Difference between revisions of "ThrS"
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+ | = [[Categories]] containing this gene/protein = | ||
+ | {{SubtiWiki category|[[translation]]}} | ||
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+ | = This gene is a member of the following [[regulons]] = | ||
+ | {{SubtiWiki regulon|[[T-box]]}} | ||
=The gene= | =The gene= | ||
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=The protein= | =The protein= | ||
Revision as of 22:17, 8 December 2010
- 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 This image was kindly provided by SubtiList
|
Contents
Categories containing this gene/protein
This gene is a member of the following regulons
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)
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- UniProt: P18255
- KEGG entry: [3]
- E.C. number: 6.1.1.3
Additional information
- subject to Clp-dependent proteolysis upon glucose starvation PubMed
Expression and regulation
- Regulatory mechanism:
- T-box: RNA switch, transcriptional antitermination PubMed
- 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)
A Wipat, N Carter, S C Brignell, B J Guy, K Piper, J Sanders, P T Emmerson, C R Harwood
The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis chromosome containing genes responsible for stress responses, the utilization of plant cell walls and primary metabolism.
Microbiology (Reading): 1996, 142 ( Pt 11);3067-78
[PubMed:8969504]
[WorldCat.org]
[DOI]
(P 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)