Evidence that KpsT, the ATP-binding component of an ATP-binding cassette transporter, is exposed to the periplasm and associates with polymer during translocation of the polysialic acid capsule of Escherichia coli K1
Author:
Affiliation:
1. Department of Microbiology and Immunology, University of Rochester Medical Center, New York 14642, USA.
Abstract
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Link
https://journals.asm.org/doi/pdf/10.1128/jb.179.4.1400-1403.1997
Reference25 articles.
1. Energy coupling in bacterial periplasmic permeases;Ames G. F.;J. Bacteriol.,1990
2. Traffic ATPases: a superfamily of transport proteins operating from Escherichia coli to humans;Ames G. F.;Adv. Enzymol.,1992
3. The ATP-binding component of a prokaryotic traffic ATPase is exposed to the periplasmic (external) surface;Baichwal V.;Proc. Natl. Acad. Sci. USA,1993
4. Coating the surface: a model for expression of capsular polysialic acid in Escherichia coli K1;Bliss J. M.;Mol. Microbiol.,1996
5. Polysialic acid export in Escherichia coli K1: the role of KpsT, the ATP-binding component of an ABC transporter, in chain translocation;Bliss J. M.;Glycobiology,1996
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