Protein Family Models

The penicillin-binding proteins are bifunctional proteins consisting of transglycosylase and transpeptidase in the N- and C-terminus respectively [1]. The transglycosylase domain catalyses the polymerisation of murein glycan chains ([4]). [1]. 9244263. Topographical and functional investigation of Escherichia coli penicillin-binding protein 1b by alanine stretch scanning mutagenesis. F. Lefevre, M. H. Remy & J. M. Masson;. J Bacteriol 1997;179:4761-4767. [2]. 9614972. X-ray studies of enzymes that interact with penicillins. Kelly JA, Kuzin AP, Charlier P, Fonze E;. Cell Mol Life Sci 1998;54:353-358. [3]. 8830253. Monofunctional biosynthetic peptidoglycan transglycosylases. Spratt BG, Zhou J, Taylor M, Merrick MJ;. Mol Microbiol 1996;19:639-640. [4]. 12867450. The glycosyltransferase domain of penicillin-binding protein 2a from Streptococcus pneumoniae catalyzes the polymerization of murein glycan chains. Di Guilmi AM, Dessen A, Dideberg O, Vernet T;. J Bacteriol 2003;185:4418-4423. (from Pfam)

Date:

2024-10-16

This family is one of the transglycosylases involved in the late stages of peptidoglycan biosynthesis. Members tend to be small, about 240 amino acids in length, and consist almost entirely of a domain described by Pfam HMM PF00912 for transglycosylases. Species with this protein will have several other transglycosylases as well. All species with this protein are Proteobacteria that produce murein (peptidoglycan).

Gene:

mtgA

Date:

2024-06-27