InterPro domain: IPR004268

Peptidoglycan synthesis (PG) biosynthesis involves the formation of peptidoglycan precursor lipid II (undecaprenyl-pyrophosphate-linked N-acetyl glucosamine-N-acetyl muramic acid-pentapeptide) on the cytosolic face of the cell membrane. Lipid II is then translocated across the membrane and its glycopeptide moiety becomes incorporated into the growing cell wall mesh.

MviN, renamed as MurJ, is a lipid II flippase essential for cell wall peptidoglycan synthesis [ 1 , 2 ]. Unlike most MviN proteins, the mycobacterial MviN orthologue possess an extended C-terminal region that contains an intracellular pseudo-kinase domain and an extracellular domain resembling carbohydrate-binding proteins [ 3 ].

1. Bioinformatics identification of MurJ (MviN) as the peptidoglycan lipid II flippase in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 105, 15553-7
2. A Burkholderia cenocepacia MurJ (MviN) homolog is essential for cell wall peptidoglycan synthesis and bacterial viability. Glycobiology 24, 564-76
3. A phosphorylated pseudokinase complex controls cell wall synthesis in mycobacteria. Sci Signal 5, ra7