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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experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
gene fusions
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grpEMolecular 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. [...] (483 aa)    
Predicted Functional Partners:
dnaK
Chaperone protein DnaK; Acts as a chaperone.
 
 0.999
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 [...]
 
 
 0.995
AGB16033.1
DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain.
 
 
 0.904
AGB14794.1
Thermosome subunit; PFAM: TCP-1/cpn60 chaperonin family; TIGRFAM: thermosome, various subunits, archaeal.
  
 0.900
AGB15855.1
PFAM: TCP-1/cpn60 chaperonin family; TIGRFAM: thermosome, various subunits, archaeal.
  
 0.900
AGB17241.1
Thermosome subunit; PFAM: TCP-1/cpn60 chaperonin family; TIGRFAM: thermosome, various subunits, archaeal.
  
 0.900
AGB15950.1
DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain.
 
 
 0.896
AGB16309.1
DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain.
  
 
 0.860
AGB16881.1
Lon-related putative ATP-dependent protease; PFAM: Magnesium chelatase, subunit ChlI; Sigma-54 interaction domain; Lon protease (S16) C-terminal proteolytic domain; TIGRFAM: lon-related putative ATP-dependent protease; Belongs to the peptidase S16 family.
  
  
 0.837
AGB17274.1
Molecular chaperone (small heat shock protein); PFAM: Hsp20/alpha crystallin family; Belongs to the small heat shock protein (HSP20) family.
 
 
 0.723
Your Current Organism:
Halovivax ruber
NCBI taxonomy Id: 797302
Other names: H. ruber XH-70, Halovivax ruber JCM 13892, Halovivax ruber XH-70, Halovivax ruber str. XH-70, Halovivax ruber strain XH-70
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