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lon protein (Midichloria mitochondrii) - STRING interaction network
"lon" - ATP-dependent protease La 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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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 (794 aa)    
Predicted Functional Partners:
clpX
ATP-dependent protease ATP-binding subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (415 aa)
   
 
  0.960
clpP
ATP-dependent Clp protease proteolytic subunit; 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 (216 aa)
   
 
  0.901
tmk
Thymidylate kinase; Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis (205 aa)
   
   
  0.885
nadD
Nicotinate (nicotinamide) nucleotide adenylyltransferase; Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD) (208 aa)
         
  0.866
ftsH
Cell division protease 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 (644 aa)
   
 
  0.827
dnaK
Molecular chaperone DnaK; Acts as a chaperone (631 aa)
   
 
  0.825
hslU
ATP-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)
   
 
  0.824
rsfS
Putative iojap-like protein; Functions as a ribosomal silencing factor. Interacts with ribosomal protein L14 (rplN), blocking formation of intersubunit bridge B8. Prevents association of the 30S and 50S ribosomal subunits and the formation of functional ribosomes, thus repressing translation (105 aa)
              0.824
grpE
Molecular chaperone GrpE; 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 [...] (183 aa)
   
 
  0.816
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (385 aa)
   
 
  0.805
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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