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hslU protein (Spirosoma linguale) - STRING interaction network
"hslU" - Heat shock protein HslVU, ATPase HslU in Spirosoma linguale
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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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hslUHeat shock protein HslVU, ATPase 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 (461 aa)    
Predicted Functional Partners:
hslV
20S proteasome subunits A and B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery (179 aa)
  0.999
Slin_1459
ATP-binding protein; Molecular chaperone. Has ATPase activity (610 aa)
     
   
  0.772
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 (829 aa)
   
 
  0.749
dnaK
Chaperone protein DnaK; Acts as a chaperone (644 aa)
     
 
  0.728
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 [...] (388 aa)
   
 
  0.723
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (545 aa)
     
   
  0.642
argS
arginyl-tRNA synthetase (599 aa)
   
   
  0.625
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 (480 aa)
   
 
  0.610
Slin_1629
Hypothetical protein (354 aa)
              0.604
groS
Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (98 aa)
     
   
  0.599
Your Current Organism:
Spirosoma linguale
NCBI taxonomy Id: 504472
Other names: S. linguale, S. linguale DSM 74, Spirosoma, Spirosoma linguale, Spirosoma linguale DSM 74, Spirosoma linguale str. DSM 74, Spirosoma linguale strain DSM 74
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