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Mettu_2895 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_2895" - Elongation factor P in Methylobacter tundripaludum
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query proteins and first shell of interactors
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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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Cooccurence
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[Homology]
Score
Mettu_2895Elongation factor P (189 aa)    
Predicted Functional Partners:
Mettu_2894
Elongation factor P--(R)-beta-lysine ligase (324 aa)
 
 
  0.997
Mettu_2896
Lysine-2,3-aminomutase-related protein (336 aa)
 
     
  0.970
rplR
50S ribosomal protein L18 ; This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance (117 aa)
   
 
  0.931
rpsE
30S ribosomal protein S5 ; Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body (168 aa)
     
 
  0.916
rplE
50S ribosomal protein L5 ; This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs (179 aa)
     
   
  0.910
rplP
50S ribosomal protein L16 ; Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs (137 aa)
   
   
  0.908
rplF
50S ribosomal protein L6 ; This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center (177 aa)
     
   
  0.902
Mettu_2595
Elongation factor G ; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (694 aa)
     
 
  0.835
Mettu_1336
Elongation factor G ; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (698 aa)
     
 
  0.835
rpsD
30S ribosomal protein S4 ; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit (206 aa)
 
   
  0.785
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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