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rimO protein (Methylobacillus flagellatus) - STRING interaction network
"rimO" - Ribosomal protein S12 methylthiotransferase in Methylobacillus flagellatus
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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rimORibosomal protein S12 methylthiotransferase; Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12 (441 aa)    
Predicted Functional Partners:
Mfla_1597
Zinc/iron permease (258 aa)
              0.694
guaA
GMP synthase; Catalyzes the synthesis of GMP from XMP (526 aa)
   
        0.643
Mfla_1141
Inosine-5’-monophosphate dehydrogenase (486 aa)
   
        0.604
rlmN
Hypothetical protein; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity (362 aa)
   
   
  0.558
queA
S-adenosylmethionine; Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA) (344 aa)
   
   
  0.552
Mfla_1134
Chaperone protein (418 aa)
   
 
  0.535
Mfla_1915
Diaminohydroxyphosphoribosylaminopyrimidine deaminase / 5-amino-6-(5-phosphoribosylamino)uracil reductase; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5’-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)- pyrimidinedione 5’-phosphate (377 aa)
   
   
  0.529
hscA
Fe-S protein assembly chaperone HscA; Chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB (622 aa)
   
 
  0.512
dnaK
Chaperone DnaK; Acts as a chaperone (640 aa)
   
 
  0.512
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 [...] (373 aa)
   
      0.504
Your Current Organism:
Methylobacillus flagellatus
NCBI taxonomy Id: 265072
Other names: M. flagellatus, M. flagellatus KT, Methylobacillus, Methylobacillus flagellatus, Methylobacillus flagellatus KT, Methylobacillus flagellatus str. KT, Methylobacillus flagellatus strain KT
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