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Mur ligase family protein
This HMM hits multiple proteins of peptidoglycan (murein) biosynthesis, such as MurC, MurD, MurE, and MurF of Escherichia coli.
glutamate ligase domain-containing protein
This family contains a number of related ligase enzymes which have EC numbers 6.3.2.*. This family includes: MurC (Swiss:P17952), MurD (Swiss:P14900), MurE (Swiss:P22188), MurF (Swiss:P11880), Mpl (Swiss:P37773) and FolC (Swiss:P08192). MurC, MurD, Mure and MurF catalyse consecutive steps in the synthesis of peptidoglycan. Peptidoglycan consists of a sheet of two sugar derivatives, with one of these N-acetylmuramic acid attaching to a small pentapeptide. The pentapeptide is is made of L-alanine, D-glutamic acid, Meso-diaminopimelic acid and D-alanyl alanine. The peptide moiety is synthesised by successively adding these amino acids to UDP-N-acetylmuramic acid. MurC transfers the L-alanine, MurD transfers the D-glutamate, MurE transfers the diaminopimelic acid, and MurF transfers the D-alanyl alanine. This family also includes Folylpolyglutamate synthase that transfers glutamate to folylpolyglutamate. [1]. 9218784. Crystal structure of UDP-N-acetylmuramoyl-L-alanine:D-glutamate. ligase from Escherichia coli.. Bertrand JA, Auger G, Fanchon E, Martin L, Blanot D, van. Heijenoort J, Dideberg O;. EMBO J 1997;16:3416-3425. (from Pfam)
Mur ligase domain-containing protein
UDP-N-acetylmuramate--L-alanine ligase
UDP-N-acetylmuramate--L-alanine ligase catalyzes the addition of the first amino acid to the cytoplasmic precursor of the bacterial cell wall peptidoglycan
This HMM describes the MurC protein in bacterial peptidoglycan (murein) biosynthesis. In a few species (Mycobacterium leprae, the Chlamydia), the amino acid may be L-serine or glycine instead of L-alanine. A related protein, UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase (murein tripeptide ligase) is described by HMM TIGR01081.
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