STRINGSTRING
ybdO ybdO mpr mpr cwlK cwlK tlpC tlpC ydaJ ydaJ ydaK ydaK ydaL ydaL ydaM ydaM ydaN ydaN ndoAI ndoAI ndoA ndoA rsbRA rsbRA rsbS rsbS rsbT rsbT rsbU rsbU rsbV rsbV rsbW rsbW sigB sigB rsbX rsbX ydcF ydcF ydcG ydcG ydcH ydcH sapB sapB yfmT yfmT yfmS yfmS yfjQ yfjQ yhcK yhcK yhcR yhcR srtA srtA lytF lytF prsA prsA yhfN yhfN aprE aprE hemAT hemAT wprA wprA nprB nprB yjbE yjbE yjcP yjcP yjcQ yjcQ yjfB yjfB htrA htrA isp isp rsbRB rsbRB ykoW ykoW motB motB motA motA ykvY ykvY mcpC mcpC cheV cheV ykuI ykuI ampS ampS ykpC ykpC nprE nprE bpr bpr yloB yloB ylqB ylqB ylqG ylqG ylqH ylqH flgB flgB flgC flgC fliE fliE fliF fliF fliG fliG fliH fliH fliI fliI fliJ fliJ ylxF ylxF fliK fliK flgD flgD flgE flgE ylzI ylzI fliL fliL fliM fliM fliY fliY cheY cheY fliZ fliZ fliP fliP fliQ fliQ fliR fliR flhB flhB flhA flhA flhF flhF ylxH ylxH cheB cheB cheA cheA cheW cheW cheC cheC cheD cheD sigD sigD aprX aprX cwlC cwlC ccdA ccdA yneI yneI yneJ yneJ ggt ggt yoaH yoaH cwlS cwlS cheR cheR ypfA ypfA rsbRD rsbRD cwlH cwlH yrvJ yrvJ yscB yscB ytrP ytrP ytxE ytxE ytxD ytxD ytaP ytaP ytvA ytvA lytG lytG tlpB tlpB mcpA mcpA tlpA tlpA mcpB mcpB yuxH yuxH pepA pepA yuxL yuxL yusZ yusZ htrB htrB cssR cssR cssS cssS yuxN yuxN yvaQ yvaQ rsbQ rsbQ rsbP rsbP pnbA pnbA yvzB yvzB yvzG yvzG fliT fliT fliS fliS fliD fliD yvyC yvyC hag hag csrA csrA fliW fliW yviE yviE flgL flgL flgK flgK yvyG yvyG flgM flgM yvyF yvyF lytC lytC lytB lytB lytA lytA lytD lytD ywrD ywrD ywpE ywpE flhP flhP flhO flhO vpr vpr epr epr ywaD ywaD yxkC yxkC yyaK yyaK
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
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a 3D structure is known or predicted
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ybdOPutative phage protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; extrachromosomal origin. (394 aa)
mprExtracellular glutamyl-endopeptidase; Evidence 1c: Function experimentally demonstrated in the studied genus; Product type e: enzyme; Belongs to the peptidase S1B family. (313 aa)
cwlKMurein L,D:-endopeptidase; Cleaves the linkage of the L-alanine-D-glutamic acid of B.subtilis cell wall; Belongs to the peptidase M15C family. (167 aa)
tlpCMethyl-accepting chemotaxis protein; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; receptor. (573 aa)
ydaJPutative glycosyl hydrolase lipoprotein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type lp: lipoprotein. (362 aa)
ydaKPutative membrane protein with diguanylate cyclase domain; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pm: putative membrane component. (283 aa)
ydaLConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. (569 aa)
ydaMPutative glycosyltransferase associated to biofilm formation; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (420 aa)
ydaNPutative regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. (703 aa)
ndoAIAntitoxin EndoAI; Antitoxin component of a type II toxin-antitoxin (TA) system. Antitoxin that directly inhibits activity of EndoA in vitro. Upon expression in E.coli counteracts inhibitory effect of endoribonuclease EndoA. The EndoA-EndoAI complex does not seem to bind its own promoter. (93 aa)
ndoAEndoribonuclease toxin; Toxic component of a type II toxin-antitoxin (TA) system. Specific for 5'-UACAU-3' sequences, cleaving after the first U. Yields cleavage products with 3' phosphate and 5' hydroxyl groups. Cannot digest substrate with a UUdUACAUAA cleavage site. Overexpression is toxic for cell growth (shown in E.coli), probably by inhibiting protein synthesis through the cleavage of single-stranded RNA. The toxicity is reversed by the antitoxin EndoAI. Toxin activity cannot be inhibited by MazE from E.coli. The EndoA-EndoAI complex does not seem to bind its own promoter. (116 aa)
rsbRAComponent of the piezosome (stressosome); Acts as a positive regulator of sigma-B activity in response to salt and heat stress by stimulating the activity of the RsbT kinase toward RsbS in vitro. Negative regulator of sigma-B activity. Non-phosphorylated RsbS binds to RsbT, preventing its association with RsbU. Requires any one of RsbRA, RsbRB, RsbRC or RsbRD to sequester RsbT. When RsbS and the RsbR paralog(s) are phosphorylated, they release RsbT, which can then bind and activate RsbU. (274 aa)
rsbSAntagonist of RsbT; Negative regulator of sigma-B activity. Non-phosphorylated RsbS binds to RsbT, preventing its association with RsbU. Requires any one of RsbRA, RsbRB, RsbRC or RsbRD to sequester RsbT. When RsbS and the RsbR paralog(s) are phosphorylated, they release RsbT, which can then bind and activate RsbU. (121 aa)
