Bacterial cell division is achieved by a dynamic protein complex called the divisome. The accurate placement of the divisome, and more specifically that of the tubulin-like protein FtsZ which forms the contractile Z-ring at mid-cell, is finely regulated by different mechanisms tailored to each bacterial class. To give rise to two viable daughter cells with the same genetic heritage and cell shape, Streptococcus pneumoniae uses an original system that relies on the membrane protein MapZ. This system is required for identifying the division site as well as positioning the Z-ring at mid-cell. In addition, MapZ undergoes phosphorylation by the serine/threonine kinase StkP and controls the constriction of the Z-ring. Here, we discuss recent advances and concepts of the MapZ system.
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