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Pertactin autotransporter (P.93) [Cleaved into: Outer membrane protein P.69; Pertactin translocator]

 PERT_BORPE              Reviewed;         910 AA.
P14283;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 3.
20-JUN-2018, entry version 136.
RecName: Full=Pertactin autotransporter;
AltName: Full=P.93;
Contains:
RecName: Full=Outer membrane protein P.69;
Contains:
RecName: Full=Pertactin translocator;
Flags: Precursor;
Name=prn; Synonyms=omp69A; OrderedLocusNames=BP1054;
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
Alcaligenaceae; Bordetella.
NCBI_TaxID=257313;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=CN2992;
PubMed=2542937; DOI=10.1073/pnas.86.10.3554;
Charles I.G., Dougan G., Pickard D., Chatfield S., Smith M.,
Novotny P., Morrissey P., Fairweather N.F.;
"Molecular cloning and characterization of protective outer membrane
protein P.69 from Bordetella pertussis.";
Proc. Natl. Acad. Sci. U.S.A. 86:3554-3558(1989).
[2]
SEQUENCE REVISION TO 264 AND 332.
PubMed=1527510; DOI=10.1099/00221287-138-8-1697;
Li J.L., Fairweather N.F., Novotny P., Dougan G., Charles I.G.;
"Cloning, nucleotide sequence and heterologous expression of the
protective outer-membrane protein P.68 pertactin from Bordetella
bronchiseptica.";
J. Gen. Microbiol. 138:1697-1705(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
PubMed=12910271; DOI=10.1038/ng1227;
Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
Chillingworth T., Collins M., Cronin A., Davis P., Doggett J.,
Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K.,
Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C.,
Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K.,
Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K.,
Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
"Comparative analysis of the genome sequences of Bordetella pertussis,
Bordetella parapertussis and Bordetella bronchiseptica.";
Nat. Genet. 35:32-40(2003).
[4]
CRYSTALLIZATION.
PubMed=17620719; DOI=10.1107/S1744309107028308;
Zhu Y., Black I., Roszak A.W., Isaacs N.W.;
"Crystallization and preliminary X-ray diffraction analysis of P30,
the transmembrane domain of pertactin, an autotransporter from
Bordetella pertussis.";
Acta Crystallogr. F 63:593-595(2007).
[5]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=8609998; DOI=10.1038/381090a0;
Emsley P., Charles I.G., Fairweather N.F., Isaacs N.W.;
"Structure of Bordetella pertussis virulence factor P.69 pertactin.";
Nature 381:90-92(1996).
-!- 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.
-----------------------------------------------------------------------
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EMBL; J04560; AAA22980.1; ALT_SEQ; Genomic_DNA.
EMBL; BX640414; CAE41353.1; -; Genomic_DNA.
RefSeq; NP_879839.1; NC_002929.2.
RefSeq; WP_010930159.1; NC_002929.2.
PDB; 1DAB; X-ray; 2.50 A; A=35-573.
PDBsum; 1DAB; -.
ProteinModelPortal; P14283; -.
SMR; P14283; -.
STRING; 257313.BP1054; -.
TCDB; 1.B.12.2.1; the autotransporter-1 (at-1) family.
PRIDE; P14283; -.
EnsemblBacteria; CAE41353; CAE41353; BP1054.
GeneID; 2664290; -.
KEGG; bpe:BP1054; -.
PATRIC; fig|257313.5.peg.1126; -.
eggNOG; ENOG4108P8G; Bacteria.
eggNOG; COG3468; LUCA.
HOGENOM; HOG000115499; -.
KO; K12681; -.
OMA; YATYIAN; -.
BioCyc; BPER257313:BP1054-MONOMER; -.
EvolutionaryTrace; P14283; -.
Proteomes; UP000002676; Chromosome.
GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
Gene3D; 2.160.20.20; -; 1.
InterPro; IPR005546; Autotransporte_beta.
InterPro; IPR036709; Autotransporte_beta_dom_sf.
InterPro; IPR006315; OM_autotransptr_brl.
InterPro; IPR012332; P22_tailspike-like_C_sf.
InterPro; IPR011050; Pectin_lyase_fold/virulence.
InterPro; IPR003992; Pertactin.
InterPro; IPR004899; Pertactin_central.
InterPro; IPR003991; Pertactin_virulence_factor.
Pfam; PF03797; Autotransporter; 1.
Pfam; PF03212; Pertactin; 1.
PRINTS; PR01482; PERTACTIN.
PRINTS; PR01484; PRTACTNFAMLY.
SMART; SM00869; Autotransporter; 1.
SUPFAM; SSF103515; SSF103515; 1.
SUPFAM; SSF51126; SSF51126; 1.
TIGRFAMs; TIGR01414; autotrans_barl; 1.
PROSITE; PS51208; AUTOTRANSPORTER; 1.