rsbTSwitch protein/serine-threonine kinase; Provides the crucial link between the upstream module (communication of environmental stress) and the downstream module (integration of the environmental signals with signals of energy stress) that compose the signal transduction pathway controlling the sigma-B factor. Phosphorylates and inactivates its specific antagonist protein RsbS thanks to its serine kinase activity. Upon phosphorylation of RsbS, RsbT is released to stimulate RsbU, a PP2C phosphatase, thereby initiating the signaling cascade that ultimately activates sigma-B. The activity o [...] (133 aa)
rsbUSerine phosphatase; Positive regulator of sigma-B activity. Dephosphorylates RsbV in response to environmental stress conveyed from the RsbXST module. (335 aa)
rsbVAnti-anti-sigma factor (antagonist of RsbW); Positive regulator of sigma-B activity. Non-phosphorylated RsbV binds to RsbW, preventing its association with sigma-B. When phosphorylated, releases RsbW, which is then free to complex with and inactivate sigma-B. (109 aa)
rsbWSwitch protein/serine kinase and anti-sigma factor (inhibitory sigma-B binding protein); Negative regulator of sigma-B activity. Phosphorylates and inactivates its specific antagonist protein, RsbV. Upon phosphorylation of RsbV, RsbW is released and binds to sigma-B, thereby blocking its ability to form an RNA polymerase holoenzyme (E-sigma-B). (160 aa)
sigBRNA polymerase sigma-37 factor (sigma(B)); Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Sigma B is not essential for sporulation; rather it is required for maximal expression of ctc and csbA which are transcribed in the early stationary phase under conditions inimical to sporulation. May play a role in the ability of the bacterium to adapt to various stresses but is not essential for its survival under these conditions. Positively regulates expression of its own operon; Belongs to the sigma-70 fac [...] (262 aa)
rsbXSerine phosphatase; Negative regulator of sigma-B activity. Dephosphorylates RsbS. Plays a role both in maintaining low sigma-B activity during growth and in reestablishing prestress sigma-B activity after induction. Could have a negative feedback role by indirectly communicating sigma-B protein levels. (199 aa)
ydcFHypothetical protein; Evidence 5: No homology to any previously reported sequences. (97 aa)
ydcGConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; Belongs to the UPF0310 family. (146 aa)
ydcHPutative transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. (147 aa)
sapBMembrane component; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type ph: phenotype. (232 aa)
yfmTPutative aldehyde dehydrogenase; A benzaldehyde dehydrogenase able to act on substrates with 3- and 4-hydroxy and methoxy substitutions; converts vanillin (4- hydroxy-3-methoxybenzaldehyde) to vanillic acid in vitro. The physiological substrate is unknown. (485 aa)
yfmSPutative chemotaxis sensory transducer; Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. Attractants increase the level of methylation while repellents decrease the level of methylation (By similarity). (286 aa)
yfjQPutative divalent cation transport protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative transporter. (319 aa)
yhcKPutative diguanylate cyclase or phosphodiesterase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (359 aa)
yhcRNon specific extracellular endonuclease cleaving RNA and DNA; Sugar-nonspecific endonuclease that yields nucleotide 3'- monophosphate products. No 5'-nucleotidase activity was detected, using 5'-AMP as the substrate, in the presence of diverse divalent metals and with various pH values. (1217 aa)
srtASortase A; Transpeptidase that anchors surface proteins to the cell wall. Recognizes and modifies its substrate by proteolytic cleavage of a C-terminal sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the sortase and its substrate, which is then transferred and covalently attached to the cell wall (Probable). This sortase recognizes a Leu-Pro-Asp-Thr-Ser/Ala (LPDTS/A) motif. It has two substrates, YhcR and YfkN. Belongs to the bacterial sortase family. Class D subfamily. (198 aa)
lytFgamma-D-glutamate-meso-diaminopimelate muropeptidase (major autolysin); Cell wall hydrolase that cleaves gamma-D-glutamate-meso- diaminopimelate bonds in peptidoglycan. LytF is necessary and sufficient for vegetative daughter cell separation, and also seems to play a role in cell autolysis. (488 aa)
prsAMolecular chaperone lipoprotein; Essential protein that plays a major role in protein secretion by helping the post-translocational extracellular folding of several secreted proteins. Has PPIase activity but it is not essential for its function in vivo; Belongs to the PrsA family. (292 aa)
yhfNPutative membrane metalloprotease; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (426 aa)
