LysC

• 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
Gene expression levels in SubtiExpress: lysC
Metabolic function and regulation of this protein in SubtiPathways: lysC
MW, pI	43 kDa, 4.643
Gene length, protein length	1224 bp, 408 aa
Immediate neighbours	yslB, uvrC
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

biosynthesis/ acquisition of amino acids, most abundant proteins

This gene is a member of the following regulons

L-box

The gene

Basic information

• Locus tag: BSU28470

Database entries

• BsubCyc: BSU28470

• DBTBS entry: [1]

• SubtiList entry: [2]

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): DapG

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactors:

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• BsubCyc: BSU28470

• Structure: 2RE1 (from Neisseria meningitidis mc58, 40% identity, 58% similarity)

• UniProt: P08495

• KEGG entry: [3]

• E.C. number: 2.7.2.4

Additional information

• subject to Clp-dependent proteolysis upon glucose starvation PubMed, also degraded upon ammonium or amino acid starvation PubMed

Expression and regulation

• Operon: lysC PubMed

• Expression browser: lysC PubMed

• Sigma factor:

• Regulation:
  • repressed in the presence of lysine (L-box) PubMed
  • 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 PubMed

• Additional information:
  • subject to Clp-dependent proteolysis upon glucose starvation PubMed, also degraded upon ammonium or amino acid starvation PubMed
  • belongs to the 100 most abundant proteins PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 1459 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 4406 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 1282 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 806 PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Original Publications

Other original Publications

Junming Wang, Dongfang Gao, Xiaoli Yu, Wen Li, Qingsheng Qi
Evolution of a chimeric aspartate kinase for L-lysine production using a synthetic RNA device.
Appl Microbiol Biotechnol: 2015, 99(20);8527-36
[PubMed:25935345] [WorldCat.org] [DOI] (I p)

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)

Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759] [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)

Y Lu, T N Shevtchenko, H Paulus
Fine-structure mapping of cis-acting control sites in the lysC operon of Bacillus subtilis.
FEMS Microbiol Lett: 1992, 71(1);23-7
[PubMed:1624109] [WorldCat.org] [DOI] (P p)

L M Graves, R L Switzer
Aspartokinase II from Bacillus subtilis is degraded in response to nutrient limitation.
J Biol Chem: 1990, 265(25);14947-55
[PubMed:2168395] [WorldCat.org] (P p)

J J Zhang, F M Hu, N Y Chen, H Paulus
Comparison of the three aspartokinase isozymes in Bacillus subtilis Marburg and 168.
J Bacteriol: 1990, 172(2);701-8
[PubMed:2153658] [WorldCat.org] [DOI] (P p)

N Y Chen, J J Zhang, H Paulus
Chromosomal location of the Bacillus subtilis aspartokinase II gene and nucleotide sequence of the adjacent genes homologous to uvrC and trx of Escherichia coli.
J Gen Microbiol: 1989, 135(11);2931-40
[PubMed:2559145] [WorldCat.org] [DOI] (P p)

M Petricek, L Rutberg, L Hederstedt
The structural gene for aspartokinase II in Bacillus subtilis is closely linked to the sdh operon.
FEMS Microbiol Lett: 1989, 52(1-2);85-7
[PubMed:2557260] [WorldCat.org] [DOI] (P p)