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.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
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Co-occurrence
Co-expression
Experiments
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[Homology]
Score
EKY22744.1Hypothetical protein; KEGG: cbe:Cbei_0830 8.2e-47 dnaK; molecular chaperone DnaK K04043; Psort location: Cytoplasmic, score: 9.97. (167 aa)    
Predicted Functional Partners:
grpE
Co-chaperone 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-depend [...]
 
 0.995
EKY22745.1
KEGG: cbe:Cbei_0830 6.8e-210 dnaK; molecular chaperone DnaK K04043; Psort location: Cytoplasmic, score: 9.97.
     0.994
groL
Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.967
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 [...]
 
 0.966
htpG
Chaperone protein HtpG; Molecular chaperone. Has ATPase activity.
  
 0.939
hrcA
Transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons.
  
  
 0.879
EKY28795.1
Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.873
EKY22743.1
Hypothetical protein.
  
 0.841
EKY29415.1
DnaJ domain protein; KEGG: tgo:TGME49_004480 8.2e-05 DnaJ domain-containing protein.
 
 0.838
EKY23482.1
Tetratricopeptide repeat protein; KEGG: ava:Ava_1552 5.1e-10 TPR repeat-containing serine/threonin protein kinase K00908; Psort location: Cytoplasmic, score: 7.50.
  
 0.819
Your Current Organism:
Clostridium celatum
NCBI taxonomy Id: 545697
Other names: C. celatum DSM 1785, Clostridium celatum DSM 1785
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