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Cell division protein ZipA is an essential bacterial protein found in organisms such as *Escherichia coli* and serves as a membrane-anchored component of the divisome, the protein complex responsible for cytokinesis in bacteria. ZipA interacts with FtsZ, a tubulin homologue, by binding both its C-terminal tail and globular core domain through a two-pronged mechanism. ZipA acts to tether and stabilize FtsZ protofilaments to the cytoplasmic membrane and is required for the assembly and integrity of the cytokinetic Z ring, thus defining the plane of cell division. Additionally, ZipA supports the recruitment of other late-division proteins necessary for septal ring formation. Overproduction of ZipA can protect FtsZ from proteolytic degradation. Owing to its absence in eukaryotes and essential role in bacterial viability, ZipA is of scientific interest as a potential antibacterial target, but no known ZipA inhibitors have progressed to therapeutic use.
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