| Description | ZapA is a cell division protein which interacts with FtsZ. FtsZ is part of a mid-cell cytokinetic structure termed the Z-ring that recruits a hierarchy of fission related proteins early in the bacterial cell cycle. The interaction of FtsZ with ZapA drives its polymerisation and promotes FtsZ filament bundling thereby contributing to the spatio-temporal tuning of the Z-ring [ ].The structure of ZapA is organised into two distinct domains, with the first 49 residues forming a globular domain comprised of a two stranded antiparallel β-sheet and an α-helix, whereas the C-terminal half of the protein (residues 50-102) forms a single, 14-turn α-helix. The ZapA protomer forms a pseudosymmetric tetramer.This superfamily represents a domain found at the N terminus of the cell division protein ZapA. Its structure is composed of an α-helix which plays a role in mediating ZapA-FtsZ interactions to facilitate FtsZ filament bundling and Z-ring stability in dividing bacterial cells. | Name | Cell division protein ZapA, N-terminal |
| Short Name | Cell_div_ZapA_N | Type | Homologous_superfamily |
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