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
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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.
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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
groESCo-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (96 aa)    
Predicted Functional Partners:
groEL
COG0459 Chaperonin GroEL (HSP60 family).
 
 
 0.999
dnaK
COG0443 Molecular chaperone.
 
 
 0.989
grpE
Molecular chaperone GrpE (heat shock 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. [...]
 
 
 0.985
hslU
ATP-dependent protease ATP-binding subunit; 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.
   
  
 0.939
EAQ31200.1
COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain.
 
 
 0.935
EAQ31474.1
Heat shock protein 90; COG0326 Molecular chaperone, HSP90 family.
   
 
 0.923
hslV
ATP-dependent protease HslVU (ClpYQ), peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
   
  
 0.918
clpP
Protease subunit of ATP-dependent Clp protease; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family.
 
 
 0.900
EAQ31081.1
NifS; COG1104 Cysteine sulfinate desulfinase/cysteine desulfurase and related enzymes.
 
 
 0.880
dsbD
COG4232 Thiol:disulfide interchange protein.
     
 0.821
Your Current Organism:
Idiomarina baltica
NCBI taxonomy Id: 314276
Other names: I. baltica OS145, Idiomarina baltica OS145, Idiomarina baltica str. OS145, Idiomarina baltica strain OS145
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