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.
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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
dnaKChaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (646 aa)    
Predicted Functional Partners:
dnaJ
Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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 interactions between DnaJ, D [...]
 0.999
grpE
GrpE protein; 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 [...]
 
 0.994
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.988
groS
Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 
 0.974
Rvan_0203
KEGG: sme:SMa0116 DnaJ/CbpA-type protein; PFAM: chaperone DnaJ domain protein; heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein.
 0.973
Rvan_1483
KEGG: sfu:Sfum_3853 hypothetical protein.
  
 0.972
Rvan_1941
KEGG: pzu:PHZ_p0115 heat shock protein DnaJ, N-terminal; PFAM: heat shock protein DnaJ domain protein; chaperone DnaJ domain protein; SMART: heat shock protein DnaJ domain protein.
 0.967
Rvan_2934
KEGG: reu:Reut_A0922 hypothetical protein; PFAM: protein of unknown function DUF323; heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein.
 
 0.939
Rvan_1702
KEGG: pla:Plav_2408 heat shock protein DnaJ domain-containing protein; PFAM: heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein.
  
 0.937
Rvan_1039
PFAM: nitrogen-fixing NifU domain protein; KEGG: azc:AZC_0943 NifU-like protein.
  
 0.934
Your Current Organism:
Rhodomicrobium vannielii
NCBI taxonomy Id: 648757
Other names: R. vannielii ATCC 17100, Rhodomicrobium vannielii ATCC 17100, Rhodomicrobium vannielii NCIMB 10020, Rhodomicrobium vannielii str. ATCC 17100, Rhodomicrobium vannielii strain ATCC 17100
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