Difference between revisions of "MraY"

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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU15190&redirect=T BSU15190]
  
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/murE-mraY-murD-spoVE-murG-murB-divIB-ylxWX-sbp.html]
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/murE-mraY-murD-spoVE-murG-murB-divIB-ylxWX-sbp.html]
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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU15190&redirect=T BSU15190]
  
 
* '''Structure:'''
 
* '''Structure:'''

Revision as of 13:38, 2 April 2014

  • Description: phospho-N-acetylmuramoyl-pentapeptide-transferase (meso-2,6-diaminopimelate), catalyzes the first commited membrane-bound step of bacterial peptidoglycan synthesis leading to the formation of lipid I

Gene name mraY
Synonyms
Essential yes PubMed
Product phospho-N-acetylmuramoyl-pentapeptide-transferase
(meso-2,6-diaminopimelate)
Function peptidoglycan precursor biosynthesis
Gene expression levels in SubtiExpress: mraY
Metabolic function and regulation of this protein in SubtiPathways:
mraY
MW, pI 35 kDa, 8.966
Gene length, protein length 972 bp, 324 aa
Immediate neighbours murE, murD
Sequences Protein DNA DNA_with_flanks
Genetic context
MraY context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
MraY expression.png















Categories containing this gene/protein

cell wall synthesis, biosynthesis of cell wall components, essential genes, membrane proteins

This gene is a member of the following regulons

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:

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • expressed during vegatative growth PubMed
  • 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

Yi Ma, Daniela Münch, Tanja Schneider, Hans-Georg Sahl, Ahmed Bouhss, Umesh Ghoshdastider, Jufang Wang, Volker Dötsch, Xiaoning Wang, Frank Bernhard
Preparative scale cell-free production and quality optimization of MraY homologues in different expression modes.
J Biol Chem: 2011, 286(45);38844-53
[PubMed:21937437] [WorldCat.org] [DOI] (I p)

Delphine Lecerclé, Anthony Clouet, Bayan Al-Dabbagh, Muriel Crouvoisier, Ahmed Bouhss, Christine Gravier-Pelletier, Yves Le Merrer
Bacterial transferase MraY inhibitors: synthesis and biological evaluation.
Bioorg Med Chem: 2010, 18(12);4560-9
[PubMed:20537545] [WorldCat.org] [DOI] (I p)

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)

A A Branstrom, S Midha, C B Longley, K Han, E R Baizman, H R Axelrod
Assay for identification of inhibitors for bacterial MraY translocase or MurG transferase.
Anal Biochem: 2000, 280(2);315-9
[PubMed:10790316] [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)

A O Henriques, H de Lencastre, P J Piggot
A Bacillus subtilis morphogene cluster that includes spoVE is homologous to the mra region of Escherichia coli.
Biochimie: 1992, 74(7-8);735-48
[PubMed:1391053] [WorldCat.org] [DOI] (P p)