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MurT ligase domain-containing protein
This entry represents the C-terminal domain of MurT ligase from Gram-positive bacteria. MurT is part of the bi-enzymatic complex MurT-GatD involved in the amidation of the alpha-carboxyl group of the D-isoglutamate residue in Lipid II in the peptidoglycan layer to produce D-isoglutamine. This domain contains an aspartate at position 349, the third residue in the catalytic triad GatD-C94, GatD-H189, MurT-D349. This C-terminal domain is built around a central six-stranded, predominantly parallel beta-sheet that is sandwiched between four alpha-helices on one side and two alpha-helices on the other. The MurT-GatD heterodimer adopts a boomerang-shaped conformation, with GatD packing against the C-terminal domain of MurT [1]. [1]. 30154570. Structural basis of cell wall peptidoglycan amidation by the. GatD/MurT complex of Staphylococcus aureus.. Noldeke ER, Muckenfuss LM, Niemann V, Muller A, Stork E, Zocher. G, Schneider T, Stehle T;. Sci Rep. 2018;8:12953. (from Pfam)
Mur ligase family protein
This HMM hits multiple proteins of peptidoglycan (murein) biosynthesis, such as MurC, MurD, MurE, and MurF of Escherichia coli.
Mur ligase family protein such as MurC, MurD, and MurE, which catalyze consecutive steps in the synthesis of peptidoglycan
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