LysC

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  • 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
Metabolic function and regulation of this protein in SubtiPathways:
Lys, Thr
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
LysC context.gif
This image was kindly provided by SubtiList







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:
  • KEGG entry: [3]

Additional information

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

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)

Narasimhan Sudarsan, J Kenneth Wickiser, Shingo Nakamura, Margaret S Ebert, Ronald R Breaker
An mRNA structure in bacteria that controls gene expression by binding lysine.
Genes Dev.: 2003, 17(21);2688-97
[PubMed:14597663] [WorldCat.org] [DOI] (P 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] (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)

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)