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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hslVATP-dependent protease hslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. (183 aa)    
Predicted Functional Partners:
hslU
ATP-dependent hsl protease ATP-binding 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
grpE
Protein 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-dependent i [...]
   
  
 0.895
groS
10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
   
  
 0.849
groL
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
   
 
 0.798
lon
Anti-sigma H sporulation factor, LonB; 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.
   
  
 0.668
lon-2
Anti-sigma H sporulation factor, LonB; 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.
   
  
 0.668
hslO
33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
  
  
 0.644
dnaK
Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
  
 0.639
AEH22235.1
Thioredoxin; KEGG: dbr:Deba_1136 thioredoxin; TIGRFAM: Thioredoxin; PFAM: Thioredoxin domain; Belongs to the thioredoxin family.
  
  
 0.616
AEH23103.1
PFAM: Heat shock protein Hsp20; KEGG: ddf:DEFDS_1576 heat shock protein Hsp20; Belongs to the small heat shock protein (HSP20) family.
   
  
 0.616
Your Current Organism:
Thermodesulfobacterium geofontis
NCBI taxonomy Id: 795359
Other names: T. geofontis OPF15, Thermodesulfobacterium geofontis OPF15, Thermodesulfobacterium sp. OPF15
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