aprESerine alkaline protease (subtilisin E); Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides; Belongs to the peptidase S8 family. (381 aa)
hemATHaem-based dioxygen sensor; Heme-containing signal transducer responsible for aerotaxis, the migratory response toward or away from oxygen. (432 aa)
wprACell wall-associated protease; CWBP52 is a serine-type protease that could be involved in proteoglycan peptide bridges; Belongs to the peptidase S8 family. (894 aa)
nprBExtracellular neutral protease B; Protease able to cleave casein in vitro. Belongs to the peptidase M4 family. (538 aa)
yjbEPutative transporter component; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter. (218 aa)
yjcPConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 15033535. (167 aa)
yjcQConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 15033535. (94 aa)
yjfBConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 15033535. (55 aa)
htrAMembrane bound serine protease Do, quality control protease (heat-shock protein); Degrades abnormal exported proteins and responsible for the propeptide processing of a natural pro-protein and for the maturation of a native protein. It also plays a prominent role in stress (heat shock, ethanol, puromycin and NaCl) resistance during active exponential growth (Probable); Belongs to the peptidase S1C family. (449 aa)
ispIntracellular serine protease; Major intracellular protease produced by Bacillus subtilis. (319 aa)
rsbRBComponent of the piezosome (stressosome); One of 4 functionally non-identical RsbR paralogs, it functions in the environmental signaling branch of the general stress response. (277 aa)
ykoWPutative sensor diguanylate cyclase; Probable signaling protein whose physiological role is not yet known. (800 aa)
motBMotility protein B; MotA and MotB comprise the stator element of the flagellar motor complex. Required for the rotation of the flagellar motor. Might be a linker that fastens the torque-generating machinery to the cell wall (By similarity). (261 aa)
motAMotility protein A; MotA and MotB comprise the stator element of the flagellar motor complex. Required for rotation of the flagellar motor. Probable transmembrane proton channel (By similarity). (270 aa)
ykvYPutative Xaa-Pro dipeptidase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (363 aa)
mcpCMethyl-accepting chemotaxis protein; Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. All amino acids serve as attractants in B.subtilis, they appear to cause an increase in the turnover methyl groups, leading to methylation of an unidentified acceptor, while repellents have been shown to cause a decrease in methyl group turnover. The methyl groups are added by a methyl [...] (655 aa)
cheVCoupling protein and response regulator for CheA activity in response to attractants (chemotaxis); Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. Chemotaxis involves both a phosphorylation-dependent excitation and a methylation-dependent adaptation. CheV and CheW are involved in the coupling of the methyl- accepting chemoreceptors to the central two-component kinase CheA; they are both necessary for efficient chemotaxis. Moreover, CheA-dependent phosphorylation of CheV is required for adaptation to attractants during B.subtilis chemotaxis. (303 aa)
ykuIConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. (407 aa)
ampSAminopeptidase; Metal-dependent exopeptidase; Belongs to the peptidase M29 family. (410 aa)
ykpCConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. (44 aa)
nprEExtracellular neutral metalloprotease; Extracellular zinc metalloprotease; Belongs to the peptidase M4 family. (521 aa)
bprEvidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (1433 aa)
yloBP-type calcium transport ATPase; This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium. (890 aa)
ylqBConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 15033535. (161 aa)
ylqGPutative glycosyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (576 aa)
ylqHPutative flagellar biosynthesis protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pf: putative factor. (93 aa)
flgBFlagellar component of cell-proximal portion of basal-body rod; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. (129 aa)
flgCFlagellar component of cell-proximal portion of basal-body rod; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type s: structure; Belongs to the flagella basal body rod proteins family. (150 aa)
fliEFlagellar basal body protein; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type s: structure. (106 aa)
fliFFlagellar basal-body M-ring protein; The M ring may be actively involved in energy transduction. (536 aa)
