PMID:8951810

Citation	van der Does, C, den Blaauwen, T, de Wit, JG, Manting, EH, Groot, NA, Fekkes, P and Driessen, AJ (1996) SecA is an intrinsic subunit of the Escherichia coli preprotein translocase and exposes its carboxyl terminus to the periplasm. Mol. Microbiol. 22:619-29
Abstract	SecA is the dissociable ATPase subunit of the Escherichia coli preprotein translocase, and cycles in a nucleotide-modulated manner between the cytosol and the membrane. Overproduction of the integral subunits of the translocase, the SecY, SecE and SecG polypeptides, results in an increased level of membrane-bound SecA. This fraction of SecA is firmly associated with the membrane as it is resistant to extraction with the chaotropic agent urea, and appears to be anchored by SecYEG rather than by lipids. Topology analysis of this membrane-associated form of SecA indicates that it exposes a carboxy-terminal domain to the periplasmic face of the membrane.
Links	PubMed
Keywords	Adenosine Triphosphatases/genetics; Adenosine Triphosphatases/metabolism; Amino Acid Sequence; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Cell Membrane/metabolism; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins; Gene Expression; Membrane Proteins/genetics; Membrane Proteins/metabolism; Membrane Transport Proteins; Molecular Sequence Data; Phospholipids/metabolism; Trypsin/metabolism
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