Exonuclease that cleaves single-stranded 3' overhangs of double-stranded RNA.
Belongs to the Rieske iron-sulfur protein family.
Iron-sulfur subunit of the cytochrome bc1 complex, an essential component of the respiratory electron transport chain required for ATP synthesis. The bc1 complex catalyzes the oxidation of menaquinol and the reduction of cytochrome c in the respiratory chain. The bc1 complex operates through a Q-cycle mechanism that couples electron transfer to generation of the proton gradient that drives ATP synthesis.
Belongs to the bacterial ribosomal protein bL33 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.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.
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.
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.
Belongs to the short-chain dehydrogenases/reductases (SDR) family.
H(+)-stimulated, divalent metal cation uptake system.
Belongs to the adenylyl cyclase class-3 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 class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.
Binds 1 pyridoxal phosphate per subunit.
May also have succinyldiaminopimelate aminotransferase activity, thus carrying out the corresponding step in lysine biosynthesis.
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. EgtE subfamily.
Probably catalyzes the conversion of hercynylcysteine sulfoxide to ergothioneine.
Belongs to the LppX/LprAFG lipoprotein family.
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains.
Belongs to the inorganic phosphate transporter (PiT) (TC 2.A.20) family.
Belongs to the metallo-dependent hydrolases superfamily. DHOase family. Class I DHOase subfamily.
Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Belongs to the 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.
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.
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.
Lacks conserved residue(s) required for the propagation of feature annotation.
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.
Belongs to the cytochrome c oxidase subunit 3 family.
Belongs to the major facilitator superfamily. Nitrate/nitrite porter (TC 2.A.1.8) family.
Belongs to the mycobacterial PPE family.
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.
Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source.
In the C-terminal section; belongs to the NAD synthetase family.
Belongs to the trans-sulfuration enzymes family.
Belongs to the complex I 49 kDa subunit family.
NDH-1 is composed of 14 different subunits. Subunits NuoB, C, D, 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 a menaquinone. 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 complex I 20 kDa subunit family.
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.
Belongs to the glycosyltransferase 39 family.
Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.
Belongs to the inositol monophosphatase superfamily.
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.
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.
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.
Belongs to the long-chain O-acyltransferase family.
Belongs to the binding-protein-dependent transport system permease family.
Acts as a transcriptional regulator. Probably redox-responsive. The apo- but not holo-form probably binds DNA.
Binds 1 [4Fe-4S] cluster per subunit. Following nitrosylation of the [4Fe-4S] cluster binds 1 [4Fe-8(NO)] cluster per subunit.
The Fe-S cluster can be nitrosylated by nitric oxide (NO).
Upon Fe-S cluster removal intramolecular disulfide bonds are formed.
Belongs to the ferredoxin--NADP reductase type 1 family.
Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family. MmpL subfamily.
Belongs to the acyl-CoA dehydrogenase family.
Belongs to the bacterial phospholipase C family.
Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.
Belongs to the group II decarboxylase family.
Electron transport system for the ribonucleotide reductase system NrdEF.
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.
Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.
The 20S proteasome core is composed of 14 alpha and 14 beta subunits that assemble into four stacked heptameric rings, resulting in a barrel-shaped structure. The two inner rings, each composed of seven catalytic beta subunits, are sandwiched by two outer rings, each composed of seven alpha subunits. The catalytic chamber with the active sites is on the inside of the barrel. Has a gated structure, the ends of the cylinder being occluded by the N-termini of the alpha-subunits. Is capped by the proteasome-associated ATPase, ARC.
The formation of the proteasomal ATPase ARC-20S proteasome complex, likely via the docking of the C-termini of ARC into the intersubunit pockets in the alpha-rings, may trigger opening of the gate for substrate entry. Interconversion between the open-gate and close-gate conformations leads to a dynamic regulation of the 20S proteasome proteolysis activity.
Belongs to the transketolase family. DXPS subfamily.
Binds 1 thiamine pyrophosphate per subunit.
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).
Belongs to the glyceraldehyde-3-phosphate dehydrogenase 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.
Belongs to the aldehyde dehydrogenase family.
Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Belongs to the ABC-3 integral membrane protein family.
Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+).
Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.
Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
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).
The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
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.
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.
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 ammonia transporter channel (TC 1.A.11.2) family.
Belongs to the BlaI transcriptional regulatory family.
Belongs to the sigma-70 factor family. ECF subfamily.
