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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
lepAGTP-binding protein LepA; 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. (617 aa)    
Predicted Functional Partners:
rpsT
30S ribosomal protein S20; Binds directly to 16S ribosomal RNA.
   
   0.994
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.
 
 
 0.993
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.
 
   0.991
rpsO
30S ribosomal protein S15; Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
 
 
 0.991
rpsB
30S ribosomal protein S2; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the universal ribosomal protein uS2 family.
  
 
 0.990
rplQ
50S ribosomal protein L17; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.989
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.
  
 
 0.989
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.
  
 
 0.989
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.
  
 
 0.989
rpsP
30S ribosomal protein S16; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the bacterial ribosomal protein bS16 family.
 
 
 0.989
Your Current Organism:
Streptomyces fradiae
NCBI taxonomy Id: 1906
Other names: ATCC 10745, ATCC 19760, Actinomyces fradii, BCRC 12196, CBS 498.68, CCM 3174, CCRC 12196, CCRC:12196, CECT 3197, DSM 40063, HAMBI 965, HUT 6095, IFO 12773, IFO 3718, IMET 42051, IMI 061202, ISP 5063, JCM 4133, JCM 4579, JCM 4824 [[Streptomyces roseoflavus]], KCTC 9760, NBRC 12773, NBRC 13439 [[Streptomyces roseoflavus]], NBRC 3718, NCIMB 11005, NCIMB 8233, NRRL B-2789 [[Streptomyces roseoflavus]], NRRL-ISP 5063, PCM 2330, RIA 97, S. fradiae, Streptomyces fradiae subsp. fradiae, Streptomyces fradii, Streptomyces roseiflavus, Streptomyces roseoflavus, Streptomyces sp. NEAE-82, UNIQEM 146, VKM Ac-150, VKM Ac-151, VKM Ac-152, VKM Ac-764
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