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
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Cooccurrence
Coexpression
Experiments
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Textmining
[Homology]
Score
VC_2418Thiol:disulfide interchange protein DsbC; Required for disulfide bond formation in some periplasmic proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process; Belongs to the thioredoxin family. DsbC subfamily. (250 aa)    
Predicted Functional Partners:
dsbD
Thiol:disulfide interchange protein DsbD; Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps (By similarity); Belongs to the thioredoxin family. DsbD subfamily.
  
 
 0.938
dsbB
Disulfide bond formation protein B; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family.
 
 
 0.898
xerD
Integrase/recombinase XerD; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids (By similarity). Belongs to the 'phage' integrase family. XerD subfamily.
  
  
 0.843
VC_2417
single-stranded-DNA-specific exonuclease RecJ; Similar to GB:M54884 SP:P21893 PID:147550 PID:887842 GB:U00096; identified by sequence similarity; putative.
     
 0.838
dsbA
Thiol:disulfide interchange protein; Involved in disulfide-bond formation. Required for the functional maturation of secreted virulence factors. Acts by transferring its disulfide bond to other proteins; Belongs to the thioredoxin family. DsbA subfamily.
  
  
 0.800
VC_2420
Flavodoxin 2; Low-potential electron donor to a number of redox enzymes. Belongs to the flavodoxin family.
       0.742
dsbE
Thiol:disulfide interchange protein DsbE; Involved in disulfide bond formation. Catalyzes a late, reductive step in the assembly of periplasmic c-type cytochromes, probably the reduction of disulfide bonds of the apocytochrome c to allow covalent linkage with the heme. Possible subunit of a heme lyase (By similarity); Belongs to the thioredoxin family. DsbE subfamily.
 
 
 0.690
VC_0559
Conserved hypothetical protein; Identified by Glimmer2; putative.
 
     0.664
VC_0761
Conserved hypothetical protein; Identified by Glimmer2; putative.
  
    0.655
VC_0577
Stringent starvation protein B; Similar to GB:M69028 SP:P25663 GB:X05088 PID:147872 PID:42999; identified by sequence similarity; putative.
  
     0.625
Your Current Organism:
Vibrio cholerae
NCBI taxonomy Id: 243277
Other names: V. cholerae O1 biovar El Tor str. N16961, Vibrio cholerae El Tor N16961, Vibrio cholerae O1 biovar El Tor str. N16961, Vibrio cholerae O1 biovar eltor str. N16961, Vibrio cholerae serotype O1 biotype El Tor strain N16961, Vibrio cholerae serotype O1 biotype ElTor strain N16961
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.