Difference between revisions of "DppA"
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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] | ||
− | * ''' | + | * '''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 This image was kindly provided by SubtiList
|
Contents
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
- Structure: 1HI9
- UniProt: P26902
- 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
- Regulatory mechanism: AbrB: transcription repression PubMed, CodY: transcription repression PubMed1 PubMed2
- 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)