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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[Homology]
Score
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)    
Predicted Functional Partners:
rsbP
Serine phosphatase; Positive regulator of sigma-B activity. Dephosphorylates RsbV in response to energy stress.
 
  
 0.998
rsbT
Switch 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 [...]
  
  
 0.929
ydeN
Alpha/beta hydrolase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the RBBP9 family.
      
 0.919
rsbV
Anti-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.
   
  
 0.901
rsbW
Switch 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).
   
  
 0.895
rsbU
Serine phosphatase; Positive regulator of sigma-B activity. Dephosphorylates RsbV in response to environmental stress conveyed from the RsbXST module.
   
  
 0.884
rsbS
Antagonist 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.
  
  
 0.868
rsbRA
Component 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.
  
  
 0.866
pksJ
Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism.
  
 
 0.799
rsbRC
Component of the piezosome (stressosome); One of 4 functionally non-identical RsbR paralogs, it functions in the environmental signaling branch of the general stress response.
   
  
 0.756
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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