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
KOH22462.1Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology. (206 aa)    
Predicted Functional Partners:
KOH21405.1
Heat shock protein 90; Molecular chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.975
grpE
Heat shock protein GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP- [...]
  
 
 0.946
hscA
Chaperone protein HscA; Involved in the maturation of iron-sulfur cluster-containing proteins; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.939
KOH22279.1
Chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.939
dnaK
Molecular chaperone DnaK; Heat shock protein 70; assists in folding of nascent polypeptide chains; refolding of misfolded proteins; utilizes ATPase activity to help fold; co-chaperones are DnaJ and GrpE; multiple copies in some bacteria; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.939
prmA
Methylates ribosomal protein L11 at multiple amino acid positions; mutations of these genes in Escherichia coli or Thermus thermophilus has no apparent phenotype; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.829
rplQ
50S ribosomal protein L17; Is a component of the macrolide binding site in the peptidyl transferase center; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
   0.810
rplM
50S ribosomal protein L13; This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.
  
 
 0.807
KOH17473.1
CoA-disulfide reductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.803
rplK
50S ribosomal protein L11; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
   
 
 0.801
Your Current Organism:
Vibrio parahaemolyticus
NCBI taxonomy Id: 670
Other names: ATCC 17802, Beneckea parahaemolytica, CAIM 320, CCUG 14474, CCUG 15657, CCUG 4224, CIP 75.2, DSM 10027, IFO 12711, LMG 2850, LMG:2850, NBRC 12711, NCCB 77010, NCCB 77018, NCTC 10903, NRRL B-4167, Oceanomonas parahaemolytica, Pasteurella parahaemolytica, V. parahaemolyticus
Server load: low (22%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.