The MalK protein of the ATP-binding cassette transporter for maltose of Escherichia coli is accessible to protease digestion from the periplasmic side of the membrane.
The ATP-hydrolyzing subunit MalK of the ATP-binding cassette transporter for maltose of Escherichia coli is demonstrated to be accessible to digestion by proteinase K in right-side-out membrane vesicles. This finding suggests a partial transmembrane orientation of the protein.
Schneider
E
E
Fachbereich Biologie/Chemie, Universität Osnabrück, Germany.
Hunke
S
S
Tebbe
S
S
D018528:ATP-Binding Cassette Transporters / Q000378:metabolism*; D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism*; D002352:Carrier Proteins / Q000378:metabolism*; D002462:Cell Membrane; D019286:Endopeptidase K; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins; D008320:Maltose / Q000378:metabolism; D012697:Serine Endopeptidases
D018528:ATP-Binding Cassette Transporters; D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D002352:Carrier Proteins; D029968:Escherichia coli Proteins; C068021:MalK protein, Bacteria; C489398:MalK protein, E coli; D008320:Maltose; D012697:Serine Endopeptidases; D019286:Endopeptidase K