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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Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
stoAThiol-disulfide isomerase; Thiol-disulfide oxidoreductase with a reductive function, involved in spore cortex synthesis. It could be involved either in breaking disulfide bonds in cortex components or in proteins that are important for cortex synthesis, or in thiol/disulfide bond interchange. Belongs to the thioredoxin family. (165 aa)    
Predicted Functional Partners:
ccdA
Cytochrome c-type biogenesis protein CcdA; Required for cytochrome c synthesis and stage V of sporulation. Might transfer reducing equivalents across the cytoplasmic membrane, promoting efficient disulfide bond isomerization of proteins localized on the outer surface of the membrane or in the spore coat.
 
  
 0.985
bdbD
Thiol-disulfide oxidoreductase; Required for the stabilization, possibly via formation of a disulfide bond, of the obligatory competence protein ComGC. May be required for the stability of secreted proteins with disulfide bonds. Not required for sporulation.
  
  
 0.927
bdbC
Thiol-disulfide oxidoreductase; Required for the stabilization, possibly via formation of a disulfide bond, of the obligatory competence protein ComGC. Not normally required for production of the secreted lantibiotic sublancin 168, although it can partially substitute for BdbB when the latter is absent. It may also be required for the stability of other secreted proteins. Not required for sporulation; Belongs to the DsbB family. BdbC subfamily.
   
  
 0.866
spoVD
Penicillin-binding protein; Penicillin-binding protein with an unknown catalytic activity. May have a specialized role in the morphogenesis of spore cortex, which is a modified form of peptidoglycan. Pore cortex formation is determined primarily by the mother cell.
   
  
 0.779
yosR
SPbeta phage putative thiol disulfide oxidoreductase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type h: extrachromosomal origin; Belongs to the thioredoxin family.
 
 
 0.779
ykvU
Spore membrane protein involved in germination; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type m: membrane component.
  
  
 0.752
yusE
Putative thiol-disulfide oxidoreductase with thioredoxin domain; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.
  
  
 0.712
cdoA
Cysteine dioxygenase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme.
      
 0.688
ydfQ
Putative thioredoxin or thiol-disulfide isomerase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.
  
 
 0.652
bdbB
Bacteriophage SPbeta thiol-disulfide oxidoreductase; Important but not absolutely essential for the production of the lantibiotic sublancin 168, it may also be required for the stability of other secreted proteins. Not required for competence for DNA uptake; Belongs to the DsbB family. BdbC subfamily.
   
  
 0.652
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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