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DVU_3303 protein (Desulfovibrio vulgaris Hildenborough) - STRING interaction network
"DVU_3303" - Endopeptidase La in Desulfovibrio vulgaris Hildenborough
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second shell of interactors
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proteins of unknown 3D structure
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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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DVU_3303Endopeptidase La; Identified by match to protein family HMM PF00004; match to protein family HMM PF00072; match to protein family HMM PF05362; Belongs to the peptidase S16 family (702 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)
 
 
  0.701
DVU_3302
Uncharacterized protein; Identified by Glimmer2; putative (108 aa)
         
  0.697
clpX
ATP-dependent Clp protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (417 aa)
 
 
  0.669
ftsH
ATP-dependent zinc metalloprotease FtsH; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family (656 aa)
 
 
  0.669
hslV
ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery (181 aa)
     
 
  0.646
htpG
Chaperone protein HtpG; Molecular chaperone. Has ATPase activity; Belongs to the heat shock protein 90 family (637 aa)
   
   
  0.624
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)
   
 
  0.599
rrmJ
Ribosomal RNA large subunit methyltransferase E; Specifically methylates the uridine in position 2552 of 23S rRNA at the 2’-O position of the ribose in the fully assembled 50S ribosomal subunit (204 aa)
   
      0.593
DVU_3298
Uncharacterized protein; Identified by Glimmer2; putative (260 aa)
         
  0.586
DVU_3301
Uncharacterized protein; Identified by Glimmer2; putative (180 aa)
              0.578
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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