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. (538 aa)    
Predicted Functional Partners:
groS
Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 
 0.995
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.980
ADU47849.1
Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family.
  
 
 0.947
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 [...]
 
 0.946
groL-2
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
  
 
0.901
ADU49506.1
COGs: COG3261 Ni Fe-hydrogenase III large subunit; InterPro IPR001268: IPR020396; KEGG: tcu:Tcur_4707 NADH dehydrogenase (ubiquinone) 30 kDa subunit; PFAM: NADH dehydrogenase (ubiquinone) 30 kDa subunit; SPTR: NADH dehydrogenase (Ubiquinone) 30 kDa subunit; PFAM: Respiratory-chain NADH dehydrogenase, 30 Kd subunit; Respiratory-chain NADH dehydrogenase, 49 Kd subunit; Nickel-dependent hydrogenase.
    
   0.883
dnaJ
Chaperone DnaJ domain protein; 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 [...]
 
 0.832
ADU49780.1
COGs: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; InterProIPR018260: IPR018253: IPR001623: IPR003095: IPR 002939; KEGG: kra:Krad_4231 chaperone DnaJ domain protein; PFAM: chaperone DnaJ domain protein; heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; SPTR: DnaJ protein; PFAM: DnaJ C terminal region; DnaJ domain.
 
 0.831
ADU48984.1
COGs: COG0567 2-oxoglutarate dehydrogenase complex dehydrogenase (E1); InterProIPR011603: IPR001078: IPR001017: IPR005475: IPR 000897; KEGG: kra:Krad_1228 alpha-ketoglutarate decarboxylase; PFAM: Transketolase central region; dehydrogenase E1 component; catalytic domain-containing protein of components of various dehydrogenase complexes; SPTR: Alpha-ketoglutarate decarboxylase; TIGRFAM: 2-oxoglutarate dehydrogenase, E1 subunit; PFAM: 2-oxoacid dehydrogenases acyltransferase (catalytic domain); Dehydrogenase E1 component; Transketolase, pyrimidine binding domain; TIGRFAM: 2-oxoglutarate [...]
   
 0.779
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.
  
 
 0.754
Your Current Organism:
Intrasporangium calvum
NCBI taxonomy Id: 710696
Other names: I. calvum DSM 43043, Intrasporangium calvum DSM 43043, Intrasporangium calvum IFO 12989, Intrasporangium calvum NBRC 12989, Intrasporangium calvum str. DSM 43043, Intrasporangium calvum strain DSM 43043
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