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hslV protein (Sulfurovum sp. NBC371) - STRING interaction network
"hslV" - ATP-dependent protease peptidase subunit in Sulfurovum sp. NBC371
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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
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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Score
hslVATP-dependent protease peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery (176 aa)    
Predicted Functional Partners:
hslU
ATP-dependent 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 (442 aa)
 
  0.999
rplI
50S ribosomal protein L9; Binds to the 23S rRNA (147 aa)
   
        0.937
dnaK
Chaperone protein DnaK; Acts as a chaperone (627 aa)
   
 
  0.801
htpG
Heat shock protein 90; Molecular chaperone. Has ATPase activity (620 aa)
   
   
  0.739
clpP
ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (195 aa)
   
 
  0.700
groS
Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (86 aa)
     
   
  0.692
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (542 aa)
     
 
  0.685
lon
ATP-dependent Lon protease; 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 (806 aa)
     
 
  0.675
SUN_1683
Oligopeptidase A (649 aa)
   
        0.667
grpE
Co-chaperone 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 AT [...] (184 aa)
     
   
  0.656
Your Current Organism:
Sulfurovum sp. NBC371
NCBI taxonomy Id: 387093
Other names: S. sp. NBC37-1, Sulfurovum, Sulfurovum Inagaki et al. 2004, Sulfurovum NBC37_1, Sulfurovum sp. NBC37-1, Sulfurovum sp. NBC371
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