Difference between revisions of "LysC"
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− | <pubmed> 14523230, 12850135, 12107147, 17981983 </pubmed> | + | <pubmed>12850135 12107147, 14523230, 12850135, 12107147, 17981983 </pubmed> |
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed] | # Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed] |
Revision as of 20:08, 8 June 2009
- Description: aspartokinase II (alpha and beta subunits)
Gene name | lysC |
Synonyms | ask, aecA |
Essential | no |
Product | aspartokinase II (alpha and beta subunits) |
Function | biosynthesis of lysine |
MW, pI | 43 kDa, 4.643 |
Gene length, protein length | 1224 bp, 408 aa |
Immediate neighbours | yslB, ask |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU28470
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-aspartate = ADP + 4-phospho-L-aspartate (according to Swiss-Prot)
- Protein family: aspartokinase family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure:
- Swiss prot entry: P08495
- KEGG entry: [3]
- E.C. number: 2.7.2.4
Additional information
Expression and regulation
- Operon:
- Regulation:
- repressed in the presence of lysine (L-box)
'** expression activated by glucose (5.4 fold) PubMed
- repressed by casamino acids PubMed
- Regulatory mechanism:
- L-box: a riboswich that mediates transcription terimnation antitermination control
- Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed, also degraded upon ammonium or amino acid 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
Ulf Gerth, Holger Kock, Ilja Kusters, Stephan Michalik, Robert L Switzer, Michael Hecker
Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis.
J Bacteriol: 2008, 190(1);321-31
[PubMed:17981983]
[WorldCat.org]
[DOI]
(I p)
Frank J Grundy, Susan C Lehman, Tina M Henkin
The L box regulon: lysine sensing by leader RNAs of bacterial lysine biosynthesis genes.
Proc Natl Acad Sci U S A: 2003, 100(21);12057-62
[PubMed:14523230]
[WorldCat.org]
[DOI]
(P p)
Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135]
[WorldCat.org]
[DOI]
(P 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)
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed