Difference between revisions of "DppA"
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|style="background:#ABCDEF;" align="center"| '''Product''' || D-alanyl-aminopeptidase | |style="background:#ABCDEF;" align="center"| '''Product''' || D-alanyl-aminopeptidase | ||
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− | |style="background:#ABCDEF;" align="center"|'''Function''' || | + | |style="background:#ABCDEF;" align="center"|'''Function''' || degradation of cell wall peptides |
|- | |- | ||
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 30 kDa, 5.19 | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 30 kDa, 5.19 |
Revision as of 11:15, 8 April 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 |
Gene sequence (+200bp) | Protein sequence |
Caution: The sequence for this gene in SubtiList contains errors | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Coordinates:
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:
- 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:
- Swiss prot entry:
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Regulation: repressed by glucose (2.9-fold) PubMed
- 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
- Blencke et al. (2003) Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways. Metab Eng. 5: 133-149 PubMed
- Lévine et al. (2006) Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes. Proteomics 6: 2157-2173 PubMed
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed