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
rnrRibonuclease R; 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs. (788 aa)    
Predicted Functional Partners:
rph
Ribonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
   
 0.997
KOO37130.1
Carboxylesterase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
    0.795
smpB
Single-stranded DNA-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 t [...]
     
 0.743
KOO46877.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family.
  
   0.698
KOO40849.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family.
  
   0.698
rsmA
16S rRNA methyltransferase; Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
  
 
 0.632
rplD
50S ribosomal protein L4; Forms part of the polypeptide exit tunnel.
  
  0.632
rpsO
30S ribosomal protein S15; Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
    
 
 0.604
KOO46577.1
50S ribosomal protein L7; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  0.604
rnpA
Ribonuclease P; RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
     
 0.598
Your Current Organism:
Bacillus koreensis
NCBI taxonomy Id: 284581
Other names: B. koreensis, Bacillus koreensis Lim et al. 2006, Bacillus sp. BR030, DSM 16467, KCTC 3914, strain BR030
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.