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Penicillin-binding protein OB-like domain
transglycosylase domain-containing protein
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)
penicillin-binding transpeptidase domain-containing protein
The active site serine (residue 337 in Swiss:P14677) is conserved in all members of this family. [1]. 8605631. X-ray structure of Streptococcus pneumoniae PBP2x, a primary. penicillin target enzyme.. Pares S, Mouz N, Petillot Y, Hakenbeck R, Dideberg O. Nat Struct Biol 1996;3:284-289. (from Pfam)
peptidoglycan glycosyltransferase/peptidoglycan DD-transpeptidase MrcA
PBP1A family penicillin-binding protein
Bacterial that synthesize a cell wall of peptidoglycan (murein) generally have several transglycosylases and transpeptidases for the task. This family consists of bifunctional transglycosylase/transpeptidase penicillin-binding proteins (PBP). In the Proteobacteria, this family includes PBP 1A but not the paralogous PBP 1B (TIGR02071). This family also includes related proteins, often designated PBP 1A, from other bacterial lineages.
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