Difference between revisions of "MraY"
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# Al-Dabbagh B, Henry X, El Ghachi M, Auger G, Blanot D, Parquet C, Mengin-Lecreulx D, Bouhss A. (2008) Active site mapping of MraY, a member of the polyprenyl-phosphate N-acetylhexosamine 1-phosphate transferase superfamily, catalyzing the first membrane step of peptidoglycan biosynthesis. ''Biochemistry.'' '''Aug 26;47(34):''' 8919-28. [http://www.ncbi.nlm.nih.gov/sites/entrez/18672909 PubMed] | # Al-Dabbagh B, Henry X, El Ghachi M, Auger G, Blanot D, Parquet C, Mengin-Lecreulx D, Bouhss A. (2008) Active site mapping of MraY, a member of the polyprenyl-phosphate N-acetylhexosamine 1-phosphate transferase superfamily, catalyzing the first membrane step of peptidoglycan biosynthesis. ''Biochemistry.'' '''Aug 26;47(34):''' 8919-28. [http://www.ncbi.nlm.nih.gov/sites/entrez/18672909 PubMed] | ||
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed] | # Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed] | ||
Revision as of 20:11, 8 June 2009
- Description: phospho-N-acetylmuramoyl-pentapeptide-transferase (meso-2,6-diaminopimelate)
| Gene name | mraY |
| Synonyms | |
| Essential | yes PubMed |
| Product | phospho-N-acetylmuramoyl-pentapeptide-transferase (meso-2,6-diaminopimelate) |
| Function | peptidoglycan precursor biosynthesis |
| MW, pI | 35 kDa, 8.966 |
| Gene length, protein length | 972 bp, 324 aa |
| Immediate neighbours | murE, murD |
| 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: BSU15190
Phenotypes of a mutant
essential PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate = UMP + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol (according to Swiss-Prot)
- Protein family: MraY subfamily (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: cell membrane (according to Swiss-Prot)
Database entries
- Structure:
- Swiss prot entry: Q03521
- KEGG entry: [3]
- E.C. number: 2.7.8.13
Additional information
Expression and regulation
- 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
Bayan Al-Dabbagh, Xavier Henry, Meriem El Ghachi, Geneviève Auger, Didier Blanot, Claudine Parquet, Dominique Mengin-Lecreulx, Ahmed Bouhss
Active site mapping of MraY, a member of the polyprenyl-phosphate N-acetylhexosamine 1-phosphate transferase superfamily, catalyzing the first membrane step of peptidoglycan biosynthesis.
Biochemistry: 2008, 47(34);8919-28
[PubMed:18672909]
[WorldCat.org]
[DOI]
(I p)
- Al-Dabbagh B, Henry X, El Ghachi M, Auger G, Blanot D, Parquet C, Mengin-Lecreulx D, Bouhss A. (2008) Active site mapping of MraY, a member of the polyprenyl-phosphate N-acetylhexosamine 1-phosphate transferase superfamily, catalyzing the first membrane step of peptidoglycan biosynthesis. Biochemistry. Aug 26;47(34): 8919-28. PubMed
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed
