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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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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groLChaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (547 aa)    
Predicted Functional Partners:
groS
Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 0.998
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.979
grpE
GrpE 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-dependent i [...]
 
 0.948
Daud_0921
TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: pca:Pcar_3068 thioredoxin; Belongs to the thioredoxin family.
   
 
 0.808
Daud_0453
PFAM: heat shock protein DnaJ domain protein; chaperone DnaJ domain protein; KEGG: pen:PSEEN4896 curved DNA-binding protein.
 
 0.786
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 [...]
 
 0.785
Daud_1736
CheC, inhibitor of MCP methylation; PFAM: surface presentation of antigens (SPOA) protein; CheC domain protein; KEGG: mta:Moth_0805 CheC, inhibitor of MCP methylation.
    
   0.743
hslU
Heat shock protein HslVU, ATPase subunit HslU; 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.
   
  
 0.735
nnrD
Carbohydrate kinase, YjeF related protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow t [...]
  
   0.733
metK
Methionine adenosyltransferase; Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
   
 
 0.727
Your Current Organism:
Desulforudis audaxviator
NCBI taxonomy Id: 477974
Other names: C. Desulforudis audaxviator MP104C, Candidatus Desulforudis audaxviator MP104C, Candidatus Desulforudis audaxviator str. MP104C, Candidatus Desulforudis audaxviator strain MP104C
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