Interacts transiently with the RNA polymerase catalytic core formed by RpoA, RpoB, RpoC and RpoZ (2 alpha, 1 beta, 1 beta' and 1 omega subunit) to form the RNA polymerase holoenzyme that can initiate transcription.
Belongs to the phosphofructokinase type A (PFKA) family. Mixed-substrate PFK group III 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 FAD-dependent glycerol-3-phosphate dehydrogenase family.
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.
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. Other proteins may also be involved.
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.
Belongs to the anti-sigma-factor antagonist family.
Belongs to the cytidine and deoxycytidylate deaminase family.
Catalyzes the deamination of adenosine to inosine at the wobble position 34 of tRNA(Arg2).
Belongs to the DNA glycosylase MPG family.
Binds 1 pyruvoyl group covalently per subunit.
Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
Heterooctamer of four alpha and four beta subunits.
Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus.
Belongs to the ABC-4 integral membrane protein family. FtsX subfamily.
Part of the ABC transporter FtsEX involved in cellular division.
Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrE subfamily.
Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Belongs to the 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 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.
Belongs to the ABC transporter superfamily. Ycf16 family.
Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.
Part of the ABC transporter complex PstSACB involved in phosphate import.
The complex is composed of two ATP-binding proteins (PstB), two transmembrane proteins (PstC and PstA) and a solute-binding protein (PstS).
Belongs to the 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.
Belongs to the ABC-2 integral membrane protein 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 CDP-alcohol phosphatidyltransferase class-I family.
Catalyzes the conjugation of the 1'-hydroxyl group of D-myo-inositol-3-phosphate (also named L-myo-inositol-1-phosphate) with a lipid tail of cytidine diphosphate diacylglycerol (CDP-DAG), forming phosphatidylinositol phosphate (PIP) and CMP. PIP is a precursor of phosphatidylinositol (PI) which is an essential lipid required for cell wall formation.
Contains a di-nuclear catalytic Mg(2+) center.
Belongs to the autoinducer-2 exporter (AI-2E) (TC 2.A.86) family.
Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family.
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.
Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
To bacterial alkanal monooxygenase alpha and beta chains.
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.
Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2B subfamily.
Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family.
Belongs to the helicase family. RAD25/XPB subfamily.
Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
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 FAD-binding monooxygenase family.
Belongs to the non-flavoprotein flavin reductase family.
Belongs to the extradiol ring-cleavage dioxygenase family.
Belongs to the thiolase-like superfamily. Thiolase family.
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.
Belongs to the zinc-containing alcohol dehydrogenase family.
Belongs to the binding-protein-dependent transport system permease family. CysTW subfamily.
Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
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.
Belongs to the acetyltransferase Eis 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).
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.
The glycine cleavage system is composed of four proteins: P, T, L and H.
Belongs to the diphosphomevalonate decarboxylase family.
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 enoyl-CoA hydratase/isomerase family.
Belongs to the short-chain fatty acyl-CoA assimilation regulator (ScfR) family.
Belongs to the myo-inositol 1-phosphate synthase family.
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
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 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.
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.
Participates in transcription elongation, termination and antitermination.
Belongs to the mycobacterial A85 antigen family.
Belongs to the helicase family. UvrD subfamily.
3'-to-5' exoribonuclease specific for small oligoribonucleotides.
Belongs to the oligoribonuclease family.
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 GTP-binding SRP family. FtsY subfamily.
Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC).
Part of the signal recognition particle protein translocation system, which is composed of SRP and FtsY.
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.
Belongs to the neutral ceramidase family.
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 low molecular weight phosphotyrosine protein phosphatase family.
Belongs to the elongation factor P family.
Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
Belongs to the LysR transcriptional regulatory family.
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.
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 acyltransferase PapA5 family.
The IMP cyclohydrolase activity resides in the N-terminal region.
Belongs to the monomeric-type IDH family.
Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
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 FtsQ/DivIB family. FtsQ subfamily.
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.
Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine.
In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.
A monovalent cation. Ammonium or potassium.
Belongs to the type III pantothenate kinase family.
Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
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.
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.
May be involved in recombinational repair of damaged DNA.
Belongs to the transglycosylase family. Rpf subfamily.
Belongs to the UDP-glucose/GDP-mannose dehydrogenase family.
Belongs to the arylamine N-acetyltransferase family.
Belongs to the glutamine synthetase family.
Oligomer of 12 subunits arranged in the form of two hexagons.
Belongs to the thymidylate synthase ThyX family.
Binds 4 FAD per tetramer. Each FAD binding site is formed by three monomers.
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 NADPH and FADH(2) as the reductant.
