PTLE_BORPE
ID PTLE_BORPE Reviewed; 233 AA.
AC Q7VSX6;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Type IV secretion system protein PtlE;
DE AltName: Full=Pertussis toxin liberation protein E;
GN Name=ptlE; OrderedLocusNames=BP3793;
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 SUBCELLULAR LOCATION.
RC STRAIN=Tohama I / BP338;
RX PubMed=8071211; DOI=10.1128/jb.176.17.5350-5356.1994;
RA Johnson F.D., Burns D.L.;
RT "Detection and subcellular localization of three Ptl proteins involved in
RT the secretion of pertussis toxin from Bordetella pertussis.";
RL J. Bacteriol. 176:5350-5356(1994).
RN [4]
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 [5]
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 [6]
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 [7]
RP FUNCTION AS A POSSIBLE PEPTIDOGLYCANASE, AND MUTAGENESIS OF ASP-10 AND
RP GLU-19.
RC STRAIN=Tohama I / BP338;
RX PubMed=12003925; DOI=10.1128/jb.184.11.2863-2869.2002;
RA Rambow-Larsen A.A., Weiss A.A.;
RT "The PtlE protein of Bordetella pertussis has peptidoglycanase activity
RT required for Ptl-mediated pertussis toxin secretion.";
RL J. Bacteriol. 184:2863-2869(2002).
RN [8]
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. Could possess peptidoglycanase activity.
CC {ECO:0000269|PubMed:10518754, ECO:0000269|PubMed:12003925,
CC ECO:0000269|PubMed:15322034, ECO:0000269|PubMed:8464913}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}.
CC -!- INDUCTION: Cotranscribed with ptxABCDE. Activated by the two-component
CC regulatory system BvgS/BvgA.
CC -!- SIMILARITY: Belongs to the virB8 family. {ECO:0000305}.
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DR EMBL; L10720; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX640422; CAE44048.1; -; Genomic_DNA.
DR RefSeq; NP_882292.1; NC_002929.2.
DR RefSeq; WP_010929498.1; NZ_CP039022.1.
DR AlphaFoldDB; Q7VSX6; -.
DR SMR; Q7VSX6; -.
DR STRING; 257313.BP3793; -.
DR GeneID; 66440818; -.
DR KEGG; bpe:BP3793; -.
DR PATRIC; fig|257313.5.peg.4097; -.
DR eggNOG; COG3736; Bacteria.
DR HOGENOM; CLU_068461_1_1_4; -.
DR OMA; DLIQVRY; -.
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; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR007430; VirB8.
DR InterPro; IPR026264; VirB8/PtlE.
DR Pfam; PF04335; VirB8; 1.
DR PIRSF; PIRSF003299; VirB8_PtlE; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..233
FT /note="Type IV secretion system protein PtlE"
FT /id="PRO_0000262576"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MUTAGEN 10
FT /note="D->A: Strong reduction of PTX secretion. Even
FT stronger reduction of PTX secretion; when associated with
FT A-19."
FT /evidence="ECO:0000269|PubMed:12003925"
FT MUTAGEN 19
FT /note="E->A: Strong reduction of PTX secretion. Slightly
FT stronger reduction of PTX secretion; when associated with
FT A-10."
FT /evidence="ECO:0000269|PubMed:12003925"
SQ SEQUENCE 233 AA; 25994 MW; 3F0B9F23B5E4BD01 CRC64;
MPDPRPLTPD QTHGRGHAEA AVDWEASRLY RLAQSERRAW TVAWAALAVT ALSLIAIATM
LPLKTTIPYL IEVEKSSGAA SVVTQFEPRD FTPDTLMNQY WLTRYVAARE RYDWHTIQHD
YDYVRLLSAP AVRHDYETSY EAPDAPDRKY GAGTTLAVKI LSAIDHGKGV GTVRFVRTRR
DADGQGAAES SIWVATVAFA YDQPRALTQA QRWLNPLGFA VTSYRVDAEA GQP
