ID Q93L98_BORPT Unreviewed; 920 AA.
AC Q93L98;
DT 01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Pertactin {ECO:0000313|EMBL:AAN84471.1, ECO:0000313|EMBL:CAC42396.1};
GN Name=prn9 {ECO:0000313|EMBL:CAC42396.1};
GN Synonyms=prnA {ECO:0000313|EMBL:AAN84471.1};
OS Bordetella pertussis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=520 {ECO:0000313|EMBL:CAC42396.1};
RN [1] {ECO:0000313|EMBL:CAC42396.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B1679 {ECO:0000313|EMBL:CAC42396.1};
RA Heuvelman K., Peppler M.S., Lewandowski A., Mooi F.R.;
RT "Bordetella pertussis prn gene for pertactin.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAN84471.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MO-121 {ECO:0000313|EMBL:AAN84471.1};
RA Neal S.E., Fry N.K., Hanauer S., Blank E., Harrison T.G.;
RT "Molecular investigation of a Bordetella pertussis outbreak in Missouri,
RT USA, identifies a dominant clone.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; AF456356; AAN84471.1; -; Genomic_DNA.
DR EMBL; AJ315611; CAC42396.1; -; Genomic_DNA.
DR RefSeq; WP_023999318.1; NZ_CP054122.1.
DR AlphaFoldDB; Q93L98; -.
DR SMR; Q93L98; -.
DR GO; GO:0019867; C:outer membrane; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR CDD; cd01343; PL1_Passenger_AT; 1.
DR Gene3D; 2.160.20.20; -; 1.
DR Gene3D; 2.40.128.130; Autotransporter beta-domain; 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_dom.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR003992; Pertactin.
DR InterPro; IPR004899; Pertactin_central.
DR InterPro; IPR003991; Pertactin_virulence_factor.
DR NCBIfam; TIGR01414; autotrans_barl; 1.
DR PANTHER; PTHR35037:SF7; AUTOTRANSPORTER PROTEIN-RELATED; 1.
DR PANTHER; PTHR35037; C-TERMINAL REGION OF AIDA-LIKE PROTEIN; 1.
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; Autotransporter; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS51208; AUTOTRANSPORTER; 1.
PE 4: Predicted;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..920
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007715691"
FT DOMAIN 652..920
FT /note="Autotransporter"
FT /evidence="ECO:0000259|PROSITE:PS51208"
FT REGION 575..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..610
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 920 AA; 94318 MW; 62AA9461DCF53E54 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 GGAVPGGFGP GGFGPGGFGP 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
//