Belongs to the GHMP kinase family. GalK subfamily.
Belongs to the universal ribosomal protein uS9 family.
Belongs to the C/M/P thioester hydrolase family.
Belongs to the glutamate synthase family.
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.
Antioxidant protein with alkyl hydroperoxidase activity. Required for the reduction of the AhpC active site cysteine residues and for the regeneration of the AhpC enzyme activity.
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.
Belongs to the FPP/GGPP synthase family.
Belongs to the Cob(I)alamin adenosyltransferase family.
Belongs to the 5-formyltetrahydrofolate cyclo-ligase family.
Belongs to the amino acid-polyamine-organocation (APC) superfamily. Amino acid transporter (AAT) (TC 2.A.3.1) family.
Belongs to the universal stress protein A family.
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.
Probable amino-acid or metabolite transport protein.
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 F420-dependent glucose-6-phosphate dehydrogenase family.
Catalyzes the coenzyme F420-dependent oxidation of glucose 6-phosphate (G6P) to 6-phosphogluconolactone. Appears to have a role in resistance to oxidative stress, via its consumption of G6P that serves as a source of reducing power to combat oxidative stress in mycobacteria.
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 class-III pyridoxal-phosphate-dependent aminotransferase family.
Belongs to the EPSP synthase family. MurA subfamily.
Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
Belongs to the AAA ATPase family. RarA/MGS1/WRNIP1 subfamily.
Belongs to the universal ribosomal protein uL29 family.
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.
Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.
Belongs to the 2-oxoacid dehydrogenase family.
Belongs to the glycosyltransferase 87 family.
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 DEAD box helicase family.
A mycothiol (MSH, N-acetylcysteinyl-glucosaminyl-inositol) S-conjugate amidase, it recycles conjugated MSH to the N-acetyl cysteine conjugate (AcCys S-conjugate, a mercapturic acid) and the MSH precursor. Involved in MSH-dependent detoxification of a number of alkylating agents and antibiotics.
Belongs to the MshB deacetylase family. Mca subfamily.
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.
Heterotrimer of RecB, RecC and RecD. All subunits contribute to DNA-binding.
Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids lysine, threonine, isoleucine and methionine.
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 bacterial ribosomal protein bS6 family.
Binds together with S18 to 16S ribosomal RNA.
Belongs to the glutamate 5-kinase family.
Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
Catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates.
Heterodimer of an alpha and a beta chain.
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.
Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity.
Belongs to the CitM (TC 2.A.11) transporter family.
Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
Could possibly oxidize fatty acids using specific components.
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.
Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.
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).
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.
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 universal ribosomal protein uS3 family.
Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation.
Part of the 30S ribosomal subunit. Forms a tight complex with proteins S10 and S14.
Belongs to the complex I 30 kDa subunit family.
Contains large globular domains required for ATP hydrolysis at each terminus and a third globular domain forming a flexible hinge near the middle of the molecule. These domains are separated by coiled-coil structures.
Required for chromosome condensation and partitioning.
Belongs to the F420H(2)-dependent quinone reductase family.
Belongs to the IPP isomerase type 2 family.
Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP).
Belongs to the precorrin methyltransferase family.
Belongs to the pterin-4-alpha-carbinolamine dehydratase family.
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.
Homohexamer. Assembles into a hexameric ring structure.
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.
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.
Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
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.
Belongs to the bacterial ribosomal protein bL27 family.
Belongs to the HAD-like hydrolase superfamily. SerB family.
Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Belongs to the 3-oxoacid CoA-transferase subunit B family.
Belongs to the glycosyl hydrolase 65 family.
Belongs to the methyltransferase superfamily. EgtD family.
Catalyzes the SAM-dependent triple methylation of the alpha-amino group of histidine to form hercynine, a step in the biosynthesis pathway of ergothioneine.
Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate.
Belongs to the thiolase-like superfamily. HMG-CoA synthase family.
The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane.
Belongs to the type 2 tetrahydrodipicolinate N-succinyltransferase family.
Catalyzes the conversion of the cyclic tetrahydrodipicolinate (THDP) into the acyclic N-succinyl-L-2-amino-6-oxopimelate using succinyl-CoA.
Belongs to the cysteine synthase/cystathionine beta-synthase family.
Belongs to the aspartate/glutamate racemases family.
Provides the (R)-glutamate required for cell wall biosynthesis.
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 glutamate--cysteine ligase type 2 family. EgtA subfamily.
