STRINGSTRING
STRING protein interaction network
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:
some 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 each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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[Homology]
Score
hagFlagellin; 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 flagellin, whic [...] (304 aa)    
Predicted Functional Partners:
fliS
Flagellar secretion chaperone FliS; Essential for filament assembly. May act as a facilitator of flagellin (hag) secretion. Antagonizes translational repressor CsrA indirectly; Belongs to the FliS family
 
 
 0.998
flgK
Flagellar hook-associated protein 1; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type s : structure
 
 
 0.998
fliD
Flagellar hook-associated protein 2; 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
 
 
 0.990
fliW
Flagellar assembly factor FliW; 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 assem [...]
 
 
 
 0.990
sigD
RNA polymerase sigma-D factor; 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
  
 0.983
flhA
Flagellar biosynthesis protein FlhA; Involved in the export of flagellum proteins
 
 
 0.981
csrA
Translational regulator CsrA; 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. Repre [...]
 
 
 
 0.976
fliM
Flagellar motor switch protein FliM; 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
 
  
 0.967
flgM
Negative regulator of flagellin synthesis; Allows the coupling of early and late flagellar synthesis through the repression of RNA polymerase sigma-D factor- dependent transcription
  
  
 0.965
flgE
Flagellar basal-body rod protein FlgG; 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
 
 
 0.964
Your Current Organism:
Bacillus subtilis
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis, Bacillus subtilis 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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