FtsA

FtsA is an actin-like cytoskeletal protein essential for bacterial cell division. It is encoded by the ftsA gene and is a core component of the divisome, the protein complex that coordinates cytokinesis in many bacteria. FtsA functions to connect the polymerized form of FtsZ, which assembles into the Z-ring at the future division site, to the cytoplasmic membrane and to other divisome proteins, thereby facilitating ring constriction and septum formation.

Structurally, FtsA is a membrane-associated, ATP-binding protein. It contains an N-terminal amphipathic helix that tethers it to the inner membrane and an actin-like core that can bind and hydrolyze ATP. Through its interactions with FtsZ, FtsA helps anchor the Z-ring to the membrane and promotes the recruitment of late-division proteins essential for septum synthesis, such as those involved in peptidoglycan remodeling and cell wall synthesis.

Function and regulation in the cell are tightly coordinated. FtsA’s activity and localization depend on FtsZ dynamics, and the abundance and state of FtsA influence divisome assembly and constriction. In Escherichia coli and many other bacteria, FtsA is considered essential for cytokinesis. In some contexts, mutations can modify the interaction between FtsA and FtsZ or compensate for the loss of other anchoring proteins, illustrating the interconnected control of Z-ring maturation and division site progression.

FtsA is widely studied as part of the bacterial division machinery and is of interest for understanding fundamental cell biology and as a potential target for antimicrobial strategies.