Catalyzes the synthesis of gamma-glutamylcysteine (gamma-GC). This compound is used as substrate for the biosynthesis of the low-molecular thiol compound ergothioneine.
Belongs to the PAPS reductase family. CysH subfamily.
Catalyzes the formation of sulfite from adenosine 5'-phosphosulfate (APS) using thioredoxin as an electron donor.
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.
Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.
May catalyze the transamination reaction in phenylalanine biosynthesis.
Belongs to the glycosyltransferase 4 family. MraY subfamily.
Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
Belongs to the ribonucleoside diphosphate reductase small chain family.
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Tetramer of two alpha and two beta subunits.
Binds between the large and small subunits.
Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds. Allows this organism to utilize ethanolamine as the sole source of nitrogen and carbon in the presence of external vitamin B12.
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.
Belongs to the phosphohexose mutase family.
Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
Belongs to the GMC oxidoreductase family.
Belongs to the drug/metabolite transporter (DMT) superfamily. Small multidrug resistance (SMR) (TC 2.A.7.1) family. Mmr subfamily.
Belongs to the complex I 51 kDa subunit family.
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain.
Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
Belongs to the bacterial ribosomal protein bS20 family.
In the C-terminal section; belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.
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.
Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
Catalyzes 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 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 both the histidine and tryptophan biosynthetic pathways.
Belongs to the Pup ligase/Pup deamidase family. Pup deamidase subfamily.
Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds. Allows this organism to utilize ethanolamine as the sole source of nitrogen and carbon in the presence of vitamin B12.
Belongs to the P-Pant transferase superfamily. AcpS family.
Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Belongs to the bacterial solute-binding protein ModA family.
Involved in the catabolism of quinolinic acid (QA).
Belongs to the ETF beta-subunit/FixA family.
Heterodimer of an alpha and a beta subunit.
The electron transfer flavoprotein serves as a specific electron acceptor for other dehydrogenases. It transfers the electrons to the main respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase).
Belongs to the metallophosphoesterase superfamily. YfcE family.
Removes 5-oxoproline from various penultimate amino acid residues except L-proline.
Belongs to the small heat shock protein (HSP20) family.
Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. NifS/IscS subfamily.
The glycine cleavage system catalyzes the degradation of glycine.
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 class-II aminoacyl-tRNA synthetase family.
Belongs to the 3-oxoacid CoA-transferase subunit A family.
Involved in the hydrocarbon hydroxylating system, which transfers electrons from NADH to rubredoxin reductase and then through rubredoxin to alkane 1 monooxygenase.
Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
Belongs to the bacterial ribosomal protein bL31 family.
Belongs to the KhpA RNA-binding protein family.
Belongs to the SIMIBI class G3E GTPase family. HypB/HupM subfamily.
Belongs to the cytochrome ubiquinol oxidase subunit 2 family.
Belongs to the short-chain dehydrogenases/reductases (SDR) family. FabI subfamily.
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.
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.
Belongs to the SIMIBI class G3E GTPase family. UreG subfamily.
Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG.
Homodimer. UreD, UreF and UreG form a complex that acts as a GTP-hydrolysis-dependent molecular chaperone, activating the urease apoprotein by helping to assemble the nickel containing metallocenter of UreC. The UreE protein probably delivers the nickel.
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. Cleaves guanosine, inosine, 2'-deoxyguanosine and 2'-deoxyinosine.
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.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily.
Belongs to the AB hydrolase superfamily. MetX family.
Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
Catalyzes the deacetylation of 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside (GlcNAc-Ins) in the mycothiol biosynthesis pathway.
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.
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.
Belongs to the radical SAM superfamily. Anaerobic sulfatase-maturating enzyme family.
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.
Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate.
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.
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.
Belongs to the Mg-chelatase subunits D/I family.
Belongs to the ketopantoate reductase family.
Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
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 LeuD family. LeuD type 1 subfamily.
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Belongs to the ATP-dependent AMP-binding enzyme family. MbtB subfamily.
Belongs to the homoserine dehydrogenase family.
Required for regulated cell division, cell wall synthesis and the maintenance of cell shape.
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.
Part of the binding-protein-dependent transport system for molybdenum; probably responsible for the translocation of the substrate across the membrane.
Belongs to the bacterial ribosomal protein bL28 family.
Catalyzes the reversible phosphorylation of UMP to UDP.
Belongs to the NADH dehydrogenase family.
Plays a role in the regulation of phosphate uptake.
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 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.
Belongs to the universal ribosomal protein uL16 family.
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.
Belongs to the aspartate-semialdehyde dehydrogenase family.
Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate.
Belongs to the aspartate/ornithine carbamoyltransferase superfamily. OTCase family.
Belongs to the aminoglycoside phosphotransferase family.
Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
Belongs to the topoisomerase GyrA/ParC subunit family.
Belongs to the type II topoisomerase GyrA/ParC subunit family.
Few gyrases are as efficient as E.coli at forming negative supercoils. Not all organisms have 2 type II topoisomerases; in organisms with a single type II topoisomerase this enzyme also has to decatenate newly replicated chromosomes.
Heterotetramer, composed of two GyrA and two GyrB chains. In the heterotetramer, GyrA contains the active site tyrosine that forms a transient covalent intermediate with DNA, while GyrB binds cofactors and catalyzes ATP hydrolysis.
Belongs to the universal ribosomal protein uS2 family.
Belongs to the bacterial ribosomal protein bL35 family.
Belongs to the arginine deiminase family.
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released.
Bifunctional enzyme that catalyzes the GTP-dependent successive addition of multiple gamma-linked L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form polyglutamated F420 derivatives, and the FMNH2-dependent reduction of dehydro-F420-0 to form F420-0.
Binds 2 divalent metal cations per subunit. The ions could be magnesium and/or manganese.
In the N-terminal section; belongs to the CofE family.
Monovalent cation. The ion could be potassium.
Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.
Belongs to the protoporphyrinogen/coproporphyrinogen oxidase family. Coproporphyrinogen III oxidase subfamily.
Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin III.
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
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.
Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
In the C-terminal section; belongs to the UPF0157 (GrpB) family.
In the N-terminal section; belongs to the CoaE family.
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 pseudouridine synthase TruB family. Type 1 subfamily.
Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Negative regulator of class I heat shock genes (grpE-dnaK-dnaJ and groELS operons). Prevents heat-shock induction of these operons.
Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
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).
Belongs to the AB hydrolase superfamily. Lipase family.
Belongs to the saccharopine dehydrogenase family. Enoyl reductase subfamily.
Belongs to the prolyl-tRNA editing family. YbaK/EbsC subfamily.
Belongs to the iron/manganese superoxide dismutase family.
Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Belongs to the ATP-dependent AMP-binding enzyme family.
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.
Decarboxylates branched-chain and aromatic alpha-keto acids to aldehydes.
Belongs to the uracil-DNA glycosylase (UDG) superfamily. Type 5 (UDGb) family.
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 type-II 3-dehydroquinase family.
Catalyzes a trans-dehydration via an enolate intermediate.
Catalyzes the synthesis of GMP from XMP.
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 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.
Involved in protein export. Participates in an early event of protein translocation.
Belongs to the 4-hydroxy-2-oxovalerate aldolase family.
Belongs to the heme-copper respiratory oxidase family.
Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.
Belongs to the argininosuccinate synthase family. Type 1 subfamily.
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.
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.
Belongs to the band 7/mec-2 family. Flotillin subfamily.
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.
Belongs to the glucosamine/galactosamine-6-phosphate isomerase family. 6-phosphogluconolactonase subfamily.
Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
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.
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.
Belongs to the bacterial ribosomal protein bL17 family.
Part of the 50S ribosomal subunit. Contacts protein L32.
Belongs to the universal ribosomal protein uL30 family.
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF.
Belongs to the threonine synthase family.
Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine.
Also displays a weak uracil phosphoribosyltransferase activity which is not physiologically significant.
Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrR subfamily.
Regulates the transcription of the pyrimidine nucleotide (pyr) operon in response to exogenous pyrimidines.
Belongs to the RNA polymerase beta' chain family.
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
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.
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 complex I 24 kDa subunit family.
Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.
Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family.
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 universal ribosomal protein uS14 family. Zinc-binding uS14 subfamily.
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.
Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.
Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Belongs to the asparagine synthetase family.
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.
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Belongs to the amidase family. GatA subfamily.
Catalyzes the hydrolysis of the gamma-glutamyl amide bond of hercynyl-gamma-L-glutamyl-L-cysteine sulfoxide to produce hercynylcysteine sulfoxide, a step in the biosynthesis pathway of ergothioneine.
Belongs to the UDP-galactopyranose/dTDP-fucopyranose mutase family.
Belongs to the MenA family. Type 1 subfamily.
Conversion of 1,4-dihydroxy-2-naphthoate (DHNA) to demethylmenaquinone (DMK).
Belongs to the 'phage' integrase family. XerC subfamily.
