PERT_BORPE
ID PERT_BORPE Reviewed; 910 AA.
AC P14283;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 3.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=Pertactin autotransporter;
DE AltName: Full=P.93;
DE Contains:
DE RecName: Full=Outer membrane protein P.69;
DE Contains:
DE RecName: Full=Pertactin translocator;
DE Flags: Precursor;
GN Name=prn; Synonyms=omp69A; OrderedLocusNames=BP1054;
OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257313;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=CN2992;
RX PubMed=2542937; DOI=10.1073/pnas.86.10.3554;
RA Charles I.G., Dougan G., Pickard D., Chatfield S., Smith M., Novotny P.,
RA Morrissey P., Fairweather N.F.;
RT "Molecular cloning and characterization of protective outer membrane
RT protein P.69 from Bordetella pertussis.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:3554-3558(1989).
RN [2]
RP SEQUENCE REVISION TO 264 AND 332.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
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).
RN [4]
RP CRYSTALLIZATION.
RX PubMed=17620719; DOI=10.1107/s1744309107028308;
RA Zhu Y., Black I., Roszak A.W., Isaacs N.W.;
RT "Crystallization and preliminary X-ray diffraction analysis of P30, the
RT transmembrane domain of pertactin, an autotransporter from Bordetella
RT pertussis.";
RL Acta Crystallogr. F 63:593-595(2007).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=8609998; DOI=10.1038/381090a0;
RA Emsley P., Charles I.G., Fairweather N.F., Isaacs N.W.;
RT "Structure of Bordetella pertussis virulence factor P.69 pertactin.";
RL Nature 381:90-92(1996).
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.69]: 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 concentration.
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DR EMBL; J04560; AAA22980.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BX640414; CAE41353.1; -; Genomic_DNA.
DR RefSeq; NP_879839.1; NC_002929.2.
DR RefSeq; WP_010930159.1; NZ_CP039022.1.
DR PDB; 1DAB; X-ray; 2.50 A; A=35-573.
DR PDBsum; 1DAB; -.
DR AlphaFoldDB; P14283; -.
DR SMR; P14283; -.
DR STRING; 257313.BP1054; -.
DR TCDB; 1.B.12.2.1; the autotransporter-1 (at-1) family.
DR KEGG; bpe:BP1054; -.
DR PATRIC; fig|257313.5.peg.1126; -.
DR eggNOG; COG3468; Bacteria.
DR HOGENOM; CLU_002318_1_1_4; -.
DR OMA; KAGERQH; -.
DR EvolutionaryTrace; P14283; -.
DR Proteomes; UP000002676; 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; Reference proteome; Repeat;
KW Secreted; Signal; Transmembrane; Transmembrane beta strand; Virulence.
FT SIGNAL 1..34
FT CHAIN 35..910
FT /note="Pertactin autotransporter"
FT /id="PRO_0000002705"
FT CHAIN 35..631
FT /note="Outer membrane protein P.69"
FT /id="PRO_0000002706"
FT CHAIN 632..910
FT /note="Pertactin translocator"
FT /id="PRO_0000002707"
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 REPEAT 286..290
FT /note="5; approximate"
FT DOMAIN 642..910
FT /note="Autotransporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00556"
FT REGION 266..290
FT /note="5 X 5 AA tandem repeats of G-G-A-V-P"
FT REGION 565..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..593
FT /note="5 X 3 AA tandem 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 572..600
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 631..632
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 78..92
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 112..124
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:1DAB"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 217..237
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 239..248
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 250..260
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 266..270
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 294..309
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 316..324
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 328..347
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 359..364
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 368..377
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 383..387
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 392..398
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:1DAB"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 413..418
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 422..425
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 430..437
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 439..442
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 446..454
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 458..461
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 472..480
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 483..489
FT /evidence="ECO:0007829|PDB:1DAB"
FT HELIX 490..492
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 497..504
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 506..514
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 525..529
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 537..540
FT /evidence="ECO:0007829|PDB:1DAB"
FT HELIX 543..545
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 546..549
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 552..557
FT /evidence="ECO:0007829|PDB:1DAB"
FT STRAND 560..566
FT /evidence="ECO:0007829|PDB:1DAB"
SQ SEQUENCE 910 AA; 93453 MW; A169871E20A2E7DB CRC64;
MNMSLSRIVK AAPLRRTTLA MALGALGAAP AAHADWNNQS IVKTGERQHG IHIQGSDPGG
VRTASGTTIK VSGRQAQGIL LENPAAELQF RNGSVTSSGQ LSDDGIRRFL GTVTVKAGKL
VADHATLANV GDTWDDDGIA LYVAGEQAQA SIADSTLQGA GGVQIERGAN VTVQRSAIVD
GGLHIGALQS LQPEDLPPSR VVLRDTNVTA VPASGAPAAV SVLGASELTL DGGHITGGRA
AGVAAMQGAV VHLQRATIRR GDAPAGGAVP GGAVPGGAVP GGFGPGGFGP VLDGWYGVDV
SGSSVELAQS IVEAPELGAA IRVGRGARVT VSGGSLSAPH GNVIETGGAR RFAPQAAPLS
ITLQAGAHAQ GKALLYRVLP EPVKLTLTGG ADAQGDIVAT ELPSIPGTSI GPLDVALASQ
ARWTGATRAV DSLSIDNATW VMTDNSNVGA LRLASDGSVD FQQPAEAGRF KVLTVNTLAG
SGLFRMNVFA DLGLSDKLVV MQDASGQHRL WVRNSGSEPA SANTLLLVQT PLGSAATFTL
ANKDGKVDIG TYRYRLAANG NGQWSLVGAK APPAPKPAPQ PGPQPPQPPQ PQPEAPAPQP
PAGRELSAAA NAAVNTGGVG LASTLWYAES NALSKRLGEL RLNPDAGGAW GRGFAQRQQL
DNRAGRRFDQ KVAGFELGAD HAVAVAGGRW HLGGLAGYTR GDRGFTGDGG GHTDSVHVGG
YATYIADSGF YLDATLRASR LENDFKVAGS DGYAVKGKYR THGVGASLEA GRRFTHADGW
FLEPQAELAV FRAGGGAYRA ANGLRVRDEG GSSVLGRLGL EVGKRIELAG GRQVQPYIKA
SVLQEFDGAG TVHTNGIAHR TELRGTRAEL GLGMAAALGR GHSLYASYEY SKGPKLAMPW
TFHAGYRYSW
