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Origin of tetracycline efflux proteins: conclusions from nucleotide sequence analysis
Author(s) -
Sheridan R.P.,
Chopra I.
Publication year - 1991
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1991.tb00763.x
Subject(s) - efflux , tetracycline , biology , homology (biology) , bacillus subtilis , nucleic acid sequence , escherichia coli , biochemistry , microbiology and biotechnology , genetics , bacteria , amino acid , antibiotics , dna , gene
Summary The sequences of six tetracycline efflux proteins and three transport proteins which have some resembalance to them were compared. The tetracycline efflux proteins fall into three families: (i) those encoded by pBR322, RP1, and Tn 10 ( Escherichia coli ); (ii) pT181 ( Staphyloccoccus aureus ) and pTHT15 ( Bacillus subtilis ); and (iii) tet 347 (Streptomyces rimosus). There is global sequence homology within each of the first two families, but there is none between the families. The pT181/pTHT15 family shares close homology with the N ‐terminal half of the methlenomycin A efflux protein ( Streptomyces coelicor ), while tet 347 ressembles the C ‐terminal half. Portions of the N ‐terminal half of the Tn 10‐encoded protein show significant resemblance to portions in the N ‐terminal half of the pT181/pTHT15 family, but this sometimes occurs among transport proteins which do not have a common subtrate. Tetracycline efflux proteins, therefore, appear to have arisen on atleast two, or possibly three, separate occasions, probably from other transport proteins.