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PMID: 9171431 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Membrane topology of the metal-tetracycline/H+ antiporter TetA(K) from Staphylococcus aureus.

Journal of bacteriology ·Vol. 179 ·No. 11 ·1997-06-00 ·Pages 3786-9

Ginn SL, Brown MH, Skurray RA

Abstract

A series of fusions to the reporter proteins alkaline phosphatase and beta-galactosidase have been constructed in the predicted periplasmic and cytoplasmic loops of TetA(K), a protein responsible for efflux-mediated tetracycline resistance in Staphylococcus aureus. The results support a topological model of 14 transmembrane segments for TetA(K).

MeSH Terms

Amino Acid Sequence Antiporters/chemistry,genetics Bacterial Proteins/chemistry,genetics Cell Membrane/chemistry Models, Molecular Molecular Sequence Data Staphylococcus aureus/chemistry

Chemicals

Antiporters Bacterial Proteins tetA protein, Bacteria

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Ginn S L

School of Biological Sciences, University of Sydney, New South Wales, Australia.

Brown M H

Skurray R A

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26 references, click to expand

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Article Info

Journal

Journal of bacteriology

Abbr.

J Bacteriol

ISSN

0021-9193

DOI

10.1128/jb.179.11.3786-3789.1997

Published

1997-06-00

Pages

3786-9

Language

English

Region

United States

NLM ID

2985120R

PMCID

PMC179179

Subset

External Links

PubMed source DOI: 10.1128/jb.179.11.3786-3789.1997 PMC Full Text View journal details

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Membrane topology of the metal-tetracycline/H+ antiporter TetA(K) from Staphylococcus aureus.

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