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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
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[Homology]
Score
spoIIPSpore autolysin (stage II sporulation); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type cp: cell process. (401 aa)    
Predicted Functional Partners:
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.
  
  
 0.994
spoIID
Autolysin required for complete dissolution of the asymmetric septum (stage II sporulation); May act at the level of sigma-G activity or its stability. SpoIID is probably required for engulfment.
  
  
 0.993
spoIIIAH
Stage III sporulation ratchet engulfment protein; Involved in forespore engulfment. Forms a channel with SpoIIIAH that is open on the forespore end and closed (or gated) on the mother cell end. This allows sigma-E-directed gene expression in the mother-cell compartment of the sporangium to trigger the activation of sigma-G forespore-specific gene expression by a pathway of intercellular signaling.
  
  
 0.976
spoIIQ
Forespore protein required for alternative engulfment; Involved in forespore engulfment and required for anchoring membrane proteins on the forespore side of the septal membrane. Forms a channel with SpoIIIAH that is open on the forespore end and closed (or gated) on the mother cell end. This allows sigma-E-directed gene expression in the mother-cell compartment of the sporangium to trigger the activation of sigma-G forespore-specific gene expression by a pathway of intercellular signaling.
  
  
 0.972
gpr
Spore endopeptidase; Initiates the degradation of small, acid-soluble proteins during spore germination.
 
  
 0.967
spoIIR
pro-sigma(E) endopeptidase (stage II sporulation); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme.
  
  
 0.959
spoIVA
Morphogenetic stage IV sporulation protein; ATPase. Has a role at an early stage in the morphogenesis of the spore coat outer layers. Its ATP hydrolysis is required for proper assembly of the spore coat. Forms a basement layer around the outside surface of the forespore and self-assembles irreversibly into higher order structures by binding and hydrolyzing ATP thus creating a durable and stable platform upon which thereafter morphogenesis of the coat can take place. Required for proper localization of spore coat protein CotE and sporulation-specific proteins including SpoVM.
 
  
 0.948
spoIIIAG
Stage III sporulation engulfment assembly protein; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type cp: cell process.
  
  
 0.945
yqxA
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function.
  
  
 0.944
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.
  
   
 0.938
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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