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The precise function of these three bitopic membrane proteins, which are central to the division process, remains unknown. We report here the characterization of a<jats:italic>divIB<\/jats:italic>deletion mutant of<jats:italic>Streptococcus pneumoniae<\/jats:italic>, which is a coccus that divides with parallel planes. Unlike its homologue FtsQ in<jats:italic>Escherichia coli<\/jats:italic>, pneumococcal DivIB is not required for growth in rich medium, but the \u0394<jats:italic>divIB<\/jats:italic>mutant forms chains of diplococci and a small fraction of enlarged cells with defective septa. However, the deletion mutant does not grow in a chemically defined medium. In the absence of DivIB and protein synthesis, the partner FtsL is rapidly degraded, whereas other division proteins are not affected, pointing to a role of DivIB in stabilizing FtsL. This is further supported by the finding that an additional copy of<jats:italic>ftsL<\/jats:italic>restores growth of the \u0394<jats:italic>divIB<\/jats:italic>mutant in defined medium. Functional mapping of the three distinct \u03b1, \u03b2, and \u03b3 domains of the extracellular region of DivIB revealed that a complete \u03b2 domain is required to fully rescue the deletion mutant. DivIB with a truncated \u03b2 domain reverts only the chaining phenotype, indicating that DivIB has distinct roles early and late in the division process. Most importantly, the deletion of<jats:italic>divIB<\/jats:italic>increases the susceptibility to \u03b2-lactams, more evidently in a resistant strain, suggesting a function in cell wall synthesis.<\/jats:p>","DOI":"10.1128\/jb.00376-08","type":"journal-article","created":{"date-parts":[[2008,4,26]],"date-time":"2008-04-26T00:58:32Z","timestamp":1209171512000},"page":"4501-4511","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":36,"title":["Roles of Pneumococcal DivIB in Cell Division"],"prefix":"10.1128","volume":"190","author":[{"given":"Audrey","family":"Le Goue\u0308llec","sequence":"first","affiliation":[{"name":"Laboratoire d'Inge\u0301nierie des Macromole\u0301cules, Institut de Biologie Structurale (Universite\u0301 Joseph Fourier, CNRS UMR 5075, CEA), Grenoble, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Laure","family":"Roux","sequence":"additional","affiliation":[{"name":"Laboratoire d'Inge\u0301nierie des Macromole\u0301cules, Institut de Biologie Structurale (Universite\u0301 Joseph Fourier, CNRS UMR 5075, CEA), Grenoble, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniela","family":"Fadda","sequence":"additional","affiliation":[{"name":"Dipartimento di Scienze e Tecnologie Biomediche, Sez. 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