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DVU_1191 protein (Desulfovibrio vulgaris Hildenborough) - STRING interaction network
"DVU_1191" - Lon protease in Desulfovibrio vulgaris Hildenborough
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Predicted Interactions
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gene co-occurrence
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textmining
co-expression
protein homology
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DVU_1191Lon 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 (856 aa)    
Predicted Functional Partners:
radC
DNA repair protein RadC; Identified by similarity to SP-P25531; match to protein family HMM PF04002; match to protein family HMM TIGR00608; Belongs to the UPF0758 family (225 aa)
              0.886
acyP
Acylphosphatase; Identified by match to protein family HMM PF00708 (100 aa)
              0.853
leuS
Leucine--tRNA ligase; Identified by similarity to SP-P07813; match to protein family HMM PF00133; match to protein family HMM TIGR00396; Belongs to the class-I aminoacyl-tRNA synthetase family (829 aa)
   
   
  0.831
DVU_1194
Uncharacterized protein; Identified by Glimmer2; putative (368 aa)
              0.804
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)
     
 
  0.762
DVU_1195
annotation not available (172 aa)
              0.731
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)
 
 
  0.729
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)
 
 
  0.706
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)
   
 
  0.693
ribD
Riboflavin biosynthesis protein RibD; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5’-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)- pyrimidinedione 5’-phosphate; In the C-terminal section; belongs to the HTP reductase family (377 aa)
   
        0.692
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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