LysC

From SubtiWiki
Revision as of 20:08, 8 June 2009 by Sroppel (talk | contribs)
Jump to: navigation, search
  • 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
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)

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)


  1. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed