Twelve-transmembrane-segment (TMS) version (DeltaTMS VII-VIII) of the 14-TMS Tet(L) antibiotic resistance protein retains monovalent cation transport modes but lacks tetracycline efflux capacity.

doi:10.1128/JB.183.8.2667-2671.2001

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Article

Twelve-transmembrane-segment (TMS) version (DeltaTMS VII-VIII) of the 14-TMS Tet(L) antibiotic resistance protein retains monovalent cation transport modes but lacks tetracycline efflux capacity.

Journal of bacteriology - 1 Apr 2001

Jin J, Guffanti A A, Beck C, Krulwich T A

Abstract excerpt

A "Tet(L)-12" version of Tet(L), a tetracycline efflux protein with 14 transmembrane segments (TMS), was constructed by deletion of two central TMS. Tet(L)-12 catalyzed Na+/H+ antiport and antiport with K+ as a coupling ion as well as or better than wild-type Tet(L) but exhibited no tetracycline-Me2+/H+ antiport in Escherichia coli vesicles.

Topics

Amino Acid Sequence
Antiporters
Bacterial Proteins
Carrier Proteins
Escherichia coli
Escherichia coli Proteins
Gene Deletion
Hydrogen
Ion Transport
Membrane Proteins
Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Potassium

Sodium

Sodium-Hydrogen Exchangers

Tetracycline

Tetracycline Resistance

Transport Vesicles

Source

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Identifiers

PMID: 11274128
DOI: 10.1128/JB.183.8.2667-2671.2001
PMCID: PMC95185

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