PERT_BORBR
ID PERT_BORBR Reviewed; 916 AA.
AC Q03035;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2003, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Pertactin autotransporter;
DE AltName: Full=P.94;
DE Contains:
DE RecName: Full=Outer membrane protein P.68;
DE Contains:
DE RecName: Full=Pertactin translocator;
DE Flags: Precursor;
GN Name=prn; OrderedLocusNames=BB1366;
OS Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
OS (Alcaligenes bronchisepticus).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257310;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 38-47.
RC STRAIN=CN7531;
RX PubMed=1527510; DOI=10.1099/00221287-138-8-1697;
RA Li J.L., Fairweather N.F., Novotny P., Dougan G., Charles I.G.;
RT "Cloning, nucleotide sequence and heterologous expression of the protective
RT outer-membrane protein P.68 pertactin from Bordetella bronchiseptica.";
RL J. Gen. Microbiol. 138:1697-1705(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
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 -!- INTERACTION:
CC Q03035; Q775D6: mtd; Xeno; NbExp=8; IntAct=EBI-15556835, EBI-15556799;
CC -!- SUBCELLULAR LOCATION: [Pertactin autotransporter]: Periplasm
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Outer membrane protein P.68]: 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; X54815; CAA38584.1; -; Genomic_DNA.
DR EMBL; BX640441; CAE31864.1; -; Genomic_DNA.
DR PIR; A47675; A47675.
DR RefSeq; WP_010926141.1; NC_002927.3.
DR PDB; 2IOU; X-ray; 3.16 A; G/H=38-572.
DR PDBsum; 2IOU; -.
DR AlphaFoldDB; Q03035; -.
DR SMR; Q03035; -.
DR DIP; DIP-46044N; -.
DR IntAct; Q03035; 1.
DR STRING; 257310.BB1366; -.
DR EnsemblBacteria; CAE31864; CAE31864; BB1366.
DR KEGG; bbr:BB1366; -.
DR eggNOG; COG3468; Bacteria.
DR HOGENOM; CLU_002318_1_1_4; -.
DR OMA; KAGERQH; -.
DR OrthoDB; 1713183at2; -.
DR EvolutionaryTrace; Q03035; -.
DR Proteomes; UP000001027; 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 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell outer membrane;
KW Direct protein sequencing; Membrane; Periplasm; Repeat; Secreted; Signal;
KW Transmembrane; Transmembrane beta strand; Virulence.
FT SIGNAL 1..37
FT /evidence="ECO:0000269|PubMed:1527510"
FT CHAIN 38..916
FT /note="Pertactin autotransporter"
FT /id="PRO_0000002702"
FT CHAIN 38..637
FT /note="Outer membrane protein P.68"
FT /id="PRO_0000002703"
FT CHAIN 638..916
FT /note="Pertactin translocator"
FT /id="PRO_0000002704"
FT REPEAT 269..273
FT /note="1"
FT REPEAT 274..278
FT /note="2"
FT REPEAT 279..283
FT /note="3"
FT REPEAT 284..288
FT /note="4; approximate"
FT DOMAIN 648..916
FT /note="Autotransporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00556"
FT REGION 269..288
FT /note="4 X 5 AA tandem repeats of G-G-A-V-P"
FT REGION 564..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..606
FT /note="6 X 3 AA repeats of P-Q-P"
FT MOTIF 263..265
FT /note="Cell attachment site; involved in adhesion to
FT various eukaryotic cell lines"
FT MOTIF 706..708
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 571..606
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 637..638
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT CONFLICT 10
FT /note="K -> L (in Ref. 1; CAA38584)"
FT /evidence="ECO:0000305"
FT CONFLICT 29..31
FT /note="Missing (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="H -> Y (in Ref. 1; CAA38584)"
FT /evidence="ECO:0000305"
FT CONFLICT 281..285
FT /note="Missing (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="V -> C (in Ref. 1; CAA38584)"
FT /evidence="ECO:0000305"
FT CONFLICT 510
FT /note="W -> L (in Ref. 1; CAA38584)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="A -> G (in Ref. 1; CAA38584)"
FT /evidence="ECO:0000305"
FT CONFLICT 595
FT /note="P -> PQPP (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 803
FT /note="A -> S (in Ref. 1; CAA38584)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 916 AA; 94352 MW; BA9C62D4E94E49AA CRC64;
MNMSLSRIVK AAPLRRTTLA MALGALGALG AAPAAHADWN NQSIIKAGER QHGIHIKQSD
GAGVRTATGT TIKVSGRQAQ GVLLENPAAE LRFQNGSVTS SGQLFDEGVR RFLGTVTVKA
GKLVADHATL ANVSDTRDDD GIALYVAGEQ AQASIADSTL QGAGGVRVER GANVTVQRST
IVDGGLHIGT LQPLQPEDLP PSRVVLGDTS VTAVPASGAP AAVSVFGANE LTVDGGHITG
GRAAGVAAMD GAIVHLQRAT IRRGDAPAGG AVPGGAVPGG AVPGGFGPLL DGWYGVDVSD
STVDLAQSIV EAPQLGAAIR AGRGARVTVS GGSLSAPHGN VIETGGGARR FPPPASPLSI
TLQAGARAQG RALLYRVLPE PVKLTLAGGA QGQGDIVATE LPPIPGASSG PLDVALASQA
RWTGATRAVD SLSIDNATWV MTDNSNVGAL RLASDGSVDF QQPAEAGRFK VLMVDTLAGS
GLFRMNVFAD LGLSDKLVVM RDASGQHRLW VRNSGSEPAS ANTMLLVQTP RGSAATFTLA
NKDGKVDIGT YRYRLAANGN GQWSLVGAKA PPAPKPAPQP GPQPGPQPPQ PPQPPQRQPE
APAPQPPAGR ELSAAANAAV NTGGVGLAST LWYAESNALS KRLGELRLNP DAGGAWGRGF
AQRQQLDNRA GRRFDQKVAG FELGADHAVA VAGGRWHLGG LAGYTRGDRG FTGDGGGHTD
SVHVGGYATY IANSGFYLDA TLRASRLEND FKVAGSDGYA VKGKYRTHGV GASLEAGRRF
AHADGWFLEP QAELAVFRVG GGAYRAANGL RVRDEGGSSV LGRLGLEVGK RIELAGGRQV
QPYIKASVLQ EFDGAGTVRT NGIAHRTELR GTRAELGLGM AAALGRGHSL YASYEYSKGP
KLAMPWTFHA GYRYSW
