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hslV protein (Nitrosomonas eutropha) - STRING interaction network
"hslV" - ATP-dependent protease subunit HslV in Nitrosomonas eutropha
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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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hslVATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery (173 aa)    
Predicted Functional Partners:
hslU
ATP-dependent protease 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 (443 aa)
  0.999
dnaK
Chaperone protein DnaK; Acts as a chaperone (647 aa)
   
 
  0.930
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 [...] (196 aa)
     
   
  0.903
htpG
Chaperone protein HtpG; Molecular chaperone. Has ATPase activity (640 aa)
     
   
  0.837
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 [...] (369 aa)
     
   
  0.781
clpB
Chaperone protein ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family (863 aa)
     
   
  0.760
groS
10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (96 aa)
     
   
  0.748
Neut_0610
KEGG- neu-NE2262 beta-ketothiolase; TIGRFAM- acetyl-CoA acetyltransferases; PFAM- Thiolase; Belongs to the thiolase family (392 aa)
   
        0.741
rplI
50S ribosomal protein L9; Binds to the 23S rRNA (151 aa)
   
        0.731
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; Belongs to the peptidase S14 family (214 aa)
   
   
  0.674
Your Current Organism:
Nitrosomonas eutropha
NCBI taxonomy Id: 335283
Other names: N. eutropha C91, Nitrosomonas eutropha, Nitrosomonas eutropha C91, Nitrosomonas eutropha str. C91, Nitrosomonas eutropha strain C91
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