ThrZ

• Description: threonyl-tRNA synthetase (minor)
  
  

Gene name	thrZ
Synonyms	thrS2
Essential	no
Product	threonyl-tRNA synthetase (minor)
Function	translation
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
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

This gene is a member of the following regulons

T-box

The gene

Basic information

• Locus tag: BSU37560

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Interactions:

• Localization:
  • cytoplasm (according to Swiss-Prot)

Database entries

• Structure: 1TJE (from Escherichia coli, 43% identity, 65% similarity) PubMed

• UniProt: P18256

• KEGG entry: [3]

• E.C. number: 6.1.1.3

Additional information

• subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

• Operon: thrZ-ywhA PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • induced by threonine limitation (T-box) PubMed

• Regulatory mechanism:
  • T-box: RNA switch, transcriptional antitermination PubMed

• 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:

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

Ana Gutiérrez-Preciado, Tina M Henkin, Frank J Grundy, Charles Yanofsky, Enrique Merino
Biochemical features and functional implications of the RNA-based T-box regulatory mechanism.
Microbiol Mol Biol Rev: 2009, 73(1);36-61
[PubMed:19258532] [WorldCat.org] [DOI] (I p)

Helena B Thomaides, Ella J Davison, Lisa Burston, Hazel Johnson, David R Brown, Alison C Hunt, Jeffery Errington, Lloyd Czaplewski
Essential bacterial functions encoded by gene pairs.
J Bacteriol: 2007, 189(2);591-602
[PubMed:17114254] [WorldCat.org] [DOI] (P p)

N Gendron, H Putzer, M Grunberg-Manago
Expression of both Bacillus subtilis threonyl-tRNA synthetase genes is autogenously regulated.
J Bacteriol: 1994, 176(2);486-94
[PubMed:8288542] [WorldCat.org] [DOI] (P p)

H Putzer, N Gendron, M Grunberg-Manago
Co-ordinate expression of the two threonyl-tRNA synthetase genes in Bacillus subtilis: control by transcriptional antitermination involving a conserved regulatory sequence.
EMBO J: 1992, 11(8);3117-27
[PubMed:1379177] [WorldCat.org] [DOI] (P p)