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clpB protein (Pseudomonas oleovorans) - STRING interaction network
"clpB" - Chaperone protein ClpB in Pseudomonas oleovorans
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second shell of interactors
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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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clpBChaperone 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)    
Predicted Functional Partners:
dnaK
Chaperone protein DnaK; Acts as a chaperone (638 aa)
 
 
  0.990
JNHE01000009_gene3295
annotation not available (189 aa)
 
 
  0.990
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)
 
  0.977
groL
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (533 aa)
 
   
  0.959
htpG
Chaperone protein HtpG; Molecular chaperone. Has ATPase activity (632 aa)
   
 
  0.934
groS
10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (97 aa)
 
 
  0.929
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 (446 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)
     
 
  0.916
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 (204 aa)
   
 
  0.912
hscA
Chaperone protein HscA homolog; Chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB (618 aa)
 
 
  0.895
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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