PTLH_BORPE
ID PTLH_BORPE Reviewed; 339 AA.
AC Q7VSX3;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Type IV secretion system protein PtlH;
DE EC=7.4.2.8 {ECO:0000250|UniProtKB:P37093};
DE AltName: Full=Pertussis toxin liberation protein H;
GN Name=ptlH; OrderedLocusNames=BP3796;
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, AND MUTAGENESIS OF GLY-175 AND LYS-176.
RC STRAIN=Tohama I / BP338;
RX PubMed=9393726; DOI=10.1128/jb.179.23.7577-7580.1997;
RA Kotob S.I., Burns D.L.;
RT "Essential role of the consensus nucleotide-binding site of PtlH in
RT secretion of pertussis toxin from Bordetella pertussis.";
RL J. Bacteriol. 179:7577-7580(1997).
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).
RN [8]
RP FUNCTION, ATPASE ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP LYS-176.
RC STRAIN=Tohama I / BP536;
RX PubMed=17339350; DOI=10.1128/iai.00008-07;
RA Verma A., Burns D.L.;
RT "Requirements for assembly of PtlH with the pertussis toxin transporter
RT apparatus of Bordetella pertussis.";
RL Infect. Immun. 75:2297-2306(2007).
CC -!- FUNCTION: ATPase component of the type IV secretion system Ptl required
CC for secretion of assembled pertussis toxin (PTX) through the outer
CC membrane (PubMed:10518754, PubMed:15322034, PubMed:8464913,
CC PubMed:9393726, PubMed:17339350). Acts as a molecular motor to provide
CC the energy that is required for the export of proteins (By similarity).
CC {ECO:0000250|UniProtKB:P37093, ECO:0000269|PubMed:10518754,
CC ECO:0000269|PubMed:15322034, ECO:0000269|PubMed:17339350,
CC ECO:0000269|PubMed:8464913, ECO:0000269|PubMed:9393726}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + cellular proteinSide 1 = ADP + phosphate +
CC cellular proteinSide 2.; EC=7.4.2.8;
CC Evidence={ECO:0000250|UniProtKB:P37093};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:17339350}; Peripheral membrane protein
CC {ECO:0000269|PubMed:17339350}; Cytoplasmic side
CC {ECO:0000269|PubMed:17339350}. Note=Membrane associated. Tight
CC association with the membrane is dependent on the toxin substrate,
CC certain other Ptl proteins, and ATP binding and/or hydrolysis.
CC {ECO:0000269|PubMed:17339350}.
CC -!- INDUCTION: Cotranscribed with ptxABCDE (PubMed:8606119). Activated by
CC the two-component regulatory system BvgS/BvgA (PubMed:7592424).
CC {ECO:0000269|PubMed:7592424, ECO:0000269|PubMed:8606119}.
CC -!- SIMILARITY: Belongs to the GSP E family. {ECO:0000305}.
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DR EMBL; L10720; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX640422; CAE44051.1; -; Genomic_DNA.
DR RefSeq; NP_882295.1; NC_002929.2.
DR RefSeq; WP_010929500.1; NZ_CP039022.1.
DR AlphaFoldDB; Q7VSX3; -.
DR SMR; Q7VSX3; -.
DR STRING; 257313.BP3796; -.
DR GeneID; 66440821; -.
DR KEGG; bpe:BP3796; -.
DR PATRIC; fig|257313.5.peg.4100; -.
DR eggNOG; COG0630; Bacteria.
DR HOGENOM; CLU_005379_3_1_4; -.
DR OMA; EAWVEKK; -.
DR Proteomes; UP000002676; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043684; C:type IV secretion system complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008564; F:protein-exporting ATPase activity; IEA:UniProtKB-EC.
DR GO; GO:0044097; P:secretion by the type IV secretion system; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR InterPro; IPR001482; T2SS/T4SS.
DR InterPro; IPR014155; VirB11.
DR Pfam; PF00437; T2SSE; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02788; VirB11; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Protein transport; Reference proteome; Translocase;
KW Transport; Virulence.
FT CHAIN 1..339
FT /note="Type IV secretion system protein PtlH"
FT /id="PRO_0000262579"
FT BINDING 170..177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 175
FT /note="G->S: Strongly reduces PTX secretion."
FT /evidence="ECO:0000269|PubMed:9393726"
FT MUTAGEN 176
FT /note="K->A: Strongly reduces PTX secretion. Loss of ATPase
FT activity."
FT /evidence="ECO:0000269|PubMed:17339350,
FT ECO:0000269|PubMed:9393726"
SQ SEQUENCE 339 AA; 37159 MW; E55F352341DBDA3E CRC64;
MNDAAPDRQA SVDFHLQALH PWLSRQDIAE ICVNRPGQLW YEDRNGWNRQ ESGALTLDHL
HALATATARF CDRDICPERP LLAASLPGGE RVQIVVPPAC EPGTLSLTIR KPARRIWPLS
ELLRDTLDLP GVPGASQARP DPLLDPWRRG AWDDFLRLAV QAGKAILVAG QTGSGKTTLM
NALSGEIPPR ERIVTIEDVR ELRLDPATNH VHLLYGTPTE GRTAAVSATE LLRAALRMAP
TRILLAELRG GEAFDFLQAC ASGHSGGIST CHAASADMAL QRLTLMCMQH PNCQMLPYST
LRALVESVID IVVVVERRAG QGARRRVVDI WYRDGLPAP
