title: Sorting of protein A to the staphylococcal cell wall.
abstract: 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.
authors.affiliation: Rockefeller University, New York, New York 10021.
authors.forename: O
authors.initials: O
authors.lastname: Schneewind
authors.forename: P
authors.initials: P
authors.lastname: Model
authors.forename: V A
authors.initials: VA
authors.lastname: Fischetti
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D001692:Biological Transport; D002473:Cell Wall / Q000378:metabolism*; D004252:DNA Mutational Analysis; D008715:Methionine / Q000378:metabolism; D008969:Molecular Sequence Data; D021382:Protein Sorting Signals / Q000737:chemistry; D013205:Staphylococcal Protein A / Q000378:metabolism*; D013211:Staphylococcus aureus / Q000378:metabolism; D013347:Subcellular Fractions / Q000737:chemistry
chemical_list: D021382:Protein Sorting Signals; D013205:Staphylococcal Protein A; D008715:Methionine