Sortase-catalysed anchoring of surface proteins to the cell wall of Staphylococcus aureus

Mol Microbiol. 2001 Jun;40(5):1049-57. doi: 10.1046/j.1365-2958.2001.02411.x.


Many surface proteins of Gram-positive bacteria are anchored to the cell wall envelope by a transpeptidation mechanism, requiring a C-terminal sorting signal with a conserved LPXTG motif. Sortase, a membrane protein of Staphylococcus aureus, cleaves polypeptides between the threonine and the glycine of the LPXTG motif and catalyses the formation of an amide bond between the carboxyl-group of threonine and the amino-group of peptidoglycan cross-bridges. S. aureus mutants lacking the srtA gene fail to anchor and display some surface proteins and are impaired in the ability to cause animal infections. Sortase acts on surface proteins that are initiated into the secretion (Sec) pathway and have their signal peptide removed by signal peptidase. The S. aureus genome encodes two sets of sortase and secretion genes. It is conceivable that S. aureus has evolved more than one pathway for the transport of 20 surface proteins to the cell wall envelope.

Publication types

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

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Aminoacyltransferases / genetics
  • Aminoacyltransferases / metabolism*
  • Bacterial Outer Membrane Proteins / metabolism*
  • Bacterial Proteins
  • Cell Wall / chemistry
  • Cell Wall / metabolism
  • Cysteine Endopeptidases
  • Gene Expression Regulation, Bacterial
  • Molecular Sequence Data
  • Peptidoglycan / chemistry
  • Peptidoglycan / metabolism
  • Staphylococcal Protein A / chemistry
  • Staphylococcal Protein A / metabolism
  • Staphylococcus aureus / cytology
  • Staphylococcus aureus / genetics
  • Staphylococcus aureus / metabolism*


  • Bacterial Outer Membrane Proteins
  • Bacterial Proteins
  • Peptidoglycan
  • Staphylococcal Protein A
  • Aminoacyltransferases
  • sortase A
  • Cysteine Endopeptidases