STRINGSTRING
tlpC tlpC hemAT hemAT motB motB motA motA mcpC mcpC cheV cheV 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 cheR cheR ytxE ytxE ytxD ytxD tlpB tlpB mcpA mcpA tlpA tlpA mcpB mcpB yvaQ yvaQ yvzB yvzB fliD fliD hag hag flhP flhP flhO flhO
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
tlpCMethyl-accepting chemotaxis protein; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; receptor. (573 aa)
hemATHaem-based dioxygen sensor; Heme-containing signal transducer responsible for aerotaxis, the migratory response toward or away from oxygen. (432 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)
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)
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)
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)
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)
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)
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)
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)
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)
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)
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)
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
Server load: low (22%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.