Difference between revisions of "MraY"

From SubtiWiki
Jump to: navigation, search
Line 120: Line 120:
 
=References=
 
=References=
  
 +
<pubmed>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]  
 
# 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
MraY context.gif
This image was kindly provided by SubtiList



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:
  • KEGG entry: [3]

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)

  1. 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
  2. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed