DapG

• Description: aspartokinase I (alpha and beta subunits)
  
  

Gene name	dapG
Synonyms	lssD
Essential	no
Product	aspartokinase I (alpha and beta subunits)
Function	biosynthesis of lysine and peptidoglycan
Gene expression levels in SubtiExpress: dapG
Metabolic function and regulation of this protein in SubtiPathways: dapG
MW, pI	42 kDa, 5.709
Gene length, protein length	1212 bp, 404 aa
Immediate neighbours	asd, dapA
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

cell wall synthesis, biosynthesis/ acquisition of amino acids, Biosynthesis of cell wall components, sporulation proteins

This gene is a member of the following regulons

SigK regulon

The gene

Basic information

• Locus tag: BSU16760

Database entries

• BsubCyc: BSU16760

• 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): LysC

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactors:

• Effectors of protein activity: inhibited by diaminopimelic acid PubMed

• Interactions:

• Localization:

Database entries

• BsubCyc: BSU16760

• Structure:

• UniProt: Q04795

• KEGG entry: [3]

• E.C. number: 2.7.2.4

Expression and regulation

• Operon:
  • spoVFA-spoVFB-asd-dapG-dapA PubMed
  • asd-dapG-dapA PubMed

• Expression browser: dapG PubMed

• Sigma factor:
  • spoVFA: SigK PubMed
  • asd: SigA PubMed

• Regulation:

• Regulatory mechanism:

• Additional information:
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 329 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 1108 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

Leif Steil, Mónica Serrano, Adriano O Henriques, Uwe Völker
Genome-wide analysis of temporally regulated and compartment-specific gene expression in sporulating cells of Bacillus subtilis.
Microbiology (Reading): 2005, 151(Pt 2);399-420
[PubMed:15699190] [WorldCat.org] [DOI] (P p)

R A Daniel, J Errington
Cloning, DNA sequence, functional analysis and transcriptional regulation of the genes encoding dipicolinic acid synthetase required for sporulation in Bacillus subtilis.
J Mol Biol: 1993, 232(2);468-83
[PubMed:8345520] [WorldCat.org] [DOI] (P p)

N Y Chen, S Q Jiang, D A Klein, H Paulus
Organization and nucleotide sequence of the Bacillus subtilis diaminopimelate operon, a cluster of genes encoding the first three enzymes of diaminopimelate synthesis and dipicolinate synthase.
J Biol Chem: 1993, 268(13);9448-65
[PubMed:8098035] [WorldCat.org] (P p)

J J Zhang, F M Hu, N Y Chen, H Paulus
Comparison of the three aspartokinase isozymes in Bacillus subtilis Marburg and 168.
J Bacteriol: 1990, 172(2);701-8
[PubMed:2153658] [WorldCat.org] [DOI] (P p)

L M Graves, R L Switzer
Aspartokinase III, a new isozyme in Bacillus subtilis 168.
J Bacteriol: 1990, 172(1);218-23
[PubMed:2152900] [WorldCat.org] [DOI] (P p)