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
ettAProbable macrolide-transport ATP-binding protein ABC transporter; A translation factor that gates the progression of the 70S ribosomal initiation complex (IC, containing tRNA(fMet) in the P-site) into the translation elongation cycle by using a mechanism sensitive to the ATP/ADP ratio. Binds to the 70S ribosome E-site where it modulates the state of the translating ribosome during subunit translocation. ATP hydrolysis probably frees it from the ribosome, which can enter the elongation phase. (558 aa)    
Predicted Functional Partners:
rplU
50S ribosomal protein L21 RplU; This protein binds to 23S rRNA in the presence of protein L20; Belongs to the bacterial ribosomal protein bL21 family.
  
   0.920
rpsO
30S ribosomal protein S15 RpsO; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it helps nucleate assembly of the platform of the 30S subunit by binding and bridging several RNA helices of the 16S rRNA.
  
 
 0.920
rplD
50S ribosomal protein L4 RplD; One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome.
  
 
 0.919
rplM
50S ribosomal protein L13 RplM; 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.
  
   0.918
rpsC
30S ribosomal protein S3 RpsC; Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation; Belongs to the universal ribosomal protein uS3 family.
  
   0.917
rplC
50S ribosomal protein L3 RplC; 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.
  
 
 0.914
rpsG
30S ribosomal protein S7 RpsG; 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.
  
 
 0.913
rplP
50S ribosomal protein L16 RplP; Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs; Belongs to the universal ribosomal protein uL16 family.
  
 
 0.912
rpsD
30S ribosomal protein S4 RpsD; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit. Belongs to the universal ribosomal protein uS4 family.
  
 
 0.912
rplI
50S ribosomal protein L9 RplI; Binds to the 23S rRNA.
   
 
 0.911
Your Current Organism:
Mycobacterium tuberculosis H37Rv
NCBI taxonomy Id: 83332
Other names: M. tuberculosis H37Rv, Mycobacterium sp. H37Rv, Mycobacterium tuberculosis str. H37Rv, Mycobacterium tuberculosis strain H37Rv
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.