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L,D-transpeptidase C-terminal domain
This is the C-terminal domain found in d-transpeptidases (Ldt) homologues from E.coli. Three of these enzymes (YbiS, ErfK, YcfS) have been shown to cross-link Braun's lipoprotein to the peptidoglycan (PG), while the other two (YnhG, YcbB) form direct meso-diaminopimelate (DAP-DAP, or 3-3) cross-links within the PG. Family members include erfK (ldtA), ybiS (ldtB), ycfS (ldtC), and ynhG (ldtE). [1]. 23832002. Phenotypic analysis of Eschericia coli mutants lacking L,D-transpeptidases. Sanders AN, Pavelka MS;. Microbiology. 2013;159:1842-1852. (from Pfam)
L,D-transpeptidase family protein
This family of proteins are found in a range of bacteria. It has been shown that this domain can act as an L,D-transpeptidase that gives rise to an alternative pathway for peptidoglycan cross-linking [1]. This gives bacteria resistance to beta-lactam antibiotics that inhibit PBPs which usually carry out the cross-linking reaction. The conserved region contains a conserved histidine and cysteine, with the cysteine thought to be an active site residue. Several members of this family contain peptidoglycan binding domains. The molecular structure of YkuD protein shows this domain has a novel tertiary fold consisting of a beta-sandwich with two mixed sheets, one containing five strands and the other, six strands. The two beta-sheets form a cradle capped by an alpha-helix. This family was formerly called the ErfK/YbiS/YcfS/YnhG family, but is now named after the first protein of known structure. [1]. 16647082. Crystal structure of a novel beta-lactam-insensitive peptidoglycan transpeptidase. Biarrotte-Sorin S, Hugonnet JE, Delfosse V, Mainardi JL, Gutmann L, Arthur M, Mayer C;. J Mol Biol. 2006;359:533-538. (from Pfam)
L,D-transpeptidase
L,D-transpeptidase catalyzes the formation of 3--3 peptidoglycan cross-links
gene synonym: erfK
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