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
Databases
Textmining
[Homology]
Score
bdbDThiol-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. (222 aa)    
Predicted Functional Partners:
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.
 
 
 0.999
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.
 
 
 0.940
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.
     
 0.933
stoA
Thiol-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.
  
  
 0.927
resA
Extracytoplasmic thioredoxin involved in cytochrome c maturation (lipoprotein); Thiol-disulfide oxidoreductase which is required in disulfide reduction during c-type cytochrome synthesis. May accept reducing equivalents from CcdA, leading to breakage of disulfide bonds in apocytochrome c; following this reduction heme can be covalently attached. Does not play a role in sporulation. Belongs to the thioredoxin family. ResA subfamily.
  
  
 0.921
comGC
Pilin-like component of the DNA transport membrane platform; Required for transformation and DNA binding. Belongs to the ComGC family.
      
 0.689
yneN
Putative membrane-bound proteins with a thioredoxin-like domain; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the thioredoxin family.
  
  
 0.666
resC
Factor required for cytochrome c synthesis; Required for the biogenesis of c-type cytochromes.
  
  
 0.603
trxA
Thioredoxin; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
     
 0.591
copA
Copper transporter ATPase; Involved in copper export.
 
 
 
 0.590
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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