TilS

• Description: tRNAIle-lysidine synthetase
  
  

Gene name	tilS
Synonyms	yacA
Essential	yes PubMed
Product	tRNAIle-lysidine synthetase
Function	tRNA modification
Metabolic function and regulation of this protein in SubtiPathways: Nucleotides (regulation)
MW, pI	53 kDa, 8.317
Gene length, protein length	1416 bp, 472 aa
Immediate neighbours	yabT, hprT
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

translation, cell envelope stress proteins (controlled by SigM, V, W, X, Y), essential genes

This gene is a member of the following regulons

SigM regulon

The gene

Basic information

• Locus tag: BSU00670

Phenotypes of a mutant

essential PubMed

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: tRNA(Ile)-lysidine synthase family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization: cytoplasm (according to Swiss-Prot), Cytoplasm (Homogeneous) PubMed

Database entries

• Structure: 3A2K (from Geobacillus kaustophilus, complex with tRNA) PubMed

• UniProt: P37563

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon: tilS-hprT-ftsH PubMed

• Sigma factor: SigM PubMed

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Reviews

Tsutomu Suzuki, Kenjyo Miyauchi
Discovery and characterization of tRNAIle lysidine synthetase (TilS).
FEBS Lett: 2010, 584(2);272-7
[PubMed:19944692] [WorldCat.org] [DOI] (I p)

Henri Grosjean, Glenn R Björk
Enzymatic conversion of cytidine to lysidine in anticodon of bacterial isoleucyl-tRNA--an alternative way of RNA editing.
Trends Biochem Sci: 2004, 29(4);165-8
[PubMed:15124629] [WorldCat.org] [DOI] (P p)