Difference between revisions of "DapG"

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==Original publications==
 
==Original publications==
<pubmed>8345520,,15699190 8098035,2152900 , </pubmed>
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<pubmed>8345520,2153658 ,15699190 8098035,2152900 , </pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 15:31, 19 May 2015

  • 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
DapG context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
DapG expression.png















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

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): LysC

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity: inhibited by diaminopimelic acid PubMed

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • 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:

Labs working on this gene/protein

Your additional remarks

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)