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lon protein (Desulfotomaculum reducens) - STRING interaction network
"lon" - Lon protease in Desulfotomaculum reducens
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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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lonLon protease; 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 (810 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 (416 aa)
   
 
  0.955
engB
Probable GTP-binding protein EngB; Necessary for normal cell division and for the maintenance of normal septation (205 aa)
 
          0.920
hslU
ATP-dependent protease 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 (466 aa)
   
 
  0.872
hslV
ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery (176 aa)
     
 
  0.859
grpE
Protein 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- dependent [...] (192 aa)
 
 
  0.835
htpG
Chaperone protein HtpG; Molecular chaperone. Has ATPase activity (615 aa)
     
   
  0.813
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; Belongs to the peptidase S14 family (195 aa)
   
 
  0.811
Dred_0180
PFAM- UvrB/UvrC protein; AAA ATPase, central domain protein; Clp N terminal domain protein; ATPase associated with various cellular activities, AAA_5; ATPase AAA-2 domain protein; SMART- AAA ATPase; KEGG- chy-CHY_2348 negative regulator of genetic competence ClpC/MecB; Belongs to the ClpA/ClpB family (812 aa)
     
 
  0.793
Dred_2560
PFAM- magnesium chelatase, ChlI subunit; AAA ATPase, central domain protein; peptidase S16, lon domain protein; SMART- AAA ATPase; KEGG- mta-Moth_0530 AAA ATPase; Belongs to the peptidase S16 family (571 aa)
   
   
0.774
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; Belongs to the AAA ATPase family (615 aa)
   
 
  0.771
Your Current Organism:
Desulfotomaculum reducens
NCBI taxonomy Id: 349161
Other names: D. reducens MI-1, Desulfotomaculum reducens, Desulfotomaculum reducens MI-1, Desulfotomaculum reducens str. MI-1, Desulfotomaculum reducens strain MI-1
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