SMART: Pfam domain APT

APT

PFAM accession number:	PF03440
Interpro abstract (IPR005138):	This is the N-terminal domain of aerolysin and pertussis toxin which contains a type-C lectin like fold. Aerolysin causes the pathogenicity of Aeromonas hydrophila, a bacterium associated with diarrhoeal diseases and deep wound infections. Like many other microbial toxins, the protein changes in a multistep process from a completely water-soluble form to produce a transmembrane channel that breaks the permeability barrier of cells [ (PUBMED:7510043) ]. Pertussis toxin is a major virulence factor of Bordetella pertussis, which causes whooping cough. The protein is a hexamer containing a catalytic subunit (S1) that is tightly associated with a pentameric cell-binding component (B-oligomer). ATP, detergents and phospholipids assist in activating the holotoxin by destabilising the interaction between S1 and the B-oligomer [ (PUBMED:8637000) ]. Pertussis toxin is an exotoxin and is an essential component of acellular vaccines [ (PUBMED:8075982) (PUBMED:7634099) ]. The catalytic A-subunit (S1) shares structural homology with other ADP-ribosylating bacterial toxins, although differences in the carboxy-terminal portion explain its unique activation mechanism [ (PUBMED:8075982) ]. The diverse biological activities of the toxin depend on its ability to recognise carbohydrate-containing receptors on a wide variety of eukaryotic cells.

PFAM accession number:

PF03440

Interpro abstract (IPR005138):

This is the N-terminal domain of aerolysin and pertussis toxin which contains a type-C lectin like fold.

Aerolysin causes the pathogenicity of Aeromonas hydrophila, a bacterium associated with diarrhoeal diseases and deep wound infections. Like many other microbial toxins, the protein changes in a multistep process from a completely water-soluble form to produce a transmembrane channel that breaks the permeability barrier of cells [ (PUBMED:7510043) ].

Pertussis toxin is a major virulence factor of Bordetella pertussis, which causes whooping cough. The protein is a hexamer containing a catalytic subunit (S1) that is tightly associated with a pentameric cell-binding component (B-oligomer). ATP, detergents and phospholipids assist in activating the holotoxin by destabilising the interaction between S1 and the B-oligomer [ (PUBMED:8637000) ]. Pertussis toxin is an exotoxin and is an essential component of acellular vaccines [ (PUBMED:8075982) (PUBMED:7634099) ]. The catalytic A-subunit (S1) shares structural homology with other ADP-ribosylating bacterial toxins, although differences in the carboxy-terminal portion explain its unique activation mechanism [ (PUBMED:8075982) ]. The diverse biological activities of the toxin depend on its ability to recognise carbohydrate-containing receptors on a wide variety of eukaryotic cells.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry APT