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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gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
groLChaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (543 aa)    
Predicted Functional Partners:
groS
Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 
 0.999
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.992
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 [...]
 
 0.986
Ccel_0492
PFAM: heat shock protein Hsp90; ATP-binding region ATPase domain protein; KEGG: cth:Cthe_0550 heat shock protein 90.
   
 
 0.970
Ccel_2211
TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: cth:Cthe_0360 thioredoxin; Belongs to the thioredoxin family.
 
 
 0.908
lon
ATP-dependent protease La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
  
 0.908
Ccel_1687
PFAM: NADH dehydrogenase (ubiquinone) 30 kDa subunit; KEGG: rci:RCIX2383 hydrogenase, large subunit-like protein (HycE-like).
    
   0.899
Ccel_2038
CheC, inhibitor of MCP methylation / FliN fusion protein; TIGRFAM: flagellar motor switch protein FliN; PFAM: surface presentation of antigens (SPOA) protein; CheC domain protein; KEGG: cth:Cthe_0478 flagellar motor switch protein.
   
   0.861
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 [...]
 
 0.844
Ccel_2331
TIGRFAM: amino acid adenylation domain protein; PFAM: AMP-dependent synthetase and ligase; condensation domain protein; short-chain dehydrogenase/reductase SDR; phosphopantetheine-binding; KR domain protein; Beta-ketoacyl synthase; KEGG: bsu:BSU17180 polyketide synthase of type I.
  
 
 0.832
Your Current Organism:
Ruminiclostridium cellulolyticum
NCBI taxonomy Id: 394503
Other names: Clostridium cellulolyticum H10, R. cellulolyticum H10, Ruminiclostridium cellulolyticum H10
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