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Mettu_3771 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_3771" - Polypeptide deformylase in Methylobacter tundripaludum
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second shell of interactors
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proteins of unknown 3D structure
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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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Score
Mettu_3771Polypeptide 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 (168 aa)    
Predicted Functional Partners:
fmt
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 (309 aa)
 
  0.997
metG
Methionyl-tRNA synthetase ; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation (672 aa)
   
 
  0.944
Mettu_3769
Ribosomal RNA small subunit methyltransferase B (435 aa)
   
      0.935
Mettu_3768
Putative uncharacterized protein (194 aa)
              0.912
Mettu_3767
Multi-sensor signal transduction histidine kinase (724 aa)
              0.912
Mettu_1734
Sigma 54 interacting domain protein (503 aa)
          0.896
rplQ
50S ribosomal protein L17 (125 aa)
     
 
  0.883
Mettu_3766
Putative two component, sigma54 specific, transcriptional regulator (453 aa)
              0.863
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 (215 aa)
 
   
  0.802
rplV
50S ribosomal protein L22 ; The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome (111 aa)
     
      0.799
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum, M. tundripaludum SV96, Methylobacter, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum Wartiainen et al. 2006, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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