fliGFlagellar motor switching and energizing component; One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation; Belongs to the FliG family. (338 aa)
fliHFlagellar export apparatus component; Needed for flagellar regrowth and assembly. (208 aa)
fliIFlagellar-specific ATPase; Probable catalytic subunit of a protein translocase for flagellum-specific export, or a proton translocase involved in local circuits at the flagellum. (438 aa)
fliJFlagellar synthesis chaperone; Flagellar protein that affects chemotactic events. (147 aa)
ylxFPutative kinesin-like protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type ps: putative structure. (204 aa)
fliKFlagellar hook-length control protein; Controls the length of the flagellar hook. (487 aa)
flgDFlagellar hook assembly protein; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type pf: putative factor; Belongs to the FlgD family. (140 aa)
flgEFlagellar hook protein; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type f: factor; Belongs to the flagella basal body rod proteins family. (264 aa)
ylzIPutative flagellar protein; Required for swarming motility. Increases flagellar power, probably via the flagellar stator components MotA and MotB. (71 aa)
fliLFlagellar basal-body associated protein; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. (140 aa)
fliMFlagellar motor switching and energizing component; One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation; Belongs to the FliM family. (332 aa)
fliYFlagellar motor switching and energizing phosphatase; Component of the flagellar switch. Binds CheY-P and increases its hydrolysis rate in vitro. May function constitutively to remove CheY-P around the flagellar switch to maintain an optimal level of CheY-P whereas CheC may function after addition of an attractant to cope with increased levels of CheY-P; Belongs to the FliN/MopA/SpaO family. (378 aa)
cheYRegulator of chemotaxis and motility; Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. Phosphorylated CheY interacts with the flagella switch components FliM and FliY, which causes counterclockwise rotation of the flagella, resulting in smooth swimming. (120 aa)
fliZFlagellar regulatory protein; May be a structural component of the flagellum that anchors the rod to the membrane. (219 aa)
fliPComponent of the flagellar export machinery; Plays a role in the flagellum-specific transport system. Belongs to the FliP/MopC/SpaP family. (221 aa)
fliQComponent of the flagellar export machinery; Role in flagellar biosynthesis; Belongs to the FliQ/MopD/SpaQ family. (89 aa)
fliRComponent of the flagellar export machinery; Role in flagellar biosynthesis; Belongs to the FliR/MopE/SpaR family. (259 aa)
flhBComponent of the flagellar export machinery; May be involved in the export of flagellum proteins; Belongs to the type III secretion exporter family. (360 aa)
flhAComponent of the flagellar export machinery; Involved in the export of flagellum proteins. (677 aa)
flhFGTPase involved in the export of flagella; Necessary for flagellar biosynthesis. May be involved in translocation of the flagellum. (366 aa)
ylxHEssential component of the flagellar assembly machinery; Involved in the placement and assembly of flagella (By similarity). Activates the SRP-GTPase activity of FlhF. (298 aa)
cheBMethyl-accepting chemotaxis proteins (MCP)-glutamate methylesterase; Involved in the modulation of the chemotaxis system; catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by CheR. B.subtilis has an effective methylation-independent adaptation system but must utilize the methylation system for adaptation to high concentrations of attractant; Belongs to the CheB family. (357 aa)
cheAChemotactic two-component sensor histidine kinase; Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to CheB, CheY or CheV. (672 aa)
cheWModulation of CheA activity in response to attractants (chemotaxis); Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheV and CheW are involved in the coupling of the methyl-accepting chemoreceptors to the central two- component kinase CheA; they are both necessary for efficient chemotaxis. (156 aa)
cheCCheY-P phosphatase CheC; Involved in restoring normal CheY-P levels following the addition of attractant by increasing the rate of CheY-P hydrolysis. Is only 6% as active as FliY, which indicates that CheC may function after addition of an attractant to cope with increased levels of CheY-P whereas FliY may function constitutively to remove CheY-P around the flagellar switch to maintain an optimal level of CheY-P. In addition, it was shown to prevent methylation of the methyl-accepting chemotaxis proteins (MCPs). Inhibits CheD. (209 aa)
