PTLD_BORPE
ID PTLD_BORPE Reviewed; 463 AA.
AC Q7VSX8;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Type IV secretion system protein PtlD;
DE AltName: Full=Pertussis toxin liberation protein D;
DE Flags: Precursor;
GN Name=ptlD; OrderedLocusNames=BP3791;
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 FUNCTION.
RC STRAIN=Tohama I / BP338;
RX PubMed=8464913; DOI=10.1073/pnas.90.7.2970;
RA Weiss A.A., Johnson F.D., Burns D.L.;
RT "Molecular characterization of an operon required for pertussis toxin
RT secretion.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:2970-2974(1993).
RN [2]
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 [3]
RP REGULATION BY BVGS/BVGA.
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX PubMed=7592424; DOI=10.1128/jb.177.22.6486-6491.1995;
RA Boucher P.E., Stibitz S.;
RT "Synergistic binding of RNA polymerase and BvgA phosphate to the pertussis
RT toxin promoter of Bordetella pertussis.";
RL J. Bacteriol. 177:6486-6491(1995).
RN [4]
RP COTRANSCRIPTION WITH PTX.
RC STRAIN=Wellcome 28;
RX PubMed=8606119; DOI=10.1128/iai.64.4.1458-1460.1996;
RA Ricci S., Rappuoli R., Scarlato V.;
RT "The pertussis toxin liberation genes of Bordetella pertussis are
RT transcriptionally linked to the pertussis toxin operon.";
RL Infect. Immun. 64:1458-1460(1996).
RN [5]
RP FUNCTION.
RC STRAIN=Tohama I / BP338;
RX PubMed=10518754; DOI=10.1111/j.1574-6968.1999.tb08766.x;
RA Craig-Mylius K.A., Weiss A.A.;
RT "Mutants in the ptlA-H genes of Bordetella pertussis are deficient for
RT pertussis toxin secretion.";
RL FEMS Microbiol. Lett. 179:479-484(1999).
RN [6]
RP FUNCTION.
RC STRAIN=Tohama I / BP338;
RX PubMed=15322034; DOI=10.1128/iai.72.9.5365-5372.2004;
RA Burns D.L., Fiddner S., Cheung A.M., Verma A.;
RT "Analysis of subassemblies of pertussis toxin subunits in vivo and their
RT interaction with the ptl transport apparatus.";
RL Infect. Immun. 72:5365-5372(2004).
CC -!- FUNCTION: Component of the type IV secretion system ptl required for
CC secretion of assembled pertussis toxin (PTX) through the outer
CC membrane. {ECO:0000269|PubMed:10518754, ECO:0000269|PubMed:15322034,
CC ECO:0000269|PubMed:8464913}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Cotranscribed with ptxABCDE. Activated by the two-component
CC regulatory system BvgS/BvgA.
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DR EMBL; L10720; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX640422; CAE44046.1; -; Genomic_DNA.
DR RefSeq; NP_882290.1; NC_002929.2.
DR RefSeq; WP_010931653.1; NZ_CP039022.1.
DR AlphaFoldDB; Q7VSX8; -.
DR STRING; 257313.BP3791; -.
DR GeneID; 45390937; -.
DR KEGG; bpe:BP3791; -.
DR PATRIC; fig|257313.5.peg.4095; -.
DR HOGENOM; CLU_592732_0_0_4; -.
DR OMA; LMMAMYE; -.
DR Proteomes; UP000002676; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030255; P:protein secretion by the type IV secretion system; IEA:InterPro.
DR InterPro; IPR007688; Conjugal_tfr_TrbL/VirB6.
DR Pfam; PF04610; TrbL; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..463
FT /note="Type IV secretion system protein PtlD"
FT /id="PRO_0000262575"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 376..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 463 AA; 48679 MW; 1D389F3183FAE2BB CRC64;
MAGLSRILLS CTLACLLAGQ AAQASVDDPT RAGGDNRVRA LRADQARRDV LLTACRDDPG
HRRGEPDCVN AERAQALQQW QAAAMTSVDA AFSDLAGALR NAAPRRMEAA IVRLTRQLQP
LVYSMMTLLV LLTGYALLAR RDRPFEWHIR HALLVAVVTS LALSPDRYLS TVVAGVQDVA
GWLSGPWTAP DGAAGRGGLA QLDQFAAQAQ AWVAQLAGQA ANDANPGSAV NWLLCAMIVA
ASAGGWLCLA ASLLIVPGLI VTLLLSLGPL FLVLLLFPAL QRWTNAWLGA LVRALVFMAL
GTPAVGLLSD VLAGALPAGL PQRFATDPLR STMLAATLCA TATLMLLTLV PLASSVNAGL
RRRLWPNAAH PGLAQAHRQA AARQYAPRPA AAAAAAGPHQ AGTYAASATP APAPARPAPS
FPAHAYRQYA LGGARRPPPR VRRDDRPAPA PDRRVLPRKP NLP
