Sorting of protein A to the staphylococcal cell wall

Cell. 1992 Jul 24;70(2):267-81. doi: 10.1016/0092-8674(92)90101-h.


The cell wall of gram-positive bacteria can be thought of as representing a unique cell compartment, which contains anchored surface proteins that require specific sorting signals. Some biologically important products are anchored in this way, including protein A and fibronectin binding protein of Staphylococcus aureus and streptococcal M protein. Studies of staphylococcal protein A and Escherichia coli alkaline phosphatase show that the signal both necessary and sufficient for cell wall anchoring consists of an LPXTGX motif, a C-terminal hydrophobic domain, and a charged tail. These sequence elements are conserved in many surface proteins from different gram-positive bacteria. We propose the existence of a hitherto undescribed sorting mechanism that positions proteins on the surface of gram-positive bacteria.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Biological Transport
  • Cell Wall / metabolism*
  • DNA Mutational Analysis
  • Methionine / metabolism
  • Molecular Sequence Data
  • Protein Sorting Signals / chemistry
  • Staphylococcal Protein A / metabolism*
  • Staphylococcus aureus / metabolism
  • Subcellular Fractions / chemistry


  • Protein Sorting Signals
  • Staphylococcal Protein A
  • Methionine

Associated data