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R2601_11694 protein (Pelagibaca bermudensis) - STRING interaction network
"R2601_11694" - Polypeptide deformylase in Pelagibaca bermudensis
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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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R2601_11694Polypeptide deformylase ; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (164 aa)    
Predicted Functional Partners:
R2601_11689
Polypeptide deformylase ; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (165 aa)
 
       
0.900
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)
 
   
  0.886
R2601_11179
Methionyl-tRNA formyltransferase ; Modifies the free amino group of the aminoacyl moiety of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by- (I) promoting its recognition by IF2 and (II) impairing its binding to EFTu-GTP (221 aa)
 
  0.836
R2601_11684
Polypeptide deformylase ; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (173 aa)
 
       
0.773
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)
   
 
  0.716
rplQ
50S ribosomal protein L17 (139 aa)
     
 
  0.702
folD
Bifunctional protein FolD ; Catalyzes the oxidation of 5,10- methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10- formyltetrahydrofolate (300 aa)
       
  0.697
prfB
Peptide chain release factor 2 ; Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA (373 aa)
 
      0.673
topA
DNA topoisomerase I ; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5’-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3’-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...] (906 aa)
   
   
  0.662
rplI
50S ribosomal protein L9 ; Binds to the 23S rRNA (206 aa)
 
   
  0.652
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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