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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
mtaBtRNA N(6)-threonylcarbamoyladenosine (t(6)A) methylthiotransferase; Catalyzes the methylthiolation of N6- threonylcarbamoyladenosine (t(6)A), leading to the formation of 2- methylthio-N6-threonylcarbamoyladenosine (ms(2)t(6)A) at position 37 in tRNAs that read codons beginning with adenine. Belongs to the methylthiotransferase family. MtaB subfamily. (451 aa)    
Predicted Functional Partners:
prmA
Ribosomal protein L11 methyltransferase; Methylates ribosomal protein L11; Belongs to the methyltransferase superfamily. PrmA family.
  
  
 0.970
rsmE
Methylase of U1498 in 16S rRNA; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit (By similarity).
  
  
 0.957
dnaJ
Co-factor of molecular chaperone; 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 betwe [...]
  
 
 0.904
rsmB
RNA-binding Sun protein; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
  
  
 0.842
rlmN
23S rRNA m2A2503 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.
 
  
 0.766
miaA
tRNA isopentenylpyrophosphate transferase; Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A); Belongs to the IPP transferase family.
  
 0.762
thiI
Putative persulfide ATP pyrophosphatase involved in thiamine biosynthesis and tRNA modification; 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.
   
  
 0.721
dnaK
Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
  
 0.700
hemN
Coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently (By similarity). Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L- methionine (By similarity).
 
  
 0.699
yrvM
Putative factor involved in sulfur-containing coenzyme synthesis; Catalyzes the ATP-dependent dehydration of threonylcarbamoyladenosine at position 37 (t(6)A37) to form cyclic t(6)A37 (ct(6)A37) in tRNAs that read codons beginning with adenine.
 
  
 0.689
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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