and associated synthases.
Interacts with FtsA via its N-terminal cytoplasmic domain.
Regulates secA expression by translational coupling of the secM secA operon. Translational pausing at a specific Pro residue 5 residues before the end of the protein may allow disruption of a mRNA repressor helix that normally suppresses secA translation initiation.
Component of the PhsABC thiosulfate reductase that catalyzes the reduction of thiosulfate to sulfite and hydrogen sulfide, with menaquinol as the sole electron donor. Proton motive force (PMF) is required to drive transmembrane electron transfer within the reductase. The PhsC subunit anchors the complex to the membrane and contains the site for menaquinol oxidation.
Part of the ABC transporter complex UgpBAEC involved in sn-glycerol-3-phosphate (G3P) import. Binds G3P.
Belongs to the Orn/Lys/Arg decarboxylase class-II family.
Catalyzes the decarboxylation of D-ornithine and D-lysine (PubMed:29024617, PubMed:30699288). Ornithine is likely the physiological substrate (PubMed:29024617). Has no detectable diaminopimelate decarboxylase activity in vitro (PubMed:29024617).
Part of the ABC transporter complex MglABC involved in galactose/methyl galactoside import (By similarity). In addition, binds D-galactose and D-glucose and plays a role in the chemotaxis towards these two sugars by interacting with the Trg chemoreceptor (Probable).
The ABC transporter complex is composed of one ATP-binding protein (MglA), two transmembrane proteins (MglC) and a solute-binding protein (MglB).
The calcium-binding site is structurally similar to that of EF-hand proteins, but is in two parts, with the last calcium ligand provided by Glu-228.
Belongs to the peroxiredoxin family. Tpx 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.
Has both ATPase and helicase activities. Unwinds DNA duplexes with 3' to 5' polarity with respect to the bound strand and initiates unwinding most effectively when a single-stranded region is present. Involved in the post-incision events of nucleotide excision repair and methyl-directed mismatch repair.
Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin.
Homohexamer. The oligomerization is ATP-dependent (By similarity).
Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Required for colonization of the gastrointestinal tract, probably due to protection from a combination of stress factors.
The Clp repeat (R) domain probably functions as a substrate-discriminating domain, recruiting aggregated proteins to the ClpB hexamer and/or stabilizing bound proteins. The NBD2 domain is responsible for oligomerization, whereas the NBD1 domain stabilizes the hexamer probably in an ATP-dependent manner. The movement of the coiled-coil domain is essential for ClpB ability to rescue proteins from an aggregated state, probably by pulling apart large aggregated proteins, which are bound between the coiled-coils motifs of adjacent ClpB subunits in the functional hexamer (By similarity).
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.
Belongs to the PAPS reductase family. CysD subfamily.
With CysN forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD.