Difference between revisions of "LysC"

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(Orginal Publications)
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<pubmed> 19946135 </pubmed>
 
<pubmed> 19946135 </pubmed>
 
==Orginal Publications==
 
==Orginal Publications==
<pubmed>2168395,1624109,14523230,2559145,14597663,2557260,,12850135 12107147, 14523230, 12850135, 12107147, 17981983 19636616 21169337 </pubmed>
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<pubmed>2168395,1624109,14523230,2559145,14597663,2557260,,12850135 12107147, 14523230, 12850135, 12107147, 17981983 19636616 21169337 22416067 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 15:05, 16 March 2012

  • 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







Categories containing this gene/protein

biosynthesis/ acquisition of amino acids

This gene is a member of the following regulons

L-box

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): DapG

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

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

  • 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

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Orginal Publications