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
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 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

Database entries

• 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:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• 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

• 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

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Original Publications

The L-box riboswitch

Sharnise N Wilson-Mitchell, Frank J Grundy, Tina M Henkin
Analysis of lysine recognition and specificity of the Bacillus subtilis L box riboswitch.
Nucleic Acids Res: 2012, 40(12);5706-17
[PubMed:22416067] [WorldCat.org] [DOI] (I p)

Simon Blouin, Raja Chinnappan, Daniel A Lafontaine
Folding of the lysine riboswitch: importance of peripheral elements for transcriptional regulation.
Nucleic Acids Res: 2011, 39(8);3373-87
[PubMed:21169337] [WorldCat.org] [DOI] (I p)

Trang Thi Phuong Phan, Wolfgang Schumann
Transcriptional analysis of the lysine-responsive and riboswitch-regulated lysC gene of Bacillus subtilis.
Curr Microbiol: 2009, 59(4);463-8
[PubMed:19636616] [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)