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lon protein (Spirosoma linguale) - STRING interaction network
"lon" - ATP-dependent protease La in Spirosoma linguale
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Known Interactions
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Predicted Interactions
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gene co-occurrence
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textmining
co-expression
protein homology
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lonATP-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)    
Predicted Functional Partners:
clpX
Sigma 54 interacting domain-containing protein; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (410 aa)
   
 
  0.904
eno
Enolase; Catalyzes the reversible conversion of 2- phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis (426 aa)
 
 
  0.821
clpP
Endopeptidase Clp; 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 (229 aa)
   
 
  0.808
hslU
Heat 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)
   
 
  0.749
dnaK
Chaperone protein DnaK; Acts as a chaperone (644 aa)
 
 
  0.741
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (545 aa)
     
 
  0.731
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)
     
 
  0.719
ftsH
ATP-dependent metalloprotease FtsH; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins (676 aa)
   
 
  0.715
valS
valyl-tRNA synthetase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a "posttransfer" editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner (895 aa)
 
   
  0.705
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)
   
   
  0.700
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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