Difference between revisions of "XepA"
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* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
| − | * '''Interactions:''' | + | * '''[[SubtInteract|Interactions]]:''' |
| − | * '''Localization:''' extracellular (no signal peptide) [http://www.ncbi.nlm.nih.gov/pubmed/18957862 PubMed] | + | * '''[[Localization]]:''' |
| + | ** extracellular (no signal peptide) [http://www.ncbi.nlm.nih.gov/pubmed/18957862 PubMed] | ||
=== Database entries === | === Database entries === | ||
Revision as of 21:39, 10 January 2012
- Description: PBSX prophage lytic exoenzyme
| Gene name | xepA |
| Synonyms | xkdY |
| Essential | no |
| Product | PBSX prophage lytic exoenzyme |
| Function | phage release |
| MW, pI | 30 kDa, 5.424 |
| Gene length, protein length | 837 bp, 279 aa |
| Immediate neighbours | xkdX, xhlA |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Contents
Categories containing this gene/protein
cell wall degradation/ turnover, PBSX prophage
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU12780
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
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:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
- extracellular (no signal peptide) PubMed
Database entries
- Structure:
- UniProt: P39797
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- 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
Birgit Voigt, Haike Antelmann, Dirk Albrecht, Armin Ehrenreich, Karl-Heinz Maurer, Stefan Evers, Gerhard Gottschalk, Jan Maarten van Dijl, Thomas Schweder, Michael Hecker
Cell physiology and protein secretion of Bacillus licheniformis compared to Bacillus subtilis.
J Mol Microbiol Biotechnol: 2009, 16(1-2);53-68
[PubMed:18957862]
[WorldCat.org]
[DOI]
(I p)
S Krogh, S T Jørgensen, K M Devine
Lysis genes of the Bacillus subtilis defective prophage PBSX.
J Bacteriol: 1998, 180(8);2110-7
[PubMed:9555893]
[WorldCat.org]
[DOI]
(P p)
P F Longchamp, C Mauël, D Karamata
Lytic enzymes associated with defective prophages of Bacillus subtilis: sequencing and characterization of the region comprising the N-acetylmuramoyl-L-alanine amidase gene of prophage PBSX.
Microbiology (Reading): 1994, 140 ( Pt 8);1855-67
[PubMed:7921239]
[WorldCat.org]
[DOI]
(P p)
