STRINGSTRING
fliR fliR fliE fliE fliF fliF fliG fliG fliH fliH fliI fliI fliJ fliJ fliK fliK flgD flgD flgE flgE ylzI ylzI fliM fliM fliY fliY cheY cheY fliP fliP fliQ fliQ flgC flgC flhB flhB flhA flhA flhF flhF cheW cheW ylxL ylxL fliT fliT fliS fliS fliD fliD yvyC yvyC hag hag csrA csrA fliW fliW flgK flgK flhO flhO flhP flhP flgM flgM motB motB flgB flgB
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:
fliRComponent of the flagellar export machinery; Role in flagellar biosynthesis; Belongs to the FliR/MopE/SpaR family. (259 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)
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)
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)
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)
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)
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)
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)
ylxLCoupling factor for flagellin transcription and translation; Required for swarming motility and for maximal sigma-D activity. (167 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)
flgKFlagellar hook-filament junction; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; structure. (507 aa)
flhOPutative flagellar basal-body rod protein; Not required for motility. (270 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)
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)
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)
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)
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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