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
smpBTrans-translation 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 switch [...] (148 aa)    
Predicted Functional Partners:
rpsB
30S ribosomal subunit protein S2; Function of homologous gene experimentally demonstrated in an other organism; structure; Belongs to the universal ribosomal protein uS2 family.
  
 
 0.997
rplT
50S ribosomal subunit protein L20, also posttranslational autoregulator; 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.
 
 
 0.997
rplS
50S ribosomal subunit 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.
 
 
 0.997
rpsO
30S ribosomal subunit protein S15; Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
 
 
 
 0.997
rplM
50S ribosomal subunit 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.
  
 
 0.997
rpmA
50S ribosomal subunit protein L27; Function of homologous gene experimentally demonstrated in an other organism; structure; Belongs to the bacterial ribosomal protein bL27 family.
 
 
 
 0.997
rpsG
30S ribosomal subunit protein S7, initiates assembly; 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.
  
 
 0.997
rpsR
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.
  
 
 
 0.997
rplD
50S ribosomal subunit protein L4, regulates expression of S10 operon; Forms part of the polypeptide exit tunnel.
  
 
 0.997
rplC
50S ribosomal subunit 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.
  
 
 0.997
Your Current Organism:
Paraburkholderia ribeironis
NCBI taxonomy Id: 1247936
Other names: Burkholderia sp. STM 7168, Burkholderia sp. STM 7217, Burkholderia sp. STM 7296, DSM 101188, LMG 29351, LMG:29351, P. ribeironis, Paraburkholderia ribeironis Bournaud et al. 2017, STM 7296, STM:7296
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