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
smpBProbable ssra-binding protein; Required for rescue of stalled ribosomes mediated by trans- translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then sw [...] (148 aa)    
Predicted Functional Partners:
rplS
Probable 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.
 
 
 0.954
rplN
Probable 50s ribosomal subunit protein l14; Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome; Belongs to the universal ribosomal protein uL14 family.
    
 
 0.946
rpsG
Probable 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.
  
 
 0.945
rpsR
Probable 30s ribosomal protein s18; Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit.; Belongs to the bacterial ribosomal protein bS18 family.
  
 
 
 0.944
rpsO
Probable 30s ribosomal subunit 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.
 
 
 
 0.943
rpsB
Probable 30s ribosomal protein s2; Belongs to the universal ribosomal protein uS2 family.
 
 
 0.942
rplC
Probable 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.
  
 
 0.939
rplT
Probable 550s ribosomal protein l20; Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit.
 
 
 0.932
rpmA
Probable 50s ribosomal protein l27; Belongs to the bacterial ribosomal protein bL27 family.
 
 
 
 0.931
rpsH
Probable 30s ribosomal protein s8; One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.; Belongs to the universal ribosomal protein uS8 family.
  
 
 0.925
Your Current Organism:
Ralstonia solanacearum
NCBI taxonomy Id: 267608
Other names: R. solanacearum GMI1000, Ralstonia solanacearum GMI1000, Ralstonia solanacearum str. GMI1000, Ralstonia solanacearum strain GMI1000
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.