PMID:11298280

Citation	Feucht, A, Lucet, I, Yudkin, MD and Errington, J (2001) Cytological and biochemical characterization of the FtsA cell division protein of Bacillus subtilis. Mol. Microbiol. 40:115-25
Abstract	The actin-like protein FtsA is present in many eubacteria, and genetic experiments have shown that it plays an important, sometimes essential, role in cell division. Here, we show that Bacillus subtilis FtsA is targeted to division sites in both vegetative and sporulating cells. As in other organisms FtsA is probably recruited immediately after FtsZ. In sporulating cells of B. subtilis FtsZ is recruited to potential division sites at both poles of the cell, but asymmetric division occurs at only one pole. We have now found that FtsA is recruited to only one cell pole, suggesting that it may play an important role in the generation of asymmetry in this system. FtsA is present in much higher quantities in B. subtilis than in Escherichia coli, with approximately one molecule of FtsA for five of FtsZ. This means that there is sufficient FtsA to form a complete circumferential ring at the division site. Therefore, FtsA may have a direct structural role in cell division. We have purified FtsA and shown that it behaves as a dimer and that it has both ATP-binding and ATP-hydrolysis activities. This suggests that ATP hydrolysis by FtsA is required, together with GTP hydrolysis by FtsZ, for cell division in B. subtilis (and possibly in most eubacteria).
Links	PubMed
Keywords	Adenosine Triphosphatases/metabolism; Adenosine Triphosphate/metabolism; Bacillus subtilis/cytology; Bacillus subtilis/metabolism; Bacterial Proteins/metabolism; Base Sequence; Cell Division; DNA Primers; Escherichia coli Proteins; Sigma Factor; Transcription Factors
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
BACSU:FTSA		GO:0016887 : ATPase activity	ECO:0000314:		F		Shown that B. subtilis FtsA is capable of binding and hydrolysing ATP (Fig. 7), To test whether FtsA has ATPase activity, a measurement of the hydrolysis of ATP by monitoring the release of 32Pi from [γ-32P]-ATP. The activity was readily detected, and analysis of the reaction revealed Michaelis–Menten kinetics (Fig. 7B) with a Km of 0.7 mM and a Vmax of 0.125 mol of ATP hydrolysed per second per mol of FtsA dimer.	complete CACAO 3991
BACSU:FTSA	enables	GO:0016887: ATPase activity	ECO:0000314: direct assay evidence used in manual assertion		F		Seeded From UniProt	complete

References

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