tilS

168

trigger enzyme, tRNA^Ile-lysidine synthetase (modifies C34 at the wobble position of tRNA2^Ile to lysidine) and part of a transcription activator

Locus: BSU_00670

Molecular weight: 53.30 kDa

Isoelectric point: 8.32

Protein length: 472 aa

Gene length: 1419 bp

Function: tRNA modification, control of ftsH expression

Product: tRNA^Ile-lysidine synthetase

Essential: yes

E.C.: 6.3.4.19

Synonyms: tilS, yacA

Genomic Context

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List of homologs in different organisms, belongs to COG0037 (Galperin et al., 2021)

Gene

Coordinates: 74,929  76,347

Phenotypes of a mutant

• essential PubMed

The protein

Catalyzed reaction/ biological activity

• modifies C34 at the wobble position of tRNA2^Ile to lysidine
• ATP + cytidine³⁴ in tRNA^Ile2 + L-lysine --> AMP + diphosphate + H⁺ + lysidine³⁴ in tRNA^Ile2 (according to UniProt)

Protein family

• tRNA(Ile)-lysidine synthase family (single member, according to UniProt)

Domains

• The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding (according to UniProt)

Structure

• 3A2K (PDB) (from Geobacillus kaustophilus, complex with tRNA) PubMed
• P37563 (AlphaFold)

Localization

• Cytoplasm (Homogeneous) PubMed

Expression and Regulation

Operons

• Genes: tilS-hprT-ftsH

  Description: PubMed

  Regulation

  • induced by heat shock (class III)

  Regulatory mechanism

  • TilS: activation, with HprT PubMed, in tilS regulon
  • HprT: activation, with TilS PubMed, in hprT regulon

  Sigma factors

  • SigM: sigma factor, PubMed, in sigM regulon
  • SigA: sigma factor, PubMed, in sigA regulon

  Additional information

  • the mRNA is very stable (half-life > 15 min) PubMed

• Genes: spoIIE-yabS-yabT-tilS-hprT-ftsH

  Description: PubMed

  Regulation

  • expressed early during sporulation in the forespore (SigF) PubMed

  Sigma factors

  • SigF: sigma factor, PubMed, in sigF regulon

Biological materials

Mutant

• MGNA-B922 (yacA::erm), available at the NBRP B. subtilis, Japan

References

Reviews

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Original Publications

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