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clpA protein (Desulfovibrio vulgaris Hildenborough) - STRING interaction network
"clpA" - ATP-dependent Clp protease, ATP-binding subunit ClpA 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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clpAATP-dependent Clp protease, ATP-binding subunit ClpA; Identified by similarity to SP-P15716; match to protein family HMM PF00004; match to protein family HMM PF02861 (776 aa)    
Predicted Functional Partners:
clpS
ATP-dependent Clp protease adapter protein ClpS; Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation (104 aa)
 
  0.996
aat
Leucyl/phenylalanyl-tRNA--protein transferase; Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine (234 aa)
 
 
 
  0.954
dnaK
Chaperone protein DnaK; Acts as a chaperone (636 aa)
 
 
  0.925
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)
 
 
  0.921
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)
   
 
  0.919
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 (201 aa)
   
 
  0.876
groEL
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (547 aa)
   
 
  0.798
htpG
Chaperone protein HtpG; Molecular chaperone. Has ATPase activity; Belongs to the heat shock protein 90 family (637 aa)
   
 
  0.794
guaA
GMP synthase [glutamine-hydrolyzing]; Catalyzes the synthesis of GMP from XMP (515 aa)
 
   
  0.778
DVU_1876
DnaJ protein, putative; Identified by similarity to SP-P08622; match to protein family HMM PF00226; match to protein family HMM PF01556 (316 aa)
 
 
  0.778
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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