The mannose permease of Escherichia coli consists of three different proteins. Amino acid sequence and function in sugar transport, sugar phosphorylation, and penetration of phage lambda DNA

J Biol Chem. 1987 Apr 15;262(11):5238-47.


The mannose permease of the bacterial phosphotransferase system mediates sugar transport across the cytoplasmic membrane concomitant with sugar phosphorylation. It also functions as a receptor for bacterial chemotaxis and is required for infection of the cell by bacteriophage lambda where it most likely functions as a pore for penetration of lambda DNA. The permease consists of three different subunits, IIIMan, II-PMan, and II-MMan, which are encoded in a single transcriptional unit ptsLPM. The complete amino acid sequence of the subunits is deduced from the nucleotide sequence. IIIMan (35 kDa) is a hydrophilic protein which is transiently phosphorylated and most likely contains the active site for sugar phosphorylation. II-PMan (28 kDa) is very hydrophobic; II-MMan (31 kDa) is moderately hydrophobic. Both are integral membrane proteins and most likely form the transmembrane channel. All three subunits are required for sugar transport and phosphorylation; II-PMan and II-MMan alone are sufficient for penetration of lambda DNA. Truncated forms of II-MMan and II-PMan are described that mediate lambda DNA penetration but have no apparent sugar transport activity. Residual sugar phosphorylation activity is found with the truncated form of II-PMan. No obvious homologies at the level of amino acid sequence could be detected with other bacterial transport proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacteriophage lambda / genetics*
  • Base Sequence
  • Biological Transport, Active
  • Carbohydrate Metabolism
  • DNA, Viral / metabolism*
  • Escherichia coli / enzymology*
  • Models, Molecular
  • Molecular Weight
  • Operon
  • Phosphoenolpyruvate Sugar Phosphotransferase System / analysis*
  • Phosphoenolpyruvate Sugar Phosphotransferase System / metabolism
  • Phosphorylation


  • DNA, Viral
  • Phosphoenolpyruvate Sugar Phosphotransferase System
  • phosphoenolpyruvate-mannose phosphotransferase

Associated data

  • GENBANK/J02699