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.
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
thiIPutative 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. (401 aa)    
Predicted Functional Partners:
iscSB
Cysteine desulfurase; Catalyzes the removal of elemental sulfur from cysteine to produce alanine.
 
 0.999
iscSA
Cysteine desulfurase involved in tRNA thiolation; Catalyzes the removal of elemental sulfur from cysteine to produce alanine.
  
 0.996
nifS
Putative desulfurase involved in iron-sulfur clusters for NAD biosynthesis; Catalyzes the removal of elemental sulfur from cysteine to produce alanine (By similarity). Seems to be required for NAD biosynthesis.
  
 0.994
thiF
Adenylate transferase and sulfur transferase (thiamine biosynthesis); Catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein ThiS; Belongs to the HesA/MoeB/ThiF family.
    
 0.989
thiG
Hydroxyethylthiazole phosphate synthetase (thiamine biosynthesis); Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
     
 0.980
mnmA
tRNA 2-thiouridylase; Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
 
  
 0.965
miaB
Enzyme for ms(2)i(6)A formation for tRNA modification; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
   
  
 0.865
rsmB
RNA-binding Sun protein; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
   
    0.827
thiE
Thiamine-phosphate pyrophosphorylase; Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). Is also able to use the 2-methoxy analog MeO-HMP-PP, as substrate in vitro, but not the 2-trifluoromethyl analog CF(3)-HMP-PP. Belongs to the thiamine-phosphate synthase family.
     
 0.826
thiD
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase; Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P. Shows no activity with pyridoxal, pyridoxamine or pyridoxine.
      
 0.822
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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