Difference between revisions of "ThrZ"

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(Expression and regulation)
(Database entries)
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=== Database entries ===
 
=== Database entries ===
  
* '''Structure:'''
+
* '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1TJE 1TJE] (from ''Escherichia coli'', 43% identity, 65% similarity) {{PubMed|15525511}}
 +
 
  
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P18256 P18256]
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P18256 P18256]

Revision as of 17:16, 18 February 2010

  • 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
ThrZ context.gif
This image was kindly provided by SubtiList







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

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

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)

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)