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Mettu_2595 protein (Methylobacter tundripaludum) - STRING interaction network
"Mettu_2595" - Elongation factor G in Methylobacter tundripaludum
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second shell of interactors
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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Mettu_2595Elongation 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)    
Predicted Functional Partners:
rplB
50S ribosomal protein L2 ; One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome (275 aa)
 
  0.999
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)
 
  0.999
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)
   
  0.999
rpsG
30S ribosomal protein S7 ; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA (156 aa)
 
  0.999
rplA
50S ribosomal protein L1 ; Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release (231 aa)
 
  0.999
rplC
50S ribosomal protein L3 ; One of the primary rRNA binding proteins, it binds directly near the 3’-end of the 23S rRNA, where it nucleates assembly of the 50S subunit (216 aa)
 
  0.998
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)
 
  0.998
rplN
50S ribosomal protein L14 ; Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome (122 aa)
 
  0.996
rplO
50S ribosomal protein L15 ; Binds to the 23S rRNA (144 aa)
   
  0.996
rpsL
30S ribosomal protein S12 ; Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit (124 aa)
 
  0.995
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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