cheDChemoreceptor glutamine deamidase CheD; Deamidates 'Gln-593' and 'Gln-594' of the chemoreceptor McpA. In addition, deamidates other chemoreceptors, including McpB and McpC. CheD-mediated MCP (methyl-accepting chemotaxis proteins) deamidation is required for productive communication of the conformational signals of the chemoreceptors to the CheA kinase. CheD is absolutely required for a behavioral response mediated by McpC but is not required for the response to asparagine mediated by McpB. CheD is necessary for the generation of wild-type prestimulus CheA autophosphorylation levels. Al [...] (166 aa)
sigDRNA polymerase sigma-28 factor (sigma-D); Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This alternative sigma factor is required for the transcription of the flagellin and motility genes as well as for wild- type chemotaxis. (254 aa)
aprXAlkaline serine protease; Displays serine protease activity. Seems to have a broad substrate specificity. (442 aa)
cwlCN-acetylmuramoyl-L-alanine amidase; Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella - in particular of its basal body - and sporulation. CwlC is able to hydrolyze type A cell walls such as B.subtilis. Its main function is to lyze the mother cell wall peptidoglycan, playing a role during sporulation. Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family. (255 aa)
ccdACytochrome c-type biogenesis protein CcdA; Required for cytochrome c synthesis and stage V of sporulation. Might transfer reducing equivalents across the cytoplasmic membrane, promoting efficient disulfide bond isomerization of proteins localized on the outer surface of the membrane or in the spore coat. (235 aa)
yneIPutative response regulator (CheY homolog); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. (120 aa)
yneJPutative integral inner membrane protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pm: putative membrane component. (163 aa)
ggtMembrane bound gamma-glutamyltranspeptidase; Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases; Belongs to the gamma-glutamyltransferase family. (587 aa)
yoaHPutative methyl-accepting chemotaxis protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative factor. (561 aa)
cwlSPeptidoglycan hydrolase (cell wall-binding d,l-endopeptidase); Probably functions as a cell separation enzyme in addition to LytE and LytF. (414 aa)
cheRMethyl-accepting chemotaxis proteins (MCPs) methyltransferase; Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP. CheR is responsible for the chemotactic adaptation to repellents. (256 aa)
ypfAPutative cyclic diGMP binding protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. (217 aa)
rsbRDComponent of the piezosome (stressosome); One of 4 functionally non-identical RsbR paralogs, it functions in the environmental signaling branch of the general stress response. (278 aa)
cwlHN-acetylmuramoyl-L-alanine amidase; Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella and sporulation. Could play a role in mother cell lysis with CwlC; Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family. (250 aa)
yrvJPutative N-acetylmuramoyl-L-alanine amidase, family 3; Probably involved in cell-wall metabolism. (518 aa)
yscBPutative lipoprotein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; lipoprotein. (221 aa)
ytrPPutative diguanylate cyclase-related enzyme; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (579 aa)
ytxEPutative flagellar motor apparatus component; May be involved in some transport function; Belongs to the MotB family. (242 aa)
ytxDPutative flagellar motor component; May be involved in some transport function; Belongs to the MotA family. (272 aa)
ytaPPutative hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the dienelactone hydrolase family. (299 aa)
ytvABlue light GTP-binding receptor; Exhibits the same spectroscopical features and blue-light induced photochemistry as plants phototropins, with the reversible formation of a blue-shifted photoproduct, assigned to an FMN-cysteine thiol adduct. Although it is a positive regulator in the activation of the environmental signaling branch of the general stress transcription factor sigma-B, its precise role is undetermined. (261 aa)
lytGExoglucosaminidase; Is the major glucosaminidase responsible for peptidoglycan structural determination during vegetative growth. Catalyzes the hydrolysis of 1,4-beta-linkages between N-acetyl-D-glucosamine and N- acetylmuramic acid residues in peptidoglycan. Acts processively from the ends of the glycan strands. Also plays a role in motility, chemotaxis and cell division. (282 aa)
tlpBMethyl-accepting chemotaxis protein; Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. All amino acids serve as attractants in B.subtilis, they appear to cause an increase in the turnover methyl groups, leading to methylation of an unidentified acceptor, while repellents have been shown to cause a decrease in methyl group turnover. The methyl groups are added by a methyl [...] (662 aa)
