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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grpECo-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 [...] (183 aa)    
Predicted Functional Partners:
groS
Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 
 0.999
groL
Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.999
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.
  
  
 0.999
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.999
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 [...]
 
 
 0.999
rph
tRNA nucleotidyltransferase; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
 
 
 0.998
D920_00538
Riboflavin biosynthesis protein RibD; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'- phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'- phosphate; In the C-terminal section; belongs to the HTP reductase family.
  
  
 0.997
D920_01950
Putative oxygen-independent coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family.
     
 0.996
polA
DNA-directed DNA polymerase; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
  
  
 0.995
D920_01543
Hsp20/alpha crystallin family protein; KEGG: apb:SAR116_0129 1.0e-07 molecular chaperone K13993; Psort location: Cellwall, score: 8.19; Belongs to the small heat shock protein (HSP20) family.
  
 
 0.993
Your Current Organism:
Enterococcus faecalis 13SDW01
NCBI taxonomy Id: 1260356
Other names: E. faecalis 13-SD-W-01, Enterococcus faecalis 13-SD-W-01
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