Difference between revisions of "DapG"

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|style="background:#ABCDEF;" align="center"|'''Function''' || biosynthesis of lysine and peptidoglycan  
 
|style="background:#ABCDEF;" align="center"|'''Function''' || biosynthesis of lysine and peptidoglycan  
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://cellpublisher.gobics.de/subtiexpress/ ''Subti''Express]''': [http://cellpublisher.gobics.de/subtiexpress/bsu/BSU16760 dapG]
 
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/lys_threo.html Lys, Thr]'''
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/lys_threo.html Lys, Thr]'''

Revision as of 09:53, 7 August 2012

  • 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:
Lys, Thr
MW, pI 42 kDa, 5.709
Gene length, protein length 1212 bp, 404 aa
Immediate neighbours asd, dapA
Get the DNA and protein sequences
(Barbe et al., 2009)
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

biosynthesis/ acquisition of amino acids, 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:
  • Domains:
  • Modification:
  • Cofactor(s):
  • 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:

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)

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)