Difference between revisions of "DppA"

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(References)
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* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1HI9 1HI9]
 
* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1HI9 1HI9]
  
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P26902 P26902]
+
* '''UniProt:''' [http://www.uniprot.org/uniprot/P26902 P26902]
  
 
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU12920]
 
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU12920]

Revision as of 12:03, 20 July 2009

  • Description: D-alanyl-aminopeptidase

Gene name dppA
Synonyms dciAA
Essential no
Product D-alanyl-aminopeptidase
Function degradation of cell wall peptides
MW, pI 30 kDa, 5.19
Gene length, protein length 822 bp, 274 aa
Immediate neighbours proG, dppB
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
DppA context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU12920

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: peptidase M55 family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: phosphorylated on ser/ thr/ tyr PubMed
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization:

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation: repressed by glucose (2.9-fold) PubMed, expressed postexponentially (AbrB) PubMed, repressed by CodY PubMed
    • repressed during growth in the presence of branched chain amino acids (CodY) PubMed
    • repressed during logrithmic growth (AbrB) PubMed
  • 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

Boris R Belitsky, Abraham L Sonenshein
Genetic and biochemical analysis of CodY-binding sites in Bacillus subtilis.
J Bacteriol: 2008, 190(4);1224-36
[PubMed:18083814] [WorldCat.org] [DOI] (I p)

Alain Lévine, Françoise Vannier, Cédric Absalon, Lauriane Kuhn, Peter Jackson, Elaine Scrivener, Valérie Labas, Joëlle Vinh, Patrick Courtney, Jérôme Garin, Simone J Séror
Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes.
Proteomics: 2006, 6(7);2157-73
[PubMed:16493705] [WorldCat.org] [DOI] (P p)

Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135] [WorldCat.org] [DOI] (P p)

Virginie Molle, Yoshiko Nakaura, Robert P Shivers, Hirotake Yamaguchi, Richard Losick, Yasutaro Fujita, Abraham L Sonenshein
Additional targets of the Bacillus subtilis global regulator CodY identified by chromatin immunoprecipitation and genome-wide transcript analysis.
J Bacteriol: 2003, 185(6);1911-22
[PubMed:12618455] [WorldCat.org] [DOI] (P p)

F J Slack, P Serror, E Joyce, A L Sonenshein
A gene required for nutritional repression of the Bacillus subtilis dipeptide permease operon.
Mol Microbiol: 1995, 15(4);689-702
[PubMed:7783641] [WorldCat.org] [DOI] (P p)

F J Slack, J P Mueller, M A Strauch, C Mathiopoulos, A L Sonenshein
Transcriptional regulation of a Bacillus subtilis dipeptide transport operon.
Mol Microbiol: 1991, 5(8);1915-25
[PubMed:1766371] [WorldCat.org] [DOI] (P p)