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hslU protein (Pseudomonas oleovorans) - STRING interaction network
"hslU" - ATP-dependent protease ATPase subunit HslU in Pseudomonas oleovorans
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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hslUATP-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 (446 aa)    
Predicted Functional Partners:
hslV
ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery (170 aa)
  0.999
dnaK
Chaperone protein DnaK; Acts as a chaperone (638 aa)
   
   
  0.944
htpG
Chaperone protein HtpG; Molecular chaperone. Has ATPase activity (632 aa)
     
   
  0.941
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)
 
 
  0.920
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; Belongs to the ClpA/ClpB family (854 aa)
     
   
  0.920
JNHE01000009_gene3295
annotation not available (189 aa)
   
   
  0.920
JNHE01000016_gene4489
Lon 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 (778 aa)
 
 
  0.907
groL
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (533 aa)
   
   
  0.904
groS
10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (97 aa)
   
   
  0.896
ftsZ
Cell division protein FtsZ; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity (386 aa)
 
 
  0.856
Your Current Organism:
Pseudomonas oleovorans
NCBI taxonomy Id: 301
Other names: ATCC 8062, CCUG 2087, CFBP 5589, CIP 59.11, IFO 13583, JCM 11598, LMG 2229, NBRC 13583, NCIMB 6576, NCTC 10692, NRRL B-778, P. oleovorans, Pseudomonas oleovorans, Pseudomonas sp. MGY01
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