Endolytic murein transglycosylase (also known as MltG, YrrL and YceG) functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation. The structure of E. coli MltG has been solved by X-ray crystallography (PDB: 2r1f). It has an extended N terminus topped by a globular head domain with an observable cleft where residues with the highest level of conservation are found [1].

Caution: This protein is often misannotated as aminodeoxychorismate lyase (PabC) due to the promiximty to PabC in numerous proteobacteria.

1. Identification of MltG as a potential terminase for peptidoglycan polymerization in bacteria. Mol. Microbiol. 99, 700-18

Endolytic murein transglycosylase (also known as MltG, YrrL and YceG) functions as a peptidoglyca
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