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hslV protein (Desulfovibrio vulgaris Hildenborough) - STRING interaction network
"hslV" - ATP-dependent protease subunit HslV in Desulfovibrio vulgaris Hildenborough
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Known Interactions
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experimentally determined
Predicted Interactions
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gene co-occurrence
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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 (181 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 (441 aa)
  0.999
dnaK
Chaperone protein DnaK; Acts as a chaperone (636 aa)
   
 
  0.905
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 [...] (191 aa)
     
   
  0.882
ispE
4-diphosphocytidyl-2-C-methyl-D-erythritol kinase; Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol (286 aa)
   
        0.865
htpG
Chaperone protein HtpG; Molecular chaperone. Has ATPase activity; Belongs to the heat shock protein 90 family (637 aa)
     
   
  0.836
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 [...] (376 aa)
     
   
  0.829
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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity); Belongs to the ClpA/ClpB family (865 aa)
     
   
  0.781
sucCD
Succinate--CoA ligase [ADP-forming] subunit alpha; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit (709 aa)
   
   
  0.766
groES
10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (95 aa)
     
   
  0.753
rplI
50S ribosomal protein L9; Binds to the 23S rRNA (167 aa)
   
        0.749
Your Current Organism:
Desulfovibrio vulgaris Hildenborough
NCBI taxonomy Id: 882
Other names: D. vulgaris str. Hildenborough, Desulfovibrio vulgaris (STRAIN HILDENBOROUGH), Desulfovibrio vulgaris ATCC 29579, Desulfovibrio vulgaris Hildenborough, Desulfovibrio vulgaris str. Hildenborough, Desulfovibrio vulgaris subsp. vulgaris (strain Hildenborough), Desulfovibrio vulgaris subsp. vulgaris ATCC 29579, Desulfovibrio vulgaris subsp. vulgaris str. Hildenborough
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