PMID:2542029

Citation	Lill, R, Cunningham, K, Brundage, LA, Ito, K, Oliver, D and Wickner, W (1989) SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coli. EMBO J. 8:961-6
Abstract	Bacterial protein export requires two forms of energy input, ATP and the membrane electrochemical potential. Using an in vitro reaction reconstituted with purified soluble and peripheral membrane components, we can now directly measure the translocation-coupled hydrolysis of ATP. This translocation ATPase requires inner membrane vesicles, SecA protein and translocation-competent proOmpA. The stimulatory activity of membrane vesicles can be blocked by either antibody to the SecY protein or by preparing the membranes from a secY-thermosensitive strain which had been incubated at the non-permissive temperature in vivo. The SecA protein itself has more than one ATP binding site. 8-azido-ATP inactivates SecA for proOmpA translocation and for translocation ATPase, yet does not inhibit a low level of ATP hydrolysis inherent in the isolated SecA protein. These data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane.
Links	PubMed PMC400897
Keywords	Adenosine Triphosphatases/metabolism; Adenosine Triphosphate/metabolism; Bacterial Proteins/metabolism; Binding Sites; Biological Transport, Active; Cell Membrane/metabolism; Escherichia coli/metabolism; Hydrolysis
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Significance

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
ECOLI:SECA	enables	GO:0015462: ATPase-coupled protein transmembrane transporter activity	ECO:0000314: direct assay evidence used in manual assertion		F		Seeded From UniProt	complete

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