ID   PERT_BORPA              Reviewed;         922 AA.
AC   P24328;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Pertactin autotransporter;
DE   AltName: Full=P.95;
DE   Contains:
DE     RecName: Full=Outer membrane protein P.70;
DE   Contains:
DE     RecName: Full=Pertactin translocator;
DE   Flags: Precursor;
GN   Name=prn; OrderedLocusNames=BPP1150;
OS   Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CN2591;
RX   PubMed=2041476; DOI=10.1111/j.1365-2958.1991.tb02123.x;
RA   Li L.J., Dougan G., Novotny P., Charles I.G.;
RT   "P.70 pertactin, an outer-membrane protein from Bordetella parapertussis:
RT   cloning, nucleotide sequence and surface expression in Escherichia coli.";
RL   Mol. Microbiol. 5:409-417(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12822 / ATCC BAA-587 / NCTC 13253;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
CC   -!- FUNCTION: Agglutinogen that binds to eukaryotic cells; a process
CC       mediated by the R-G-D sequence. Pertactin may have a role in bacterial
CC       adhesion, and thus play a role in virulence. May contribute to the
CC       disease state of whooping cough.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: [Pertactin autotransporter]: Periplasm
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Outer membrane protein P.70]: Secreted. Cell
CC       surface.
CC   -!- SUBCELLULAR LOCATION: [Pertactin translocator]: Cell outer membrane
CC       {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=The
CC       cleaved C-terminal fragment (autotransporter domain) is localized in
CC       the outer membrane.
CC   -!- DOMAIN: The signal peptide, cleaved at the inner membrane, guides the
CC       autotransporter protein to the periplasmic space. Then, insertion of
CC       the C-terminal translocator domain in the outer membrane forms a
CC       hydrophilic pore for the translocation of the passenger domain to the
CC       bacterial cell surface, with subsequent cleavage (By similarity).
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: Synthesized only in the presence of low Mg(2+)
CC       concentrations.
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DR   EMBL; X54547; CAA38419.1; -; Genomic_DNA.
DR   EMBL; BX640426; CAE36451.1; -; Genomic_DNA.
DR   PIR; S15204; S15204.
DR   RefSeq; WP_010927881.1; NC_002928.3.
DR   AlphaFoldDB; P24328; -.
DR   SMR; P24328; -.
DR   EnsemblBacteria; CAE36451; CAE36451; BPP1150.
DR   KEGG; bpa:BPP1150; -.
DR   HOGENOM; CLU_002318_1_1_4; -.
DR   OMA; KAGERQH; -.
DR   Proteomes; UP000001421; Chromosome.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   Gene3D; 2.160.20.20; -; 1.
DR   Gene3D; 2.40.128.130; -; 1.
DR   InterPro; IPR005546; Autotransporte_beta.
DR   InterPro; IPR036709; Autotransporte_beta_dom_sf.
DR   InterPro; IPR012332; Autotransporter_pectin_lyase_C.
DR   InterPro; IPR006315; OM_autotransptr_brl.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR003992; Pertactin.
DR   InterPro; IPR004899; Pertactin_central.
DR   InterPro; IPR003991; Pertactin_virulence_factor.
DR   Pfam; PF03797; Autotransporter; 1.
DR   Pfam; PF03212; Pertactin; 1.
DR   PRINTS; PR01482; PERTACTIN.
DR   PRINTS; PR01484; PRTACTNFAMLY.
DR   SMART; SM00869; Autotransporter; 1.
DR   SUPFAM; SSF103515; SSF103515; 1.
DR   SUPFAM; SSF51126; SSF51126; 1.
DR   TIGRFAMs; TIGR01414; autotrans_barl; 1.
DR   PROSITE; PS51208; AUTOTRANSPORTER; 1.
PE   3: Inferred from homology;
KW   Cell adhesion; Cell outer membrane; Membrane; Periplasm; Repeat; Secreted;
KW   Signal; Transmembrane; Transmembrane beta strand; Virulence.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000255"
FT   CHAIN           35..922
FT                   /note="Pertactin autotransporter"
FT                   /id="PRO_0000002708"
FT   CHAIN           35..643
FT                   /note="Outer membrane protein P.70"
FT                   /id="PRO_0000002709"
FT   CHAIN           644..922
FT                   /note="Pertactin translocator"
FT                   /id="PRO_0000002710"
FT   REPEAT          266..270
FT                   /note="1"
FT   REPEAT          271..275
FT                   /note="2"
FT   REPEAT          276..280
FT                   /note="3"
FT   REPEAT          281..285
FT                   /note="4; approximate"
FT   DOMAIN          654..922
FT                   /note="Autotransporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00556"
FT   REGION          266..290
FT                   /note="4 X 5 AA tandem repeats of G-G-A-V-P"
FT   REGION          561..619
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          575..603
FT                   /note="9 X 3 AA approximate repeats of P-Q-P"
FT   MOTIF           260..262
FT                   /note="Cell attachment site; involved in adhesion to
FT                   various eukaryotic cell lines"
FT   COMPBIAS        568..612
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            643..644
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   922 AA;  95178 MW;  3DF7BC58D4712478 CRC64;
     MNMSLSRIVK AAPLRRTTLA MALGALGAAP AAYADWNNQS IIKAGERQHG IHIKQSDGAG
     VRTATGTTIK VSGRQAQGVL LENPAAELRF QNGSVTSSGQ LFDEGVRRFL GTVTVKAGKL
     VADHATLANV SDTRDDDGIA LYVAGEQAQA SIADSTLQGA GGVRVERGAN VTVQRSTIVD
     GGLHIGTLQP LQPEDLPPSR VVLGDTSVTA VPASGAPAAV FVFGANELTV DGGHITGGRA
     AGVAAMDGAI VHLQRATIRR GDAPAGGAVP GGAVPGGAVP GGFGPLLDGW YGVDVSDSTV
     DLAQSIVEAP QLGAAIRAGR GARVTVSGGS LSAPHGNVIE TGGGARRFPP PASPLSITLQ
     AGARAQGRAL LYRVLPEPVK LTLAGGAQGQ GDIVATELPP IPGASSGPLD VALASQARWT
     GATRAVDSLS IDNATWVMTD NSNVGALRLA SDGSVDFQQP AEAGRFKVLM VDTLAGSGLF
     RMNVFADLGL SDKLVVMRDA SGQHRLWVRN SGSEPASGNT MLLVQTPRGS AATFTLANKD
     GKVDIGTYRY RLAANGNGQW SLVGAKAPPA PKPAPQPGPQ PGPQPPQPPQ PPQPPQPPQP
     PQRQPEAPAP QPPAGRELSA AANAAVNTGG VGLASTLWYA ESNALSKRLG ELRLNPDAGG
     AWGRGFAQRQ QLDNRAGRRF DQKVAGFELG ADHAVAVAGG RWHLGGLAGY TRGDRGFTGD
     GGGHTDSVHV GGYATYIANS GFYLDATLRA SRLENDFKVA GSDGYAVKGK YRTHGVGVSL
     EAGRRFAHAD GWFLEPQAEL AVFRVGGGAY RAANGLRVRD EGGSSVLGRL GLEVGKRIEL
     AGGRQVQPYI KASVLQEFDG AGTVRTNGIA HRTELRGTRA ELGLGMAAAL GRGHSLYASY
     EYSKGPKLAM PWTFHAGYRY SW