UniProt functional annotation for P14283



	UniProt functional annotation for P14283

UniProt code: P14283.

Organism: Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).

Taxonomy: Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Alcaligenaceae; Bordetella.

Function: Agglutinogen that binds to eukaryotic cells; a process mediated by the R-G-D sequence. Pertactin may have a role in bacterial adhesion, and thus play a role in virulence. May contribute to the disease state of whooping cough.

Subunit: Monomer.

Subcellular location: [Pertactin autotransporter]: Periplasm {ECO:0000250}.

Subcellular location: [Outer membrane protein P.69]: Secreted. Cell surface.

Subcellular location: [Pertactin translocator]: Cell outer membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=The cleaved C-terminal fragment (autotransporter domain) is localized in the outer membrane.

Domain: The signal peptide, cleaved at the inner membrane, guides the autotransporter protein to the periplasmic space. Then, insertion of the C-terminal translocator domain in the outer membrane forms a hydrophilic pore for the translocation of the passenger domain to the bacterial cell surface, with subsequent cleavage (By similarity). {ECO:0000250}.

Miscellaneous: Synthesized only in the presence of low Mg(2+) concentration.

Annotations taken from UniProtKB at the EBI.


Organism:		Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
Taxonomy:		Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Alcaligenaceae; Bordetella.



Function:		Agglutinogen that binds to eukaryotic cells; a process mediated by the R-G-D sequence. Pertactin may have a role in bacterial adhesion, and thus play a role in virulence. May contribute to the disease state of whooping cough.


Subunit:		Monomer.
Subcellular location:		[Pertactin autotransporter]: Periplasm {ECO:0000250}.
Subcellular location:		[Outer membrane protein P.69]: Secreted. Cell surface.
Subcellular location:		[Pertactin translocator]: Cell outer membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=The cleaved C-terminal fragment (autotransporter domain) is localized in the outer membrane.
Domain:		The signal peptide, cleaved at the inner membrane, guides the autotransporter protein to the periplasmic space. Then, insertion of the C-terminal translocator domain in the outer membrane forms a hydrophilic pore for the translocation of the passenger domain to the bacterial cell surface, with subsequent cleavage (By similarity). {ECO:0000250}.
Miscellaneous:		Synthesized only in the presence of low Mg(2+) concentration.