ZipA, C-terminal domain (FtsZ-binding)
SMART accession number:SM00771
Description: C-terminal domain of ZipA, a component of cell division in E.coli. It interacts with the FtsZ protein in one of the initial steps of septum formation. The structure of this domain is composed of three alpha-helices and a beta-sheet consisting of six antiparallel beta-strands.
Interpro abstract (IPR007449):

This entry represents the ZipA C-terminal domain. ZipA, a membrane-anchored protein, is an essential cell division protein involved in septum formation [ (PUBMED:9008158) (PUBMED:9864327) ]. FtsA and the C-terminal domain of ZipA bind FtsZ, a homologue of eukaryotic tubulins and a major component of the bacterial septal ring [ (PUBMED:10209756) ], at the prospective division site. This is followed by the sequential addition of FtsK, FtsQ, FtsL, FtsW, FtsI, and FtsN [ (PUBMED:11163134) (PUBMED:11948172) (PUBMED:11847116) ]. ZipA contains three domains: a short N-terminal membrane-anchored domain, a central P/Q domain that is rich in proline and glutamine and a C-terminal domain, which comprises almost half the protein. The structure of the C-terminal domain is an alpha-beta fold with three alpha helices and a beta sheet of six antiparallel beta strands. The major loops protruding from the beta sheet surface are thought to form a binding site for FtsZ [ (PUBMED:10924108) ].

GO process:cell septum assembly (GO:0090529)
Family alignment:
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There are 4893 ZipA_C domains in 4891 proteins in SMART's nrdb database.

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