Difference between revisions of "AmiE"
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=Expression and regulation= | =Expression and regulation= | ||
| − | * '''Operon:''' | + | * '''Operon:''' ''[[murQ]]-[[murR]]-[[murP]]-[[amiE]]-[[nagZ]]-[[ybbC]]'' {{PubMed|22383849}} |
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ybbE_188408_189733_-1 amiE] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ybbE_188408_189733_-1 amiE] {{PubMed|22383849}} | ||
| Line 140: | Line 140: | ||
=References= | =References= | ||
| − | <pubmed>10627040, 20400549 </pubmed> | + | <pubmed>10627040, 20400549 22383849</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 16:19, 19 April 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
| |
Expression at a glance PubMed
| |
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
- Sigma factor:
- 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
Pierre Nicolas, Ulrike Mäder, Etienne Dervyn, Tatiana Rochat, Aurélie Leduc, Nathalie Pigeonneau, Elena Bidnenko, Elodie Marchadier, Mark Hoebeke, Stéphane Aymerich, Dörte Becher, Paola Bisicchia, Eric Botella, Olivier Delumeau, Geoff Doherty, Emma L Denham, Mark J Fogg, Vincent Fromion, Anne Goelzer, Annette Hansen, Elisabeth Härtig, Colin R Harwood, Georg Homuth, Hanne Jarmer, Matthieu Jules, Edda Klipp, Ludovic Le Chat, François Lecointe, Peter Lewis, Wolfram Liebermeister, Anika March, Ruben A T Mars, Priyanka Nannapaneni, David Noone, Susanne Pohl, Bernd Rinn, Frank Rügheimer, Praveen K Sappa, Franck Samson, Marc Schaffer, Benno Schwikowski, Leif Steil, Jörg Stülke, Thomas Wiegert, Kevin M Devine, Anthony J Wilkinson, Jan Maarten van Dijl, Michael Hecker, Uwe Völker, Philippe Bessières, Philippe Noirot
Condition-dependent transcriptome reveals high-level regulatory architecture in Bacillus subtilis.
Science: 2012, 335(6072);1103-6
[PubMed:22383849]
[WorldCat.org]
[DOI]
(I p)
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)
