STRINGSTRING
STRING protein interaction network
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:
a 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 to 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
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
lepAPutative GTP-binding protein; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner. (615 aa)    
Predicted Functional Partners:
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.
 
 
 0.939
rpsT
30S ribosomal protein S20; Binds directly to 16S ribosomal RNA.
   
   0.935
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; Belongs to the universal ribosomal protein uL3 family.
  
 
 0.919
rpsB
30S ribosomal protein S2; Similar to Mycobacterium tuberculosis 30S ribosomal protein S2 RpsB or Rv2890c or MT2958 or MTCY274.21c SW:RS2_MYCTU (Q10796) (287 aa) fasta scores: E(): 1.4e-68, 70.94% id in 265 aa, and to Escherichia coli 30S ribosomal protein S2 RpsB or B0169 or Z0180 or ECS0171 SW:RS2_ECOLI (P02351) (240 aa) fasta scores: E(): 2.8e-40, 50.22% id in 225 aa; Belongs to the universal ribosomal protein uS2 family.
  
 
 0.918
rpsI
30S ribosomal protein S9; Similar to Mycobacterium tuberculosis 30S ribosomal protein S9 RpsI or Rv3442c or MT3547 or MTCY77.14c SW:RS9_MYCTU (O06259) (151 aa) fasta scores: E(): 8.2e-33, 66.89% id in 145 aa; Belongs to the universal ribosomal protein uS9 family.
  
 
 0.917
rplQ
Similar to Mycobacterium leprae 50S ribosomal protein L17 RplQ or ML1956 or MLCB1222.26c SW:RL17_MYCLE (Q9X797) (170 aa) fasta scores: E(): 3.1e-26, 58.86% id in 158 aa.
  
 
 0.914
rplS
50S ribosomal protein L19; This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site.
 
   0.913
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; Belongs to the universal ribosomal protein uS7 family.
  
 
 0.911
rplO
50s ribosomal protein L15; Binds to the 23S rRNA; Belongs to the universal ribosomal protein uL15 family.
  
 
 
 0.911
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.
   
 
 0.910
Your Current Organism:
Corynebacterium diphtheriae
NCBI taxonomy Id: 257309
Other names: C. diphtheriae NCTC 13129, Corynebacterium diphtheriae NCTC 13129, Corynebacterium diphtheriae NCTC13129
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.