mcpAMethyl-accepting chemotaxis protein; Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. All amino acids serve as attractants in B.subtilis, they appear to cause an increase in the turnover methyl groups, leading to methylation of an unidentified acceptor, while repellents have been shown to cause a decrease in methyl group turnover. The methyl groups are added by a methyl [...] (661 aa)
tlpAMethyl-accepting chemotaxis protein; Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. All amino acids serve as attractants in B.subtilis, they appear to cause an increase in the turnover methyl groups, leading to methylation of an unidentified acceptor, while repellents have been shown to cause a decrease in methyl group turnover. The methyl groups are added by a methyl [...] (662 aa)
mcpBMethyl-accepting chemotaxis protein; Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. All amino acids serve as attractants in B.subtilis, they appear to cause an increase in the turnover methyl groups, leading to methylation of an unidentified acceptor, while repellents have been shown to cause a decrease in methyl group turnover. The methyl groups are added by a methyl [...] (662 aa)
yuxHPutative phosphodiesterase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (409 aa)
pepALeucyl aminopeptidase; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N- terminal amino acids from various peptides (By similarity). (500 aa)
yuxLPutative acylaminoacyl-peptidase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the peptidase S9C family. (657 aa)
yusZOligoendopeptidase; Evidence 7: Gene remnant; Product type e: enzyme; Belongs to the short-chain dehydrogenases/reductases (SDR) family. (280 aa)
htrBHtrA-like serine protease; Degrades abnormal exported proteins and responsible for the propeptide processing of a natural pro-protein and for the maturation of a native protein. It also plays a prominent role in stress (heat shock, ethanol, puromycin and NaCl) resistance during active exponential growth (Probable); Belongs to the peptidase S1C family. (458 aa)
cssRTwo-component response regulator; Member of the two-component regulatory system CssS/CssR required to control the cellular response to secretion stress. (225 aa)
cssSTwo-component sensor histidine kinase; Member of the two-component regulatory system CssS/CssR required to control the cellular response to secretion stress. Required for the transcription of htrA. Could detect misfolded proteins at the membrane-cell wall interface and then activate CssR by phosphorylation. (451 aa)
yuxNPutative transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator. (291 aa)
yvaQPutative methyl-accepting transducer; Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. Attractants increase the level of methylation while repellents decrease the level of methylation (By similarity). (566 aa)
rsbQRegulator of RsbP phosphatase; Positive regulator required for energy stress activation of the sigma-B transcription factor. Could be required for RsbP phosphatase activity; Belongs to the AB hydrolase superfamily. (269 aa)
rsbPSerine phosphatase; Positive regulator of sigma-B activity. Dephosphorylates RsbV in response to energy stress. (403 aa)
pnbAPara-nitrobenzyl esterase (intracellular esterase B); Catalyzes hydrolysis of several beta-lactam antibiotic PNB esters to the corresponding free acid and PNB alcohol; Belongs to the type-B carboxylesterase/lipase family. (489 aa)
yvzBPutative flagellin; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure; Belongs to the bacterial flagellin family. (160 aa)
yvzGConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. (125 aa)
fliTFlagellar assembly protein FliT involved in control of flagella expression; May act as an export chaperone for the filament capping protein FliD; Belongs to the bacillales FliT family. (113 aa)
fliSFlagellar assembly protein FliS; Essential for filament assembly. May act as a facilitator of flagellin (hag) secretion. Antagonizes translational repressor CsrA indirectly. Belongs to the FliS family. (133 aa)
fliDFlagellar hook-associated capping protein 2 (HAP2); Required for the morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end (By similarity); Belongs to the FliD family. (498 aa)
yvyCPutative flagellar protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. (109 aa)
