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hslV hslV hslU hslU grpE grpE dnaK dnaK htpG htpG dnaJ dnaJ trx trx lon lon ACS40420.1 ACS40420.1 groL groL groL-2 groL-2
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
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a 3D structure is known or predicted
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textmining
co-expression
protein homology
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hslVATP-dependent protease hslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. (186 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
Putative heat shock protein (HSP-70 COFACTOR), 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 c [...]
  
  
 0.868
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
  
 0.867
htpG
Chaperone Hsp90, heat shock protein C 62.5; Molecular chaperone. Has ATPase activity.
   
  
 0.865
dnaJ
Heat shock protein (Hsp40), co-chaperone with DnaK; 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 [...]
   
  
 0.862
trx
Thioredoxin; Function of strongly homologous gene; carrier.
  
  
 0.860
lon
ATP-dependent protease La (Lon); 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.
   
  
 0.851
ACS40420.1
Hypothetical protein; No homology to any previously reported sequences.
   
  
 0.829
groL
60 kDa chaperonin (protein Cpn60, groEL protein); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
   
 
 0.829
groL-2
60 kDa chaperonin (protein Cpn60, groEL protein); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
   
 
 0.829
Your Current Organism:
Methylorubrum extorquens
NCBI taxonomy Id: 272630
Other names: M. extorquens AM1, Methylobacterium extorquens AM1, Methylorubrum extorquens AM1, Pseudomonas sp. AM1
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