Forms a cyclic heterotetrameric complex composed of two molecules of XerC and two molecules of XerD.
Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC-XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids.
Belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family.
Carbamylation allows a single lysine to coordinate two nickel ions.
Carboxylation allows a single lysine to coordinate two nickel ions.
Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha) subunits. Three heterotrimers associate to form the active enzyme.
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 complex I subunit 4L family.
NDH-1 is composed of 14 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex.
Belongs to the pseudouridine synthase RluA family.
Responsible for synthesis of pseudouridine from uracil.
Belongs to the heat shock protein 90 family.
Molecular chaperone. Has ATPase activity.
Belongs to the aconitase/IPM isomerase family. LeuC type 1 subfamily.
Belongs to the prokaryotic/mitochondrial release factor family.
Methylated by PrmC. Methylation increases the termination efficiency of RF1.
Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
Belongs to the glutaminase PdxT/SNO family.
Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
In the presence of PdxS, forms a dodecamer of heterodimers. Only shows activity in the heterodimer.
Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.
In the C-terminal section; belongs to the radical SAM superfamily. CofH family.
In the N-terminal section; belongs to the radical SAM superfamily. CofG 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.
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.
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 truncated hemoglobin family. Group I subfamily.
Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes.
Belongs to the beta-class carbonic anhydrase family.
Catalyzes the reversible hydration of carbon dioxide to form bicarbonate.
Catalyzes the reduction of sulfite to sulfide, a step in the biosynthesis of sulfur-containing amino acids and cofactors.
Belongs to the glycosyltransferase 85 family.
Belongs to the iron-sulfur dependent L-serine dehydratase family.
Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin.
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.
Belongs to the ThrE exporter (TC 2.A.79) family.
Belongs to the prokaryotic ubiquitin-like protein family.
Is modified by deamidation of its C-terminal glutamine to glutamate by the deamidase Dop, a prerequisite to the subsequent pupylation process.
Protein modifier that is covalently attached to lysine residues of substrate proteins, thereby targeting them for proteasomal degradation. The tagging system is termed pupylation.
Strongly interacts with the proteasome-associated ATPase ARC through a hydrophobic interface; the interacting region of Pup lies in its C-terminal half. There is one Pup binding site per ARC hexamer ring.
The N-terminal unstructured half of Pup provides a signal required to initiate unfolding and degradation by the proteasome but is not needed for pupylation, while the C-terminal helical half of Pup interacts with ARC to target proteins to the proteasome.
Belongs to the acetyl-CoA hydrolase/transferase family.
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.
Belongs to the ABC transporter superfamily.
Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Belongs to the fatty acid desaturase type 1 family. AlkB subfamily.
Belongs to the ACC deaminase/D-cysteine desulfhydrase family.
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 GatB/GatE family. GatB subfamily.
Component of the Sec protein translocase complex. Heterotrimer consisting of SecY, SecE and SecG subunits. The heterotrimers can form oligomers, although 1 heterotrimer is thought to be able to translocate proteins. Interacts with the ribosome. Interacts with SecDF, and other proteins may be involved. Interacts with SecA.
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
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.
Belongs to the peroxiredoxin family. Tpx subfamily.
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.
Belongs to the mannose-6-phosphate isomerase type 1 family.
Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Belongs to the fatty acid desaturase type 2 family.
Belongs to the transferase hexapeptide repeat family.
Tetramer of two alpha and two beta chains.
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Belongs to the prokaryotic pantothenate kinase family.
Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase.
Belongs to the bacterial ribosomal protein bL36 family.
Cell division protein that is part of the divisome complex and is recruited early to the Z-ring. Probably stimulates Z-ring formation, perhaps through the cross-linking of FtsZ protofilaments. Its function overlaps with FtsA.
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 homogentisate dioxygenase family.
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.
Part of the 30S ribosomal subunit. Contacts proteins S8 and S17. May interact with IF1 in the 30S initiation complex.
With S4 and S5 plays an important role in translational accuracy.
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 GTP cyclohydrolase I family.
Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the insertion of ferrous iron into coproporphyrin III to form Fe-coproporphyrin III.
Belongs to the bacterial ribosomal protein bS16 family.
Belongs to the ATPase alpha/beta chains family.
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
Binds 1 heme b group per subunit, that coordinates a highly solvent-exposed Fe(III) atom.
Forms a 10-stranded antiparallel beta-barrel structure able to accommodate a hydrophobic ligand in its interior. In fact, this fold hosts the heme group, which is located in a wide surface cleft.
