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lon protein (Pelagibaca bermudensis) - STRING interaction network
"lon" - ATP-dependent protease La in Pelagibaca bermudensis
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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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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 (421 aa)
   
 
  0.937
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 (210 aa)
   
 
  0.839
tmk
dTMP kinase ; Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis (208 aa)
   
   
  0.830
R2601_09877
Methyltransferase (367 aa)
         
  0.774
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)
   
 
  0.772
dnaK
Heat shock protein 70 ; Acts as a chaperone (642 aa)
 
 
  0.761
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 (436 aa)
   
 
  0.737
ftsH
ATP-dependent zinc 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 (637 aa)
     
 
  0.731
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, [...] (385 aa)
 
   
  0.718
dnaA
Chromosomal replication initiator protein DnaA ; Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box)- 5’-TTATC[CA]A[CA]A-3’. DnaA binds to ATP and to acidic phospholipids (451 aa)
     
 
  0.711
Your Current Organism:
Pelagibaca bermudensis
NCBI taxonomy Id: 314265
Other names: P. bermudensis HTCC2601, Pelagibaca, Pelagibaca Cho and Giovannoni 2006, Pelagibaca bermudensis, Pelagibaca bermudensis Cho and Giovannoni 2006, Pelagibaca bermudensis HTCC2601, Pelagibaca bermudensis str. HTCC2601, Pelagibaca bermudensis strain HTCC2601, Roseovarius sp. HTCC2601
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