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
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.
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from curated databases
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experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
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groLChaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (542 aa)    
Predicted Functional Partners:
groS
Chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 0.999
dnaK
Chaperone dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.997
htpG
Hypothetical protein; Molecular chaperone. Has ATPase activity.
   
 0.989
grpE
Hypothetical 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-dep [...]
 
 0.973
dnaJ
Chaperone 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, DnaK and [...]
 
 0.956
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.
  
 
 0.926
EHO85959.1
Thioredoxin; Belongs to the thioredoxin family.
  
 
 0.908
EHO86798.1
Hypothetical protein.
  
 0.906
EHO86337.1
Hypothetical protein.
  
 0.906
ftsH
Hypothetical protein; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family.
   
 0.905
Your Current Organism:
Eubacterium infirmum
NCBI taxonomy Id: 883109
Other names: E. infirmum F0142, Eubacterium infirmum F0142
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