EC 3.1.1.103     
Accepted name: teichoic acid D-alanine hydrolase
Reaction: [(4-D-Ala)-(2-GlcNAc)-Rib-ol-P]n-[Gro-P]m-β-D-ManNAc-(1→4)-α-D-GlcNAc-P-peptidoglycan + n H2O = [(2-GlcNAc)-Rib-ol-P]n-[Gro-P]m-β-D-ManNAc-(1→4)-α-D-GlcNAc-P-peptidoglycan + n D-alanine
Glossary: Rib-ol = ribitol
Other name(s): fmtA (gene name)
Systematic name: teichoic acid D-alanylhydrolase
Comments: The enzyme, characterized from the bacterium Staphylococcus aureus, removes D-alanine groups from the teichoic acid produced by this organism, thus modulating the electrical charge of the bacterial surface. The activity greatly increases methicillin resistance in MRSA strains.
References:
1.  Komatsuzawa, H., Sugai, M., Ohta, K., Fujiwara, T., Nakashima, S., Suzuki, J., Lee, C.Y. and Suginaka, H. Cloning and characterization of the fmt gene which affects the methicillin resistance level and autolysis in the presence of triton X-100 in methicillin-resistant Staphylococcus aureus. Antimicrob. Agents Chemother. 41 (1997) 2355–2361. [PMID: 9371333]
2.  Qamar, A. and Golemi-Kotra, D. Dual roles of FmtA in Staphylococcus aureus cell wall biosynthesis and autolysis. Antimicrob. Agents Chemother. 56 (2012) 3797–3805. [PMID: 22564846]
3.  Rahman, M.M., Hunter, H.N., Prova, S., Verma, V., Qamar, A. and Golemi-Kotra, D. The Staphylococcus aureus methicillin resistance factor FmtA is a D-amino esterase that acts on teichoic acids. MBio 7 (2016) e02070. [PMID: 26861022]
[EC 3.1.1.103 created 2018]