Difference between revisions of "ThrS"

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|style="background:#ABCDEF;" align="center"|'''Function''' || translation  
 
|style="background:#ABCDEF;" align="center"|'''Function''' || translation  
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/tRNA_charging.html tRNA charging]'''
 
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|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 73 kDa, 5.214   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 73 kDa, 5.214   

Revision as of 16:31, 16 June 2009

  • Description: threonyl-tRNA synthetase (major)

Gene name thrS
Synonyms
Essential no
Product threonyl-tRNA synthetase (major)
Function translation
Metabolic function and regulation of this protein in SubtiPathways:
tRNA charging
MW, pI 73 kDa, 5.214
Gene length, protein length 1929 bp, 643 aa
Immediate neighbours ysaA, ytxC
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
ThrS context.gif
This image was kindly provided by SubtiList





The gene

Basic information

  • Locus tag: BSU28950

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): ThrZ, 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:

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

  • subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

  • Operon:
  • Regulation:
  • Regulatory mechanism:
  • Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

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)

Harald Putzer, Ciarán Condon, Dominique Brechemier-Baey, Renata Brito, Marianne Grunberg-Manago
Transfer RNA-mediated antitermination in vitro.
Nucleic Acids Res: 2002, 30(14);3026-33
[PubMed:12136084] [WorldCat.org] [DOI] (I p)

H Putzer, S Laalami, A A Brakhage, C Condon, M Grunberg-Manago
Aminoacyl-tRNA synthetase gene regulation in Bacillus subtilis: induction, repression and growth-rate regulation.
Mol Microbiol: 1995, 16(4);709-18
[PubMed:7476165] [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)