{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,18]],"date-time":"2026-09-18T18:20:44Z","timestamp":1789755644914,"version":"4.0.1"},"reference-count":56,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2017,8,29]],"date-time":"2017-08-29T00:00:00Z","timestamp":1503964800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000268","name":"Biotechnology and Biological Sciences Research Council","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000268","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[2017,10]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p>Bacterial cell division involves the dynamic assembly of a diverse set of proteins that coordinate the invagination of the cell membrane and synthesis of cell wall material to create the new cell poles of the separated daughter cells. Penicillin\u2010binding protein PBP 2B is a key cell division protein in <jats:italic>Bacillus subtilis<\/jats:italic> proposed to have a specific catalytic role in septal wall synthesis. Unexpectedly, we find that a catalytically inactive mutant of PBP 2B supports cell division, but in this background the normally dispensable PBP 3 becomes essential. Phenotypic analysis of <jats:italic>pbpC<\/jats:italic> mutants (encoding PBP 3) shows that PBP 2B has a crucial structural role in assembly of the division complex, independent of catalysis, and that its biochemical activity in septum formation can be provided by PBP 3. Bioinformatic analysis revealed a close sequence relationship between PBP 3 and <jats:italic>Staphylococcus aureus<\/jats:italic> PBP 2A, which is responsible for methicillin resistance. These findings suggest that mechanisms for rescuing cell division when the biochemical activity of PBP 2B is perturbed evolved prior to the clinical use of \u03b2\u2010lactams.<\/jats:p>","DOI":"10.1111\/mmi.13765","type":"journal-article","created":{"date-parts":[[2017,8,9]],"date-time":"2017-08-09T10:36:39Z","timestamp":1502274999000},"page":"304-318","source":"Crossref","is-referenced-by-count":43,"title":["Functional redundancy of division specific penicillin\u2010binding proteins in <i>Bacillus subtilis<\/i>"],"prefix":"10.1111","volume":"106","author":[{"given":"Jad","family":"Sassine","sequence":"first","affiliation":[{"name":"Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, The Medical School Newcastle University Newcastle upon Tyne NE2 4AH UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Meizhu","family":"Xu","sequence":"additional","affiliation":[{"name":"Centre for Bacterial Cell Biology, Institute for Cell and Molecular 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