PTLG_BORPE
ID PTLG_BORPE Reviewed; 374 AA.
AC Q7VSX4;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Type IV secretion system protein PtlG;
DE AltName: Full=Pertussis toxin liberation protein G;
GN Name=ptlG; OrderedLocusNames=BP3795;
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.
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}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Cotranscribed with ptxABCDE. Activated by the two-component
CC regulatory system BvgS/BvgA.
CC -!- SIMILARITY: Belongs to the TrbI/VirB10 family. {ECO:0000305}.
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DR EMBL; L10720; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX640422; CAE44050.1; -; Genomic_DNA.
DR RefSeq; NP_882294.1; NC_002929.2.
DR RefSeq; WP_010931655.1; NZ_CP039022.1.
DR AlphaFoldDB; Q7VSX4; -.
DR SMR; Q7VSX4; -.
DR STRING; 257313.BP3795; -.
DR GeneID; 45390941; -.
DR KEGG; bpe:BP3795; -.
DR PATRIC; fig|257313.5.peg.4099; -.
DR eggNOG; COG2948; Bacteria.
DR HOGENOM; CLU_041899_7_0_4; -.
DR OMA; PGKDRNT; -.
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 CDD; cd16429; VirB10; 1.
DR Gene3D; 2.40.128.260; -; 1.
DR InterPro; IPR005498; T4SS_VirB10/TraB/TrbI.
DR InterPro; IPR042217; T4SS_VirB10/TrbI.
DR Pfam; PF03743; TrbI; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..374
FT /note="Type IV secretion system protein PtlG"
FT /id="PRO_0000262578"
FT TRANSMEM 38..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 86..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..117
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 374 AA; 39471 MW; 082C94EF938BE6FD CRC64;
MLNRPSSPDG GEAHAWPPDP EIPVFANAEH AHRRPLRWMF ALVAVALSCL LATGIWRSRA
APPHAATQTV APAGQALPPG RIFTVHPREP EPAPLPDMPA APDPILPQPR PAPPVPPPPI
RAPYDYDEPA PRRDSAALKS GPAMMVATAA RLGQTERAGM ADDGVSADAA TLIGRNVSRA
TRSGGRDYRL LPGTFIDCIL QTRIVTNVPG LTTCIVSRDV YSASGKRVLV PRGTTVVGEY
RADLAQGSQR IYVAWSRLFM PSGLTIELAS PAVDGTGAAG LPGVVDDKFA QRFGGALLLS
VLGDATSYML ARATDARHGV NVNLTAAGTM NSLAASALNN TINIPPTLYK NHGDQIGILV
ARPLDFSILR GTNE
