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frr protein (Thermosynechococcus elongatus) - STRING interaction network
"frr" - Ribosome recycling factor in Thermosynechococcus elongatus
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query proteins and first shell of interactors
white nodes:
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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frrRibosome recycling factor; Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another (182 aa)    
Predicted Functional Partners:
rpmA
50S ribosomal protein L27 (86 aa)
 
  0.998
rpl2
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 (288 aa)
     
  0.998
rplQ
50S ribosomal protein L17 (116 aa)
   
  0.996
rpl1
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 (237 aa)
   
  0.994
rps2
30S ribosomal protein S2 (263 aa)
 
  0.992
rplM
50S ribosomal protein L13; This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly (152 aa)
   
  0.988
rplP
50S ribosomal protein L16; Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs (143 aa)
     
  0.984
fusA
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 (691 aa)
   
  0.983
rps9
30S ribosomal protein S9 (137 aa)
   
  0.982
rplN
50S ribosomal protein L14; Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome (122 aa)
     
 
  0.981
Your Current Organism:
Thermosynechococcus elongatus
NCBI taxonomy Id: 197221
Other names: T. elongatus, T. elongatus BP-1, Thermosynechococcus, Thermosynechococcus elongatus, Thermosynechococcus elongatus BP-1, Thermosynechococcus elongatus str. BP-1, Thermosynechococcus elongatus strain BP-1
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