The Great Escape: Structure and Function of the Autotransporter Proteins

Trends Microbiol. 1998 Sep;6(9):370-8. doi: 10.1016/s0966-842x(98)01318-3.

Abstract

The autotransporters, a family of secreted proteins from Gram-negative bacteria, possess an overall unifying structure comprising three functional domains: the amino-terminal leader sequence, the secreted mature protein (passenger domain) and a carboxy-terminal (beta-) domain that forms a beta-barrel pore to allow secretion of the passenger protein. Members of this family have been implicated as important or putative virulence factors in many Gram-negative pathogens.

Publication types

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

MeSH terms

  • Adhesins, Bacterial / chemistry
  • Adhesins, Bacterial / physiology*
  • Amino Acid Sequence
  • Carrier Proteins / chemistry
  • Carrier Proteins / metabolism
  • Carrier Proteins / physiology*
  • Gram-Negative Bacteria / metabolism*
  • Molecular Sequence Data
  • Phylogeny
  • Sequence Homology, Amino Acid
  • Serine Endopeptidases / chemistry
  • Serine Endopeptidases / genetics
  • Serine Endopeptidases / metabolism

Substances

  • Adhesins, Bacterial
  • Carrier Proteins
  • Serine Endopeptidases
  • IgA-specific serine endopeptidase