z-logo
open-access-imgOpen Access
Nucleotide and deduced protein sequences of the class D tetracycline resistance determinant: relationship to other antimicrobial transport proteins
Author(s) -
Manuel F. Varela,
Jeffreyk . Griffith
Publication year - 1993
Publication title -
antimicrobial agents and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.07
H-Index - 259
eISSN - 1070-6283
pISSN - 0066-4804
DOI - 10.1128/aac.37.6.1253
Subject(s) - antiporter , peptide sequence , biology , nucleic acid sequence , tetracycline , amino acid , nucleotide , biochemistry , membrane transport protein , plasmid , efflux , transport protein , gene , consensus sequence , atp binding cassette transporter , transporter , antibiotics , membrane
The nucleotide sequence of the plasmid pRA1 gene encoding the TetA(D) tetracycline/H+ antiporter was determined. The deduced amino acid sequence was compared with those of other antimicrobial and antiseptic transporters. The deduced product of tetA(D) is a 41.1-kDa protein consisting of 394 amino acids comprising 12 membrane-spanning domains. Three classes of amino acid motifs found in TetA(D) are highly conserved in other transporters, implying that they participate in structures necessary for substrate recognition, binding, or translocation. A common mechanism of transport is suggested, with subtle sequence variations accounting for varied substrate specificities, modes of transport, and directions of transport.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here