Difference between revisions of "XlyA"
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* '''[[Domains]]:''' | * '''[[Domains]]:''' | ||
− | ** contains | + | ** contains a N-acetylglucosamine-polymer-binding [[LysM domain]] {{PubMed|18430080}} |
** contains an amidase_2 domain (like [[BlyA]], [[CwlA]], [[CwlH]], [[XlyB]]) | ** contains an amidase_2 domain (like [[BlyA]], [[CwlA]], [[CwlH]], [[XlyB]]) | ||
Revision as of 14:53, 27 December 2013
- Description: N-acetylmuramoyl-L-alanine amidase
Gene name | xlyA |
Synonyms | |
Essential | no |
Product | N-acetylmuramoyl-L-alanine amidase |
Function | PBSX prophage-mediated lysis |
Gene expression levels in SubtiExpress: xlyA | |
MW, pI | 31 kDa, 5.342 |
Gene length, protein length | 891 bp, 297 aa |
Immediate neighbours | xhlB, spoIISB |
Sequences | Protein DNA DNA_with_flanks |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
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: BSU12810
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides (according to Swiss-Prot)
- Protein family: LysM repeat (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
- Localization:
- extracellular (no signal peptide) PubMed
Database entries
- UniProt: P39800
- KEGG entry: [2]
- E.C. number: 3.5.1.28
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
Reviews
Original publications