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hslU protein (Midichloria mitochondrii) - STRING interaction network
"hslU" - ATP-dependent protease HslVU, ATPase subunit HslU in Midichloria mitochondrii
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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 HslVU, 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 (443 aa)    
Predicted Functional Partners:
hslV
ATP-dependent protease HslVU, peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery (175 aa)
  0.999
dnaK
Molecular chaperone DnaK; Acts as a chaperone (631 aa)
   
 
  0.863
htpG
Chaperone protein htpG; Molecular chaperone. Has ATPase activity (579 aa)
   
   
  0.854
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 [...] (385 aa)
   
 
  0.840
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 (794 aa)
   
 
  0.824
dksA
DnaK suppressor protein; Transcription factor that acts by binding directly to the RNA polymerase (RNAP). Required for negative regulation of rRNA expression and positive regulation of several amino acid biosynthesis promoters (141 aa)
       
  0.812
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (385 aa)
     
   
  0.807
argS
arginyl-tRNA synthetase (558 aa)
   
   
  0.792
murF
UDP-N-acetylmuramyl pentapeptide synthase; Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein (461 aa)
              0.778
groS
Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (97 aa)
     
   
  0.771
Your Current Organism:
Midichloria mitochondrii
NCBI taxonomy Id: 696127
Other names: C. Midichloria, C. Midichloria mitochondrii, C. Midichloria mitochondrii IricVA, Candidatus Midichloria, Candidatus Midichloria mitochondrii, Candidatus Midichloria mitochondrii IricVA, Candidatus Midichloria mitochondrii str. IricVA, Candidatus Midichloria mitochondrii strain IricVA, Ixodes ricinus endosymbiont, Ixodes ricinus endosymbiont 1 (IricES1), Midichloria, Midichloria mitochondrii, Midichloria mitochondrii IricVA, endosymbiont of Ixodes ricinus
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