ThrZ

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  • Description: threonyl-tRNA synthetase (minor)

Gene name thrZ
Synonyms thrS2
Essential no
Product threonyl-tRNA synthetase (minor)
Function translation
Gene expression levels in SubtiExpress: thrZ
Metabolic function and regulation of this protein in SubtiPathways:
tRNA charging
MW, pI 73 kDa, 5.753
Gene length, protein length 1914 bp, 638 aa
Immediate neighbours ywhA, mmr
Sequences Protein DNA DNA_with_flanks
Genetic context
ThrZ context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
ThrZ expression.png




























Categories containing this gene/protein

translation

This gene is a member of the following regulons

T-box

The gene

Basic information

  • Locus tag: BSU37560

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr) (according to Swiss-Prot)
  • Protein family: class-II aminoacyl-tRNA synthetase family (according to Swiss-Prot)
  • Paralogous protein(s): ThrS, one of the two proteins has to be present for viability PubMed

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 1TJE (from Escherichia coli, 43% identity, 65% similarity) PubMed
  • KEGG entry: [3]

Additional information

  • subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

  • Regulation:
  • Additional information:
    • subject to Clp-dependent proteolysis upon glucose starvation PubMed
    • the amount of the mRNA is substantially decreased upon depletion of RNase Y PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J  
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y. 
Mol Microbiol. 2011 81(6): 1459-1473. 
PubMed:21815947