Cloning and nucleotide sequence of the mphB gene for macrolide 2'-phosphotransferase II in Escherichia coli.
Macrolide 2'-phosphotransferase II [MPH(2')II] inactivates macrolide antibiotics. The mphB gene for MPH(2')II was cloned from Escherichia coli and sequenced. Analysis of the nucleotide sequence indicated that mphB encoded a protein of 302 amino acids with a molecular mass of 34483 Da. The carboxy terminal region of the deduced protein contained a sequence that resembled a conserved functional domain in aminoglycoside phosphotransferases.
Noguchi
N
N
Department of Microbiology, School of Pharmacy, Tokyo University of Pharmacy and Life Science, Japan. noguchin@ps.toyaku.ac.jp
Katayama
J
J
O'Hara
K
K
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics* / Q000378:metabolism; D001483:Base Sequence; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D029968:Escherichia coli Proteins; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000235:genetics* / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D011993:Recombinant Fusion Proteins; D017853:Phosphotransferases (Alcohol Group Acceptor); C061369:macrolide 2'-kinase; C501557:mphB protein, E coli