STRINGSTRING
hslV hslV hslU hslU grpE grpE htpG htpG azo0358 azo0358 dnaJ1 dnaJ1 dnaJ2 dnaJ2 fliG fliG lon lon azo2132 azo2132 groEL1 groEL1
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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:
a 3D structure is known or predicted
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textmining
co-expression
protein homology
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hslVATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. (178 aa)    
Predicted Functional Partners:
hslU
ATP-dependent Hsl protease ATP-binding subunit; 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.
 
 0.999
grpE
Probable heat shock 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 round [...]
  
  
 0.900
htpG
Probable chaperon protein HtpG; Molecular chaperone. Has ATPase activity.
   
  
 0.897
azo0358
Putative two-component sensor kinase; Region start changed from 382943 to 383189 (246 bases).
   
  
 0.816
dnaJ1
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 [...]
   
  
 0.807
dnaJ2
Putative chaperone protein dnaJ. homology to dnaJ of E. coli of 32% (sprot|DNAJ_ECOLI) Acts as a co-chaperone. Stimulates jointly with grpE the ATPase activity of dnaK (By similarity). Pfam: DnaJ domain, DnaJ central domain (4 repeats), DnaJ Cterminal region no singal peptide no TMHs; Family membership.
   
  
 0.807
fliG
Flagellar motor switch protein fliG. FLIG IS ONE OF THREE PROTEINS (FLIG FLIN FLIM) THAT FORM A SWITCH COMPLEX THAT IS PROPOSED TO BE LOCATED AT THE BASE OF THE BASAL BODY. THIS COMPLEX INTERACTS WITH THE CHEY AND CHEZ CHEMOTAXIS PROTEINS IN ADDITION TO CONTACTING COMPONENTS OF THE MOTOR THAT DETERMINE THE DIRECTION OF FLAGELLAR ROTATION (BY SIMILARITY). fliG: flagellar motor switch protein Pfam: fliG C-terminal domain no signal peptide no TMHs; High confidence in function and specificity.
   
   0.748
lon
ATP-dependent protease La; 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.
   
  
 0.740
azo2132
Conserved hypothetical ATPase. Homology to Daro03000733 of Dechloromonas aromatica of 64% (gi|41725756|ref|ZP_00152514.1|(NBCI ENTREZ)). Domain structure: 101 aa - 293 aa AAA-protein. InterPro: AAA-protein (ATPases associated with various cellular activities) (IPR003959); AAA ATPase superfamily (IPR003593). Pfam: ATPases associated with various cellular activities. no signal peptide. no TMHS; Conserved hypothetical protein.
   
  
 0.740
groEL1
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
   
 
 0.726
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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