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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groL60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (553 aa)    
Predicted Functional Partners:
groS
10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 0.998
EHA63430.1
KEGG: pmf:P9303_15251 heat shock protein 90; PFAM: ATPase-like, ATP-binding domain; Heat shock protein Hsp90, C-terminal; SMART: ATPase-like, ATP-binding domain.
   
 0.986
grpE
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-dependent i [...]
  
 0.978
dnaK-2
Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
   
 0.957
EHA60370.1
KEGG: pmf:P9303_05101 HSP70 family molecular chaperone; Belongs to the heat shock protein 70 family.
   
 0.957
dnaK
Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
   
 0.940
dnaK-3
Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
   
 0.940
groL-2
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
     
  0.920
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 [...]
   
 0.897
EHA60611.1
TIGRFAM: RNA helicase, ATP-dependent DEAH box, HrpB type; PFAM: RNA helicase, ATP-dependent, HrpB type, C-terminal; Helicase, C-terminal; Helicase-associated domain; KEGG: pmf:P9303_02411 DEAD/DEAH box helicase domain-containing protein; SMART: DEAD-like helicase, N-terminal; Helicase, C-terminal; Helicase-associated domain.
   
 0.872
Your Current Organism:
Synechococcus sp. WH 8016
NCBI taxonomy Id: 166318
Other names: S. sp. WH 8016, Synechococcus sp. WH8016
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