Difference between revisions of "ThrB"
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= [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
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= This gene is a member of the following [[regulons]] = | = This gene is a member of the following [[regulons]] = | ||
| − | + | {{SubtiWiki regulon|[[CodY regulon]]}} | |
=The gene= | =The gene= | ||
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* '''Kinetic information:''' | * '''Kinetic information:''' | ||
| − | * '''Domains:''' | + | * '''[[Domains]]:''' |
* '''Modification:''' | * '''Modification:''' | ||
| − | * ''' | + | * '''[[Cofactors]]:''' |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=thrB_3312844_3313773_-1 thrB] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=thrB_3312844_3313773_-1 thrB] {{PubMed|22383849}} | ||
| − | * '''Sigma factor:''' | + | * '''[[Sigma factor]]:''' |
| − | * '''Regulation:''' repressed by casamino acids {{PubMed|12107147}} | + | * '''Regulation:''' |
| + | ** repressed by casamino acids {{PubMed|12107147}} | ||
| + | ** repressed during growth in the presence of branched chain amino acids ([[CodY]]) {{PubMed|24163341}} | ||
* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
| + | ** [[CodY]]: transcription repression {{PubMed|24163341}} | ||
* '''Additional information:''' | * '''Additional information:''' | ||
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=References= | =References= | ||
| − | <pubmed>12107147 3098560, </pubmed> | + | <pubmed>12107147 3098560,24163341 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 14:06, 22 December 2013
- Description: homoserine kinase
| Gene name | thrB |
| Synonyms | thrA |
| Essential | no |
| Product | homoserine kinase |
| Function | biosynthesis of threonine |
| Gene expression levels in SubtiExpress: thrB | |
| Metabolic function and regulation of this protein in SubtiPathways: Lys, Thr | |
| MW, pI | 33 kDa, 4.735 |
| Gene length, protein length | 927 bp, 309 aa |
| Immediate neighbours | yuxL, thrC |
| Sequences | Protein DNA DNA_with_flanks |
Genetic context 
This image was kindly provided by SubtiList
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Expression at a glance PubMed
| |
Contents
Categories containing this gene/protein
biosynthesis/ acquisition of amino acids
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU32240
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: ATP + L-homoserine = ADP + O-phospho-L-homoserine (according to Swiss-Prot)
- Protein family: Homoserine kinase subfamily (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- Structure: 3HUL (from Listeria monocytogenes, 41% identity, 61% similarity)
- UniProt: P04948
- KEGG entry: [2]
- E.C. number: 2.7.1.39
Additional information
Expression and regulation
- Regulation:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Allison Kriel, Shaun R Brinsmade, Jessica L Tse, Ashley K Tehranchi, Alycia N Bittner, Abraham L Sonenshein, Jue D Wang
GTP dysregulation in Bacillus subtilis cells lacking (p)ppGpp results in phenotypic amino acid auxotrophy and failure to adapt to nutrient downshift and regulate biosynthesis genes.
J Bacteriol: 2014, 196(1);189-201
[PubMed:24163341]
[WorldCat.org]
[DOI]
(I p)
Ulrike Mäder, Georg Homuth, Christian Scharf, Knut Büttner, Rüdiger Bode, Michael Hecker
Transcriptome and proteome analysis of Bacillus subtilis gene expression modulated by amino acid availability.
J Bacteriol: 2002, 184(15);4288-95
[PubMed:12107147]
[WorldCat.org]
[DOI]
(P p)
C Parsot
Evolution of biosynthetic pathways: a common ancestor for threonine synthase, threonine dehydratase and D-serine dehydratase.
EMBO J: 1986, 5(11);3013-9
[PubMed:3098560]
[WorldCat.org]
[DOI]
(P p)
