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SecA is an intrinsic subunit of the Escherichia coli preprotein translocase and exposes its carboxyl terminus to the periplasm
Author(s) -
Van Der Does Chris,
Den Blaauwen Tanneke,
De Wit Janny G.,
Manting Erik H.,
Groot Nancy A.,
Fekkes Peter,
Driessen Arnold J. M.
Publication year - 1996
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.1996.d01-1712.x
Subject(s) - translocase , periplasmic space , biology , protein subunit , membrane transport protein , biochemistry , inner membrane , translocase of the inner membrane , microbiology and biotechnology , escherichia coli , transmembrane domain , membrane protein , membrane , mitochondrial membrane transport protein , chromosomal translocation , gene
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.