The cellobiose permease of Escherichia coli consists of three proteins and is homologous to the lactose permease of Staphylococcus aureus.
The cellobiose (cel) operon of Escherichia coli was recently sequenced and shown to consist of five genes, celABCDF (Parker and Hall, 1990). We have shown that the CelA, CelB and CelC proteins possess amino acid sequences which are homologous to different domains of the lactose permease of Staphylococcus aureus. CelB corresponds to the integral membrane portion of the permease (IIcel) while CelC (IIIcel) and CelA (IVcel) correspond to the two cytoplasmic domains which appear to comprise the first and second phosphorylation sites in the permease, respectively. The cellobiose permease is the only one of several homologous sequenced permeases of the phosphoenolpyruvate:sugar phosphotransferase system which has its three known functional domains residing on distinct polypeptide chains.
Reizer
J
J
Department of Biology, University of California at San Diego, La Jolla 92093-0116.
Reizer
A
A
Saier
M H
MH
D000595:Amino Acid Sequence; D002475:Cellobiose / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D007785:Lactose / Q000378:metabolism*; D026901:Membrane Transport Proteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D013211:Staphylococcus aureus / Q000201:enzymology*
D026901:Membrane Transport Proteins; D002475:Cellobiose; D007785:Lactose