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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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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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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EIC29777.1Molecular chaperone; PFAM: DNA-K related protein; Hsp70 protein. (918 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 [...]
  
 0.974
htpG
Molecular chaperone of HSP90 family; Molecular chaperone. Has ATPase activity.
   
 0.967
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. [...]
  
 0.966
groL
Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
 0.957
groS
Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.924
EIC29258.1
DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ C terminal region; DnaJ domain.
   
 0.916
EIC28996.1
PFAM: NifU-like N terminal domain; TIGRFAM: SUF system FeS assembly protein, NifU family.
  
 0.884
EIC30823.1
DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain.
   
 0.876
clpB
ATP-dependent chaperone ClpB; 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.
   
 
 0.862
EIC28580.1
ATP-dependent Clp protease ATP-binding subunit clpA; PFAM: AAA domain (Cdc48 subfamily); C-terminal, D2-small domain, of ClpB protein; Clp amino terminal domain; ATPase family associated with various cellular activities (AAA); TIGRFAM: ATP-dependent Clp protease ATP-binding subunit clpA; Belongs to the ClpA/ClpB family.
   
 
 0.862
Your Current Organism:
Methylomicrobium album
NCBI taxonomy Id: 686340
Other names: M. album BG8, Methylomicrobium album BG8, Methylomicrobium album str. BG8, Methylomicrobium album strain BG8
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