Heme-binding protein able to scavenge peroxynitrite and to protect free L-tyrosine against peroxynitrite-mediated nitration, by acting as a peroxynitrite isomerase that converts peroxynitrite to nitrate. Therefore, this protein likely plays a role in peroxynitrite sensing and in the detoxification of reactive nitrogen and oxygen species (RNS and ROS, respectively). Is able to bind nitric oxide (NO) in vitro, but may act as a sensor of peroxynitrite levels in vivo.
Associates with subunits I, II and III to form cytochrome c oxidase.
Belongs to the cytochrome c oxidase bacterial subunit CtaF family.
Part of cytochrome c oxidase, its function is unknown.
Belongs to the glycosyltransferase 20 family.
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).
Belongs to the universal ribosomal protein uL15 family.
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.
In the C-terminal section; belongs to the phosphate acetyltransferase and butyryltransferase family.
In the N-terminal section; belongs to the CobB/CobQ family.
The N-terminal region seems to be important for proper quaternary structure. The C-terminal region contains the substrate-binding site.
Belongs to the class II fructose-bisphosphate aldolase family.
Binds 2 Zn(2+) ions per subunit. One is catalytic and the other provides a structural contribution.
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.
A 50S ribosomal subunit assembly protein with GTPase activity, required for 50S subunit assembly at low temperatures, may also play a role in translation. Binds GTP and analogs. Binds the 70S ribosome between the 30S and 50S subunits, in a similar position as ribosome-bound EF-G; it contacts a number of ribosomal proteins, both rRNAs and the A-site tRNA.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. BipA subfamily.
With LigD forms a non-homologous end joining (NHEJ) DNA repair enzyme, which repairs dsDNA breaks with reduced fidelity. Binds linear dsDNA with 5'- and 3'- overhangs but not closed circular dsDNA nor ssDNA. Recruits and stimulates the ligase activity of LigD.
Belongs to the GHMP kinase family. Homoserine kinase subfamily.
Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
Belongs to the glucose-1-phosphate thymidylyltransferase family.
Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis.
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 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.
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.
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 class-I aminoacyl-tRNA synthetase family.
Belongs to the nucleobase:cation symporter-2 (NCS2) (TC 2.A.40) family.
Belongs to the type-B carboxylesterase/lipase family.
Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
Belongs to the polyribonucleotide nucleotidyltransferase family.
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Belongs to the methylmalonyl-CoA epimerase family.
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.
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.
Belongs to the carbon-nitrogen hydrolase superfamily. NIT1/NIT2 family.
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.
Belongs to the transaldolase family. Type 2 subfamily.
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Belongs to the acetaldehyde dehydrogenase family.
Belongs to the alpha-acetolactate decarboxylase family.
Belongs to the NAD(P)-dependent epimerase/dehydratase family. SDR39U1 subfamily.
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 ETF alpha-subunit/FixB family.
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
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.
APS kinase catalyzes the synthesis of activated sulfate.
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. CysN/NodQ subfamily.
Catalyzes the synthesis of activated sulfate.
Heterodimer composed of CysD, the smaller subunit, and CysN.
In the C-terminal section; belongs to the APS kinase family.
In the N-terminal section; belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. CysN/NodQ subfamily.
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.
Belongs to the SAICAR synthetase family.
Belongs to the glycosyl hydrolase 13 family. TreS subfamily.
Belongs to the class II aldolase/RraA-like family.
Catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2-oxoglutarate (HMG) into 2 molecules of pyruvate. Also contains a secondary oxaloacetate (OAA) decarboxylase activity due to the common pyruvate enolate transition state formed following C-C bond cleavage in the retro-aldol and decarboxylation reactions.
Belongs to the complex I subunit 2 family.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family.
Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family. TrmL subfamily.
Could methylate the ribose at the nucleotide 34 wobble position in tRNA.
Belongs to the urease beta subunit family.
Catalyzes the oxidative sulfurization of hercynine (N-alpha,N-alpha,N-alpha-trimethyl-L-histidine) into hercynyl-gamma-L-glutamyl-L-cysteine sulfoxide, a step in the biosynthesis pathway of ergothioneine.
Belongs to the bacterial ribosomal protein bL9 family.
Belongs to the Mg-chelatase subunits D/I family. ComM subfamily.
Belongs to the LDH/MDH superfamily. MDH type 2 family.
Catalyzes the reversible oxidation of malate to oxaloacetate.
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.
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
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.
Acyl carrier protein involved in meromycolate extension.
Belongs to the acyl carrier protein (ACP) family.
