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
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
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Textmining
[Homology]
Score
spoIIRpro-sigma(E) endopeptidase (stage II sporulation); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (224 aa)    
Predicted Functional Partners:
spoIIGA
Protease processing pro-sigma-E; Probable aspartic protease that is responsible for the proteolytic cleavage of the RNA polymerase sigma E factor (SigE/spoIIGB) to yield the active peptide in the mother cell during sporulation. Responds to a signal from the forespore that is triggered by the extracellular signal protein SpoIIR. Belongs to the peptidase U4 family.
 
   
 0.994
spoIIAB
Anti-sigma factor (antagonist of sigma(F)) and serine kinase; Binds to sigma F and blocks its ability to form an RNA polymerase holoenzyme (E-sigma F). Phosphorylates SpoIIAA on a serine residue. This phosphorylation may enable SpoIIAA to act as an anti- anti-sigma factor that counteracts SpoIIAB and thus releases sigma F from inhibition.
  
   
 0.977
spoIIE
SpoIIAA-phosphate serine phosphatase; Normally needed for pro-sigma E processing during sporulation but can be bypassed in vegetative cells. Activates SpoIIAA by dephosphorylation.
  
  
 0.970
spoIIP
Spore autolysin (stage II sporulation); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type cp: cell process.
  
  
 0.961
spoIIID
Transcriptional regulator; This protein regulates the transcription of sigK, which encodes mother cell chamber RNA polymerase sigma-factor (sigma K).
  
  
 0.952
spo0A
Response regulator; May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with Spo0H (a sigma factor) to control the expression of some genes that are critical to the sporulation process. Repressor of abrB, activator of the spoIIa operon. Binds the DNA sequence 5'-TGNCGAA-3' (0A box).
  
   
 0.931
spoIIAA
Anti-anti-sigma factor (antagonist of SpoIIAB); In the phosphorylated form it could act as an anti-anti-sigma factor that counteracts SpoIIAB and thus releases sigma f from inhibition; Belongs to the anti-sigma-factor antagonist family.
  
   
 0.930
spoIVB
Regulatory membrane-associated serine protease; Plays a central role in the sigma-K checkpoint which coordinates gene expression during the later stages of spore formation. The protease is activated by trans cleavage of the zymogen precursor producing SpoIVB-45 kDa. This undergoes further trimming by cis cleavage to form SpoIVB-43 kDa and SpoIVB-42 kDa. The protease then cleaves the C-terminus of the SpoIVFA metalloprotease activating the latter.
  
  
 0.925
spoIIIAA
ATP-binding stage III sporulation protein; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type cp: cell process.
  
  
 0.918
spoIIM
Autolysin component for dissolution of the septal cell wall (stage II sporulation); Required for complete septum migration and engulfment of the forespore compartment during sporulation. Required for stabilizing and recruiting of SpoIIP to the septal membrane.
  
  
 0.906
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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