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:
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
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Score
sigOAlternative sigma factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Together with its coactivator RsoA, positively regulates the expression of at least three operons, including oxdC-yvrL, sigO-rsoA and yvrJ. Required for the acid stress-dependent induction of the oxalate decarboxylase oxdC. (176 aa)    
Predicted Functional Partners:
rsoA
Regulator of sigma-O; Together with RNA polymerase sigma factor SigO, positively regulates the expression of at least three operons, including oxdC- yvrL, sigO-rsoA and yvrJ. Required for the acid stress-dependent induction of the oxalate decarboxylase oxdC.
  
 
 0.994
yvrL
Putative integral inner membrane protein; Negatively regulates RNA polymerase sigma factor SigO- dependent transcription. Prevents the expression or secretion of OxdC under nonstress conditions. May act as an anti-sigma factor.
  
  
 0.989
oxdC
Oxalate decarboxylase; Converts oxalate to formate and CO(2) in an O(2)-dependent reaction. Can also catalyze minor side reactions: oxalate oxidation to produce H(2)O(2), and oxalate-dependent, H(2)O(2)-independent dye oxidations.
  
  
 0.850
flgM
Anti-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.
  
 
 0.841
rpoC
RNA polymerase (beta' subunit); DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
    
 
 0.824
rpoB
RNA polymerase (beta subunit); DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
    
 
 0.803
cheV
Coupling 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.
  
  
 0.796
fliY
Flagellar 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.
  
  
 0.719
flgB
Flagellar 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.
  
 
 0.718
flgC
Flagellar 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.
  
 
 0.717
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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