STRINGSTRING
fusA protein (Thermoproteus tenax) - STRING interaction network
"fusA" - Elongation factor aEF-2 in Thermoproteus tenax
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
fusAElongation factor aEF-2; 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 (740 aa)    
Predicted Functional Partners:
rpl18
50S ribosomal protein L18p; 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 (203 aa)
 
  0.999
rpl5
50S ribosomal protein L5p; 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. May contact the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs (184 aa)
 
  0.999
rpl1
50S ribosomal protein L1p; Binds directly to 23S rRNA. Probably involved in E site tRNA release (223 aa)
 
  0.999
rpl2
50S ribosomal protein L2p; 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 (243 aa)
 
  0.999
rpl3
50S ribosomal protein L3p; 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 (339 aa)
 
  0.999
rps7
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 (225 aa)
 
  0.999
rpl15
50S ribosomal protein L15; Binds to the 23S rRNA (157 aa)
   
  0.999
rps5
Ribosomal protein S5p/L7e; With S4 and S12 plays an important role in translational accuracy (203 aa)
  0.999
rpl23p
50S ribosomal protein L23p; Binds to 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome (83 aa)
   
  0.999
rps12
30S ribosomal protein S12p; With S4 and S5 plays an important role in translational accuracy. Located at the interface of the 30S and 50S subunits (147 aa)
   
  0.999
Your Current Organism:
Thermoproteus tenax
NCBI taxonomy Id: 768679
Other names: T. tenax, T. tenax Kra 1, Thermoproteus tenax, Thermoproteus tenax DSM 2078, Thermoproteus tenax JCM 9277, Thermoproteus tenax Kra 1, Thermoproteus tenax str. Kra 1, Thermoproteus tenax strain Kra 1
Server load: low (9%) [HD]