The great escape: structure and function of the autotransporter proteins.
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.
Dept of Medicine, University of Maryland School of Medicine, Baltimore 21201, USA.
I R
IR
Henderson
F
F
Navarro-Garcia
J P
JP
Nataro
D018829:Adhesins, Bacterial / Q000737:chemistry / Q000502:physiology*; D000595:Amino Acid Sequence; D002352:Carrier Proteins / Q000737:chemistry / Q000378:metabolism / Q000502:physiology*; D006090:Gram-Negative Bacteria / Q000378:metabolism*; D008969:Molecular Sequence Data; D010802:Phylogeny; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
D018829:Adhesins, Bacterial; D002352:Carrier Proteins; D012697:Serine Endopeptidases; C021433:IgA-specific serine endopeptidase