1: Evidence at protein level;
3D-structure; Cell adhesion; Cell outer membrane; Complete proteome;
Direct protein sequencing; Membrane; Periplasm; Reference proteome;
Repeat; Secreted; Signal; Transmembrane; Transmembrane beta strand;
Virulence.
SIGNAL 1 34
CHAIN 35 910 Pertactin autotransporter.
/FTId=PRO_0000002705.
CHAIN 35 631 Outer membrane protein P.69.
/FTId=PRO_0000002706.
CHAIN 632 910 Pertactin translocator.
/FTId=PRO_0000002707.
REPEAT 266 270 1.
REPEAT 271 275 2.
REPEAT 276 280 3.
REPEAT 281 285 4; approximate.
REPEAT 286 290 5; approximate.
DOMAIN 642 910 Autotransporter. {ECO:0000255|PROSITE-
ProRule:PRU00556}.
REGION 266 290 5 X 5 AA tandem repeats of G-G-A-V-P.
REGION 579 593 5 X 3 AA tandem repeats of P-Q-P.
MOTIF 260 262 Cell attachment site; involved in
adhesion to various eukaryotic cell
lines.
SITE 631 632 Cleavage. {ECO:0000250}.
STRAND 40 43 {ECO:0000244|PDB:1DAB}.
STRAND 50 53 {ECO:0000244|PDB:1DAB}.
STRAND 60 66 {ECO:0000244|PDB:1DAB}.
STRAND 68 71 {ECO:0000244|PDB:1DAB}.
STRAND 78 92 {ECO:0000244|PDB:1DAB}.
STRAND 94 97 {ECO:0000244|PDB:1DAB}.
STRAND 104 107 {ECO:0000244|PDB:1DAB}.
STRAND 112 124 {ECO:0000244|PDB:1DAB}.
STRAND 126 129 {ECO:0000244|PDB:1DAB}.
TURN 133 135 {ECO:0000244|PDB:1DAB}.
STRAND 139 145 {ECO:0000244|PDB:1DAB}.
STRAND 148 154 {ECO:0000244|PDB:1DAB}.
STRAND 156 159 {ECO:0000244|PDB:1DAB}.
STRAND 162 166 {ECO:0000244|PDB:1DAB}.
STRAND 170 175 {ECO:0000244|PDB:1DAB}.
STRAND 183 186 {ECO:0000244|PDB:1DAB}.
STRAND 199 205 {ECO:0000244|PDB:1DAB}.
STRAND 207 210 {ECO:0000244|PDB:1DAB}.
STRAND 217 237 {ECO:0000244|PDB:1DAB}.
STRAND 239 248 {ECO:0000244|PDB:1DAB}.
STRAND 250 260 {ECO:0000244|PDB:1DAB}.
STRAND 266 270 {ECO:0000244|PDB:1DAB}.
STRAND 281 283 {ECO:0000244|PDB:1DAB}.
STRAND 294 309 {ECO:0000244|PDB:1DAB}.
STRAND 311 313 {ECO:0000244|PDB:1DAB}.
STRAND 316 324 {ECO:0000244|PDB:1DAB}.
STRAND 328 347 {ECO:0000244|PDB:1DAB}.
STRAND 354 356 {ECO:0000244|PDB:1DAB}.
STRAND 359 364 {ECO:0000244|PDB:1DAB}.
STRAND 368 377 {ECO:0000244|PDB:1DAB}.
STRAND 383 387 {ECO:0000244|PDB:1DAB}.
STRAND 392 398 {ECO:0000244|PDB:1DAB}.
STRAND 403 405 {ECO:0000244|PDB:1DAB}.
HELIX 407 409 {ECO:0000244|PDB:1DAB}.
STRAND 413 418 {ECO:0000244|PDB:1DAB}.
STRAND 422 425 {ECO:0000244|PDB:1DAB}.
STRAND 430 437 {ECO:0000244|PDB:1DAB}.
STRAND 439 442 {ECO:0000244|PDB:1DAB}.
STRAND 446 454 {ECO:0000244|PDB:1DAB}.
STRAND 458 461 {ECO:0000244|PDB:1DAB}.
STRAND 472 480 {ECO:0000244|PDB:1DAB}.
STRAND 483 489 {ECO:0000244|PDB:1DAB}.
HELIX 490 492 {ECO:0000244|PDB:1DAB}.
STRAND 497 504 {ECO:0000244|PDB:1DAB}.
STRAND 506 514 {ECO:0000244|PDB:1DAB}.
STRAND 525 529 {ECO:0000244|PDB:1DAB}.
STRAND 537 540 {ECO:0000244|PDB:1DAB}.
HELIX 543 545 {ECO:0000244|PDB:1DAB}.
STRAND 546 549 {ECO:0000244|PDB:1DAB}.
STRAND 552 557 {ECO:0000244|PDB:1DAB}.
STRAND 560 566 {ECO:0000244|PDB:1DAB}.
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


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