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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grpEHeat 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. Several rounds of ATP-depen [...] (194 aa)    
Predicted Functional Partners:
dnaJ
Chaperone Hsp40/DnaJ, co-chaperone with DnaK; 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 intera [...]
 
 
 0.997
groL
Cpn60 chaperonin GroEL, large subunit of GroESL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.993
groS
Cpn10 chaperonin GroES, small subunit of GroESL; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.991
dnaK
Chaperone Hsp70/DnaK, co-chaperone with DnaJ; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.991
dnaK1
Chaperone, DnaK-like protein; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.989
hslU
Molecular chaperone and ATPase component of HslUV protease; 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.
 
  
 0.973
hslV
Peptidase component of the HslUV protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
  
  
 0.965
VF_1108
Chaperone protein DnaJ-like protein.
 
 
 0.952
htpG
Molecular chaperone HSP90 family; Molecular chaperone. Has ATPase activity.
 
 
 0.948
clpB
Protein disaggregation chaperone; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family.
  
 
 0.929
Your Current Organism:
Aliivibrio fischeri
NCBI taxonomy Id: 312309
Other names: A. fischeri ES114, Aliivibrio fischeri ES114, Vibrio fischeri ES114, Vibrio fischeri str. ES114, Vibrio fischeri strain ES114
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