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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
rbfAPutative ribosome-binding factor A; One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA. (147 aa)    
Predicted Functional Partners:
infB
Translation initiation factor IF-2; One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. IF-2 subfamily.
  
  
 0.984
rpsO
30S ribosomal protein S15; 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.
  
 
 0.948
truB
tRNA pseudouridine synthase B; Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs; Belongs to the pseudouridine synthase TruB family. Type 1 subfamily.
  
  
 0.948
rpsE
30S ribosomal protein S5; With S4 and S12 plays an important role in translational accuracy; Belongs to the universal ribosomal protein uS5 family.
   
 
 0.946
rpsQ
30S ribosomal protein S17; One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
   
 
 0.919
DIP1475
Conserved hypothetical protein; Similar to, although shorter in its N-terminal region than, Mycobacterium tuberculosis hypothetical 35.4 kDa protein Rv2837c or MTCY16B7.05 TR:P71615 (EMBL:Z81331) (336 aa) fasta scores: E(): 8.5e-29, 34.84% id in 287 aa, and to Clostridium acetobutylicum exopolyphosphatase family protein CAC1804 TR:AAK79769 (EMBL:AE007689) (321 aa) fasta scores: E(): 1.9e-19, 33.19% id in 235 aa.
  
    0.915
rpsD
30S ribosomal protein S4; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit.
   
 
 0.910
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.
   
 
 0.905
rpsK
30S ribosomal protein S11; Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine- Dalgarno cleft in the 70S ribosome; Belongs to the universal ribosomal protein uS11 family.
   
 
 0.891
rpsF
30S ribosomal protein S6; Binds together with S18 to 16S ribosomal RNA.
  
 
 0.882
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.