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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from curated databases
textmining
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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
hslVATP dependent peptidase CodWX, CodW component; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. (179 aa)    
Predicted Functional Partners:
hslU
Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
 0.999
ADW17097.1
GrpE protein; COGs: COG0576 Molecular chaperone GrpE (heat shock protein); InterPro IPR000740; KEGG: dak:DaAHT2_0057 GrpE protein; PFAM: GrpE protein; SPTR: Protein grpE; PFAM: GrpE.
  
  
 0.915
ADW18122.1
COGs: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; InterProIPR003095: IPR012724: IPR018253: IPR001623: IPR 001305: IPR002939; KEGG: dps:DP1482 chaperone protein DnaJ; PFAM: chaperone DnaJ domain protein; heat shock protein DnaJ domain protein; DnaJ central domain protein; SMART: heat shock protein DnaJ domain protein; SPTR: Chaperone protein dnaJ; TIGRFAM: chaperone protein DnaJ; PFAM: DnaJ domain; DnaJ central domain (4 repeats); DnaJ C terminal region; TIGRFAM: chaperone protein DnaJ.
   
  
 0.908
htpG
Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity.
   
  
 0.907
groS
Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
   
  
 0.887
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
   
 
 0.880
ADW17196.1
KEGG: tau:Tola_0702 hypothetical protein; SPTR: Putative uncharacterized protein.
   
  
 0.843
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
  
 0.833
ADW18962.1
COGs: COG1188 Ribosome-associated heat shock protein implicated in the recycling of the 50S subunit (S4 paralog); InterPro IPR002942; KEGG: tkm:TK90_2048 RNA-binding S4 domain protein; PFAM: RNA-binding S4 domain protein; SMART: RNA-binding S4 domain protein; SPTR: RNA-binding S4 domain protein; PFAM: S4 domain.
  
    0.808
lon
ATP-dependent proteinase; 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.
   
  
 0.792
Your Current Organism:
Desulfobulbus propionicus
NCBI taxonomy Id: 577650
Other names: D. propionicus DSM 2032, Desulfobulbus propionicus DSM 2032, Desulfobulbus propionicus str. DSM 2032, Desulfobulbus propionicus strain DSM 2032
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