| Description | Cell division in bacteria is a complex process driven by the septal ring, a membrane-associated cytoskeletal element that directs the formation of the septum [ ]. Central to formation of the septal ring, and hence cell division itself, is the tubulin-like GTPase protein FtsZ which is the first cell division component to specifically accumulate at the division site. Here it self-assembles into a ring-like polymer structure associated with the inner surface of the cytoplasmic membrane, providing a scaffold to recruit other members of the septal ring.This entry represents the bacterial cell division protein ZipA. ZipA is one of the first proteins recruited to the division site after FtsZ, which it directly binds, and is essential for cell division and viability in Escherichia coli. ZipA has been shown to The protein contains five distinct regions. The N terminus contains a short hydrophobic regions which anchors the protein to the cytoplasmic membrane. This is followed by short basic and acidic regions, and a longer proline-rich region. The C-terminal domain interacts with FtsZ through hydrophobic interactions involving exposed non-polar residues, and forms a six-stranded β sheet packed against three α helices [ , ]. Since ZipA is anchored to the cytoplasmic membrane while binding FtsZ, it has been speculated that the function of ZipA may be to link the membrane with the FtsZ rings, to stabilise or organise the FtsZ rings, or to link invagination of the membrane to constriction of the FtsZ ring during septation. ZipA has been shown to induce association of FtsZ protofilaments into arrays of long thick bundles in vitro. | Name | Cell division protein ZipA |
| Short Name | Cell_div_ZipA | Type | Family |
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