MraY

• 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
Metabolic function and regulation of this protein in SubtiPathways: Cell wall
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

The gene

Basic information

• Locus tag: BSU15190

Phenotypes of a mutant

essential PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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

Expression and regulation

• Operon: murE-mraY-murD-spoVE-murG-murB-divIB-ylxW-ylxX-sbp

• Sigma factor: SigE

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Yi Zheng, Douglas K Struck, Thomas G Bernhardt, Ry Young
Genetic analysis of MraY inhibition by the phiX174 protein E.
Genetics: 2008, 180(3);1459-66
[PubMed:18791230] [WorldCat.org] [DOI] (P p)

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)

Ahmed Bouhss, Amy E Trunkfield, Timothy D H Bugg, Dominique Mengin-Lecreulx
The biosynthesis of peptidoglycan lipid-linked intermediates.
FEMS Microbiol Rev: 2008, 32(2);208-33
[PubMed:18081839] [WorldCat.org] [DOI] (P p)

Ahmed Bouhss, Muriel Crouvoisier, Didier Blanot, Dominique Mengin-Lecreulx
Purification and characterization of the bacterial MraY translocase catalyzing the first membrane step of peptidoglycan biosynthesis.
J Biol Chem: 2004, 279(29);29974-80
[PubMed:15131133] [WorldCat.org] [DOI] (P p)

M A Lehrman
A family of UDP-GlcNAc/MurNAc: polyisoprenol-P GlcNAc/MurNAc-1-P transferases.
Glycobiology: 1994, 4(6);768-71
[PubMed:7734839] [WorldCat.org] [DOI] (P p)

R A Daniel, J Errington
DNA sequence of the murE-murD region of Bacillus subtilis 168.
J Gen Microbiol: 1993, 139(2);361-70
[PubMed:8436954] [WorldCat.org] [DOI] (P 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