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

Reviews

Chien-Chi Lo, Carol A Bonner, Gary Xie, Mark D'Souza, Roy A Jensen
Cohesion group approach for evolutionary analysis of aspartokinase, an enzyme that feeds a branched network of many biochemical pathways.
Microbiol Mol Biol Rev: 2009, 73(4);594-651
[PubMed:19946135] [WorldCat.org] [DOI] (I p)

Original Publications

The L-box riboswitch

Larry R Fiegland, Andrew D Garst, Robert T Batey, David J Nesbitt
Single-molecule studies of the lysine riboswitch reveal effector-dependent conformational dynamics of the aptamer domain.
Biochemistry: 2012, 51(45);9223-33
[PubMed:23067368] [WorldCat.org] [DOI] (I p)

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)