Characterization of domains of penicillin binding proteins of S. pneumo

In most bacteria, multiple proteins with 'amino acid sequence homology' to a transpeptidase exist. These proteins are almost always labeled as 'putative transpeptidases' (again, simply because of amino acid sequence homology). This way of identifying a protein without confirming their function by biochemical characterization or other direct method can be risky or misleading. In Mtb there are multiple proteins that are 'putative transpeptidases'. Many of them have not been studied beyond their sequence homology to a known protein. In this article authors characterize functional domains of two PBPs of S. pneumoniae. Similar studies of Mtb transpeptidases would greatly enhance our understanding of peptidoglycan biology in Mtb.