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
GroESChaperonin 10kD subunit; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (105 aa)    
Predicted Functional Partners:
groEL
Chaperonin 60kD subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.998
groEL1
Chaperonin 60kD subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.992
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- [...]
  
 
 0.953
dnaK
Heat shock protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 
 0.949
hptG
Probable chaperone heat shock protein hptG; Molecular chaperone. Has ATPase activity.
   
 
 0.919
dnaJ
Heat shock 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, [...]
 
 
 0.890
hscA
Chaperone protein; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB.
  
 
 0.880
CV_2395
Probable heat-shock protein Hsp 70; Identified by sequence similarity; putative; ORF located using Glimmer/GeneMark/Blastx/COG0443.
  
 
 0.880
hslU
Heat shock protein hslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
   
  
 0.845
hslV
Heat shock protein; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
   
  
 0.829
Your Current Organism:
Chromobacterium violaceum
NCBI taxonomy Id: 243365
Other names: C. violaceum ATCC 12472, Chromobacterium violaceum ATCC 12472, Chromobacterium violaceum ATCC12472, Chromobacterium violaceum str. ATCC 12472
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