hagFlagellin protein; Flagellin is the subunit which polymerizes to form the filaments of bacterial flagella. Assembly into flagella requires FliW. Acts as a homeostatic autoinhibitory regulator to control its own cytoplasmic levels. Partner switching by flagellin between FliW and CsrA provides a flagellar assembly checkpoint to tightly control the timing of flagellin synthesis. Flagellin binds to assembly factor FliW, freeing translation regulator CsrA to repress translation of the flagellin mRNA. When the flagellar hook is assembled flagellin is secreted, depleting intracellular flagell [...] (304 aa)
csrACarbon storage regulator; A translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability. Usually binds in the 5'- UTR at or near the Shine-Dalgarno sequence preventing ribosome-binding, thus repressing translation. Represses expression of flagellin (hag) in a post-transcriptional fashion. Specifically binds to 2 sites in the 5'-UTR of hag mRNA in a cooperative fashion; the second site overlaps the Shine-Dalgarno sequence and prevents 30S ribosomal subunit binding. Mutation of either binding site abolishes CsrA regulation of hag expression. Repressio [...] (74 aa)
fliWAssembly factor of the flagellum; Acts as an anti-CsrA protein, binds CsrA and prevents it from repressing translation of its target genes, one of which is flagellin. Binds to flagellin (hag), which is implicated in polymerization, and participates in the assembly of the flagellum. An antagonist to translational regulator CsrA, it binds CsrA at an allosteric site and non-competitively inhibits CsrA binding to hag RNA. Partner switching by flagellin between FliW and CsrA provides a flagellar assembly checkpoint to tightly control the timing of flagellin synthesis. Flagellin binds to ass [...] (143 aa)
yviEConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 15033535. (191 aa)
flgLFlagellar hook-filament junction; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; structure. (298 aa)
flgKFlagellar hook-filament junction; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; structure. (507 aa)
yvyGPutative flagellar protein; May be involved in the assembly, structure, or function of the flagellum. May polymerize to form a filamentous structure that is part of the flagellum. (160 aa)
flgMAnti-sigma factor repressor of sigma(D)-dependent transcription; Allows the coupling of early and late flagellar synthesis through the repression of RNA polymerase sigma-D factor-dependent transcription. (88 aa)
yvyFPutative regulator of flagella formation; May be involved in the assembly, structure, or function of the flagellum. May polymerize to form a filamentous structure that is part of the flagellum. (139 aa)
lytCPutative undecaprenyl-phosphate N-acetylgalactosaminyl-1-phosphate transferase; Autolysins are cell wall hydrolases involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella - in particular of its basal body - and sporulation. Has a high affinity for teichoic acid-endowed peptidoglycan. LytC is required for efficient swarming motility but not at the level of cell separation or flagellum biosynthesis. Rather, LytC appears to be important for proper flagellar function. (496 aa)
lytBModifier protein of major autolysin LytC; Possibly involved in cell wall metabolism during spore formation. Enhances the amidase activity approximately threefold. (705 aa)
lytAMembrane bound lipoprotein; Possible role in the secretion of LytB and LytC. (102 aa)
lytDExported N-acetylglucosaminidase (major autolysin) (CWBP90); Cell wall hydrolase not involved in cell autolysis, competence, sporulation or germination. It hydrolyzes the beta-1,4 glycan bond between the N-acetylglucosaminyl and the N-acetylmuramoyl residues in the glycan chain. (880 aa)
ywrDPutative enzyme; Overexpressed protein with an N-terminal His tag has been reported not to hydrolyze glutathione; it is not clear if the construct is processed to 2 subunits. (525 aa)
ywpEPutative sortase; Seems not to play a major role if any as a sortase. (102 aa)
flhPPutative flagellar hook-basal body protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type ps: putative structure; Belongs to the flagella basal body rod proteins family. (269 aa)
flhOPutative flagellar basal-body rod protein; Not required for motility. (270 aa)
vprExtracellular serine protease; Not required for growth or sporulation. (806 aa)
eprExtracellular serine protease; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the peptidase S8 family. (645 aa)
ywaDDouble-zinc aminopeptidase; Catalyzes the hydrolysis of a range of N-terminal amino acids. (455 aa)
yxkCConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 12823818, 15033535. (180 aa)
yyaKPutative integral inner membrane protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pm: putative membrane component. (299 aa)
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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