Difference between revisions of "AmiE"
| Line 1: | Line 1: | ||
| − | * '''Description:''' | + | * '''Description:''' N-acetylmuramyl-L-alanine amidase <br/><br/> |
{| align="right" border="1" cellpadding="2" | {| align="right" border="1" cellpadding="2" | ||
| Line 10: | Line 10: | ||
|style="background:#ABCDEF;" align="center"| '''Essential''' || no | |style="background:#ABCDEF;" align="center"| '''Essential''' || no | ||
|- | |- | ||
| − | |style="background:#ABCDEF;" align="center"| '''Product''' || | + | |style="background:#ABCDEF;" align="center"| '''Product''' || N-acetylmuramyl-L-alanine amidase |
|- | |- | ||
| − | |style="background:#ABCDEF;" align="center"|'''Function''' || | + | |style="background:#ABCDEF;" align="center"|'''Function''' || recycling of cell wall material |
|- | |- | ||
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 49 kDa, 9.349 | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 49 kDa, 9.349 | ||
| Line 18: | Line 18: | ||
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1323 bp, 441 aa | |style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1323 bp, 441 aa | ||
|- | |- | ||
| − | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ | + | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[nagZ]]'', ''[[murP]]'' |
|- | |- | ||
|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+[EMBLCDS:CAB11943]+-newId sequences] <br/> (Barbe ''et al.'', 2009)''' | |colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+[EMBLCDS:CAB11943]+-newId sequences] <br/> (Barbe ''et al.'', 2009)''' | ||
| Line 54: | Line 54: | ||
=== Basic information/ Evolution === | === Basic information/ Evolution === | ||
| − | * '''Catalyzed reaction/ biological activity:''' | + | * '''Catalyzed reaction/ biological activity:''' hydrolyzes the amide bond between MurNAc and the L-alanine residue of the stem peptide {{PubMed|20400549}} |
* '''Protein family:''' UPF0214 family (according to Swiss-Prot) | * '''Protein family:''' UPF0214 family (according to Swiss-Prot) | ||
| Line 120: | Line 120: | ||
=References= | =References= | ||
| − | <pubmed>10627040, </pubmed> | + | <pubmed>10627040, 20400549 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 16:55, 20 April 2010
- Description: N-acetylmuramyl-L-alanine amidase
| Gene name | ybbE |
| Synonyms | |
| Essential | no |
| Product | N-acetylmuramyl-L-alanine amidase |
| Function | recycling of cell wall material |
| 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
| |
Contents
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:
- Interactions:
- Localization:
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)
