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
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[Homology]
Score
BVIR_92Chaperone protein DnaJ. (206 aa)    
Predicted Functional Partners:
dnaK_1
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
 0.895
hoxF
NAD-reducing hydrogenase HoxS subunit alpha.
   
  0.890
grpE
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-dependent i [...]
  
 
 0.881
htpG
Chaperone protein HtpG; Molecular chaperone. Has ATPase activity.
  
 0.852
cobT
Aerobic cobaltochelatase subunit CobT.
 
     0.851
dnaK_2
Chaperone protein DnaK.
  
 0.843
lgrD_1
Carboxylic acid reductase.
   
 0.794
cobS-2
Aerobic cobaltochelatase subunit CobS.
 
     0.750
groL3
60 kDa chaperonin 3; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
 0.714
groL_1
60 kDa chaperonin 7; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
 0.714
Your Current Organism:
Blastochloris viridis
NCBI taxonomy Id: 1079
Other names: ATCC 19567, B. viridis, CCUG 30818, CCUG 7830, DSM 133, LMG 4321, LMG:4321, NBRC 102659, Rhodopseudomonas viridis, strain G. Drews F
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