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
KOO52232.130S ribosomal protein S12 methylthiotransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. (445 aa)    
Predicted Functional Partners:
prmA
Ribosomal protein L11 methyltransferase; Methylates ribosomal protein L11; Belongs to the methyltransferase superfamily. PrmA family.
  
  
 0.913
dnaJ
Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...]
  
 
 0.831
KOO52233.1
16S rRNA methyltransferase; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
       0.773
KOO49331.1
16S rRNA methyltransferase; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
  
  
 0.756
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.
    
   0.713
thiI
Thiamine biosynthesis protein ThiI; Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
   
  
 0.530
rlmN
23S rRNA (adenine(2503)-C2)-methyltransferase; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs; Belongs to the radical SAM superfamily. RlmN family.
 
  
 0.526
dnaK
Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
     
 0.521
prfA
Peptide chain release factor 1; Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
  
  
 0.521
KOO48448.1
Chromosome partitioning protein ParA; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family.
  
   
 0.520
Your Current Organism:
Viridibacillus arvi
NCBI taxonomy Id: 263475
Other names: Bacillus arvi, Bacillus arvi Heyrman et al. 2005, Bacillus sp. 433-D9, DSM 16317, LMG 22165, LMG:22165, V. arvi, Viridibacillus arvi (Heyrman et al. 2005) Albert et al. 2007
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