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cell division protein ZipA C-terminal FtsZ-binding domain-containing protein
This family represents the ZipA C-terminal domain. ZipA is involved in septum formation in bacterial cell division. Its C-terminal domain binds FtsZ, a major component of the bacterial septal ring. The structure of this 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 [1]. [1]. 10924108. Solution structure of ZipA, a crucial component of Escherichia. coli cell division.. Moy FJ, Glasfeld E, Mosyak L, Powers R;. Biochemistry 2000;39:9146-9156. (from Pfam)
cell division protein ZipA
This HMM represents the full length of bacterial cell division protein ZipA. The N-terminal hydrophobic stretch is an uncleaved signal-anchor sequence. This is followed by an unconserved, variable length, low complexity region, and then a conserved C-terminal region of about 140 amino acids (see PF04354) that interacts with the tubulin-like cell division protein FtsZ.
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