Carrier of the growing fatty acid chain in fatty acid biosynthesis.
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 isocitrate lyase/PEP mutase superfamily. Methylisocitrate lyase family.
Catalyzes the thermodynamically favored C-C bond cleavage of (2R,3S)-2-methylisocitrate to yield pyruvate and succinate.
Belongs to the ATPase delta chain family.
In the C-terminal section; belongs to the ATPase delta chain family.
In the N-terminal section; belongs to the ATPase B chain family.
This fusion protein includes a component of the F(0) channel (subunit b) and of the F(1) subunit (subunit delta). Two copies of subunit b and one of delta together form the peripheral 'stator' stalk which links F(1) to F(0).
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.
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
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.
Belongs to the bacterial ribosomal protein bL25 family. CTC subfamily.
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 adenosylhomocysteinase family.
May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine.
Catalyzes the methylation of methanethiol (MeSH) to yield dimethylsulphide (DMS).
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.
Monomer and homodimer. Part of the essential Sec protein translocation apparatus which comprises SecA, SecYEG and auxiliary proteins SecDF. Other proteins may also be involved.
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Belongs to the thiolase-like superfamily. Chalcone/stilbene synthases family.
Belongs to the glycosyl hydrolase 5 (cellulase A) family.
Belongs to the Stf0 sulfotransferase family.
Catalyzes the sulfuryl group transfer from 3'-phosphoadenosine-5'-phosphosulfate (PAPS) to trehalose, leading to trehalose-2-sulfate (T2S).
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 cyclophilin-type PPIase family.
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits.
Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
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 menaquinone. 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.
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 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. Other proteins may also be involved.
Belongs to the trehalose phosphatase family.
Removes the phosphate from trehalose 6-phosphate to produce free trehalose.
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 RNA polymerase-binding protein RbpA family.
Binds to RNA polymerase (RNAP), stimulating transcription from principal, but not alternative sigma factor promoters.
Forms a complex with the RNAP catalytic core and with free principal sigma factors.
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.
Belongs to the 'phage' integrase family. XerD subfamily.
Belongs to the universal ribosomal protein uS10 family.
Involved in the binding of tRNA to the ribosomes.
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 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.
Belongs to the ribose-phosphate pyrophosphokinase family. Class I subfamily.
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).
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 class-II pyridine nucleotide-disulfide oxidoreductase family.
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 urease gamma subunit family.
Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 2 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.
Belongs to the helicase family. DnaB subfamily.
Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity.
Belongs to the NiCoT transporter (TC 2.A.52) family.
Belongs to the carbohydrate kinase PfkB family.
Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35) family.
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.
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 fructosamine kinase family.
Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family.
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIIA subfamily.
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 acetolactate synthase small subunit family.
Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine.
Belongs to the NAD(P)-dependent epimerase/dehydratase family. dTDP-glucose dehydratase subfamily.
Belongs to the carotenoid/retinoid oxidoreductase family.
Belongs to the imidazoleglycerol-phosphate dehydratase family.
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.
Has an organic peroxide-dependent peroxidase activity.
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.
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.
Catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to formate and tetrahydrofolate (FH4).
Methylated by PrmC. Methylation increases the termination efficiency of RF2.
Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA.
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.
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.
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.
Belongs to the class I-like SAM-binding methyltransferase superfamily. TRM61 family.
Catalyzes the S-adenosyl-L-methionine-dependent formation of N(1)-methyladenine at position 58 (m1A58) in tRNA.
Homotetramer composed of a dimer of dimers.
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.
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
UreD, UreF and UreG form a complex that acts as a GTP-hydrolysis-dependent molecular chaperone, activating the urease apoprotein by helping to assemble the nickel containing metallocenter of UreC. The UreE protein probably delivers the nickel.
Belongs to the haloalkane dehalogenase family. Type 1 subfamily.
Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons.
Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
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.
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 uroporphyrinogen decarboxylase family.
Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Belongs to the complex I subunit 3 family.
Belongs to the dGTPase family. Type 2 subfamily.
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 RNA methyltransferase TrmD family.
Specifically methylates guanosine-37 in various tRNAs.
Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.
Belongs to the NucS endonuclease family.
Cleaves both 3' and 5' ssDNA extremities of branched DNA structures.
Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.
Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Belongs to the bacterial ribosomal protein bL31 family. Type A subfamily.
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.
The complex is composed of two ATP-binding proteins (CysA), two transmembrane proteins (CysT and CysW) and a solute-binding protein (CysP).
Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.