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lon protein (Maritimibacter alkaliphilus) - STRING interaction network
"lon" - ATP-dependent protease La in Maritimibacter alkaliphilus
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Predicted Interactions
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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 (801 aa)    
Predicted Functional Partners:
clpX
ATP-dependent Clp protease ATP-binding subunit ClpX ; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (423 aa)
   
 
  0.949
eno
2-phosphoglycerate dehydratase ; Catalyzes the reversible conversion of 2- phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis (424 aa)
 
 
  0.859
tmk
dTMP kinase ; Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis (207 aa)
   
   
  0.853
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 (193 aa)
   
 
  0.813
dnaK
Heat shock protein 70 ; Acts as a chaperone (636 aa)
 
 
  0.787
hslU
Unfoldase 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 (435 aa)
   
 
  0.771
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, [...] (382 aa)
 
   
  0.745
RB2654_15514
Methyltransferase (364 aa)
         
  0.742
grpE
HSP-70 cofactor ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. 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- depend [...] (199 aa)
   
 
  0.735
hslV
ATP-dependent protease subunit HslV ; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery (183 aa)
     
 
  0.723
Your Current Organism:
Maritimibacter alkaliphilus
NCBI taxonomy Id: 314271
Other names: M. alkaliphilus, M. alkaliphilus HTCC2654, Maritimibacter, Maritimibacter Lee et al. 2007, Maritimibacter alkaliphilus, Maritimibacter alkaliphilus HTCC2654, Maritimibacter alkaliphilus Lee et al. 2007, Maritimibacter alkaliphilus str. HTCC2654, Maritimibacter alkaliphilus strain HTCC2654, Rhodobacterales bacterium HTCC2654
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