Sorting of protein A to the staphylococcal cell wall.
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.
Schneewind
O
O
Rockefeller University, New York, New York 10021.
Model
P
P
Fischetti
V A
VA
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
D021382:Protein Sorting Signals; D013205:Staphylococcal Protein A; D008715:Methionine