|PROSITE documentation PDOC01046 [for PROSITE entry PS01348]|
Phospho-N-acetylmuramoyl-pentapeptide-transferase (EC 184.108.40.206) (mraY)  is a bacterial enzyme responsible for the formation of the first lipid intermediate of the cell wall peptidoglycan synthesis. It catalyzes the formation of undecaprenyl-pyrophosphoryl-N-acetylmuramoyl-pentapeptide from UDP-MurNAc-pentapeptide and undecaprenyl-phosphate.
It is an integral membrane protein with probably ten transmembrane domains. It belongs to family 4 of glycosyl transferases. Homologs of mraY have been found in the archaebacteria Methanobacterium thermoautotrophicum and in Arabidopsis thaliana.
We developed two patterns for this family of enzyme. The first one is located at the end of the first cytoplasmic loop and the beginning of the second transmembrane domain. The second pattern is located in the third cytoplasmic loop.Expert(s) to contact by email:
April 2006 / Pattern revised.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Bouhss A. Mengin-Lecreulx D. Le Beller D. Van Heijenoort J.|
|Title||Topological analysis of the MraY protein catalysing the first membrane step of peptidoglycan synthesis.|
|Source||Mol. Microbiol. 34:576-585(1999).|