Difference between revisions of "AmiE"
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* '''Locus tag:''' BSU01670 | * '''Locus tag:''' BSU01670 | ||
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| + | [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ybbE_188408_189733_-1 Expression] | ||
===Phenotypes of a mutant === | ===Phenotypes of a mutant === | ||
Revision as of 12:41, 24 January 2012
- Description: N-acetylmuramyl-L-alanine amidase
| Gene name | amiE |
| Synonyms | ybbE |
| Essential | no |
| Product | N-acetylmuramyl-L-alanine amidase |
| Function | recycling of cell wall material |
| Metabolic function and regulation of this protein in SubtiPathways: Murein recycling | |
| MW, pI | 49 kDa, 9.349 |
| Gene length, protein length | 1323 bp, 441 aa |
| Immediate neighbours | nagZ, murP |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
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Contents
Categories containing this gene/protein
cell wall degradation/ turnover
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU01670
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 amide bond between MurNAc and the L-alanine residue of the stem peptide PubMed
- Protein family: UPF0214 family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure:
- UniProt: O05213
- 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
Silke Litzinger, Amanda Duckworth, Katja Nitzsche, Christian Risinger, Valentin Wittmann, Christoph Mayer
Muropeptide rescue in Bacillus subtilis involves sequential hydrolysis by beta-N-acetylglucosaminidase and N-acetylmuramyl-L-alanine amidase.
J Bacteriol: 2010, 192(12);3132-43
[PubMed:20400549]
[WorldCat.org]
[DOI]
(I p)
Jonathan Reizer, Steffi Bachem, Aiala Reizer, Maryvonne Arnaud, Milton H Saier, Jörg Stülke
Novel phosphotransferase system genes revealed by genome analysis - the complete complement of PTS proteins encoded within the genome of Bacillus subtilis.
Microbiology (Reading): 1999, 145 ( Pt 12);3419-3429
[PubMed:10627040]
[WorldCat.org]
[DOI]
(P p)
