SecA is an intrinsic subunit of the Escherichia coli preprotein translocase and exposes its carboxyl terminus to the periplasm.

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.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

van der Does C,den Blaauwen T,de Wit JG,Manting EH,Groot NA,Fekkes P,Driessen AJ

doi

10.1046/j.1365-2958.1996.d01-1712.x

subject

Has Abstract

pub_date

1996-11-01 00:00:00

pages

619-29

issue

4

eissn

0950-382X

issn

1365-2958

journal_volume

22

pub_type

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