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- Q4827027 subject Q8707319.
- Q4827027 subject Q9089708.
- Q4827027 abstract "In molecular biology, an autotransporter domain is a structural domain found in some bacterial outer membrane proteins. The domain is always located at the C-terminal end of the protein and forms a beta-barrel structure. The barrel is oriented in the membrane such that the N-terminal portion of the protein, termed the passenger domain, is presented on the cell surface. These proteins are typically virulence factors, associated with infection or virulence in pathogenic bacteria. The name autotransporter derives from an initial understanding that the protein was self-sufficient in transporting the passenger domain through the outermembrane. This view has since been challenged by Benz and Schmidt.Secretion of polypeptide chains through the outer membrane of Gram-negative bacteria can occur via a number of different pathways. The type V(a), or autotransporter, secretion pathway constitutes the largest number of secreted virulence factors of any one of the seven known types of secretion in Gram-negative bacteria. This secretion pathway is exemplified by the prototypical IgA1 Protease of Neisseria gonorrhoeae. The protein is directed to the inner membrane by a signal peptide transported across the inner membrane via the Sec machinery. Once in the periplasm, the autotransporter domain inserts into the outer membrane. The passenger domain is passed through the center of the autotransporter domain to be presented on the outside of the cell, however the mechanism by which this occurs remains unclear.The C-terminal translocator domain corresponds to an outer membrane beta-barrel domain. The N-terminal passenger domain is translocated across the membrane, and may or may not be cleaved from the translocator domain. In those proteins where the cleavage is auto-catalytic, the peptidase domains belong to MEROPS peptidase families S6 and S8. Passenger domains structurally characterized to date have been shown to be dominated by a protein fold known as a beta helix, typified by pertactin. The folding of this domain is thought to be intrinsically linked to its method of outer membrane translocation.".
- Q4827027 symbol "Autotransporter".
- Q4827027 thumbnail PDB_1uyn_EBI.jpg?width=300.
- Q4827027 wikiPageWikiLink Q1623405.
- Q4827027 wikiPageWikiLink Q25712.
- Q4827027 wikiPageWikiLink Q258248.
- Q4827027 wikiPageWikiLink Q284398.
- Q4827027 wikiPageWikiLink Q310424.
- Q4827027 wikiPageWikiLink Q310425.
- Q4827027 wikiPageWikiLink Q487869.
- Q4827027 wikiPageWikiLink Q632006.
- Q4827027 wikiPageWikiLink Q7842189.
- Q4827027 wikiPageWikiLink Q8707319.
- Q4827027 wikiPageWikiLink Q898273.
- Q4827027 wikiPageWikiLink Q899779.
- Q4827027 wikiPageWikiLink Q899790.
- Q4827027 wikiPageWikiLink Q906465.
- Q4827027 wikiPageWikiLink Q9089708.
- Q4827027 wikiPageWikiLink Q973079.
- Q4827027 symbol "Autotransporter".
- Q4827027 type Biomolecule.
- Q4827027 type Protein.
- Q4827027 type Thing.
- Q4827027 type Q206229.
- Q4827027 type Q8054.
- Q4827027 comment "In molecular biology, an autotransporter domain is a structural domain found in some bacterial outer membrane proteins. The domain is always located at the C-terminal end of the protein and forms a beta-barrel structure. The barrel is oriented in the membrane such that the N-terminal portion of the protein, termed the passenger domain, is presented on the cell surface. These proteins are typically virulence factors, associated with infection or virulence in pathogenic bacteria.".
- Q4827027 label "Autotransporter domain".
- Q4827027 depiction PDB_1uyn_EBI.jpg.