Summary: A γ-D-glutamate--diaminopimelate muropeptidase was detected in the vegetative growth phase of 168. It is encoded by the monocistronic operon expressed by the alternative vegetative sigma factor, σ. Sequence analysis of LytF revealed two domains, an organization common to exoproteins of as well as to those from other organisms. The N-terminal domain contains a fivefold-repeated motif attributed to cell wall binding, whilst the C-terminal domain is probably endowed with the catalytic activity. Overrexpression of LytF allowed its purification and biochemical characterization. Inactivation of led to the loss of the cell-wall-bound protein 49′ (CWBP49′) and of the corresponding lytic activity as revealed by renaturation gel assay. Native cell walls prepared from the multiple -deficient mutant did not exhibit any autolysis, whereas walls prepared from a strain endowed with LytF but not with the other three enzymes underwent a slight lysis. Analysis of degradation products of cell wall devoid of teichoic-acid-bound -esterified D-alanine unambiguously confirmed that LytF cuts the γ-D-glutamate--diaminopimelate bond.


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