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PTLC_BORPE
ID   PTLC_BORPE              Reviewed;         824 AA.
AC   Q7VSX9; Q45392;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Type IV secretion system protein PtlC;
DE   AltName: Full=Pertussis toxin liberation protein C;
GN   Name=ptlC; OrderedLocusNames=BP3790;
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-205.
RC   STRAIN=BP165;
RX   PubMed=3584073; DOI=10.1128/jb.169.6.2847-2853.1987;
RA   Arico B., Rappuoli R.;
RT   "Bordetella parapertussis and Bordetella bronchiseptica contain
RT   transcriptionally silent pertussis toxin genes.";
RL   J. Bacteriol. 169:2847-2853(1987).
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, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-462.
RC   STRAIN=Tohama I / BP338;
RX   PubMed=9916087; DOI=10.1128/iai.67.2.754-759.1999;
RA   Cook D.M., Farizo K.M., Burns D.L.;
RT   "Identification and characterization of PtlC, an essential component of the
RT   pertussis toxin secretion system.";
RL   Infect. Immun. 67:754-759(1999).
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 essential 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, ECO:0000269|PubMed:9916087}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9916087}.
CC   -!- INDUCTION: Cotranscribed with ptxABCDE. Activated by the two-component
CC       regulatory system BvgS/BvgA.
CC   -!- SIMILARITY: Belongs to the TrbE/VirB4 family. {ECO:0000305}.
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DR   EMBL; L10720; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX640422; CAE44045.1; -; Genomic_DNA.
DR   EMBL; M14378; AAA83987.1; -; Genomic_DNA.
DR   PIR; B47301; B47301.
DR   RefSeq; NP_882289.1; NC_002929.2.
DR   RefSeq; WP_010931652.1; NZ_CP039022.1.
DR   AlphaFoldDB; Q7VSX9; -.
DR   SMR; Q7VSX9; -.
DR   STRING; 257313.BP3790; -.
DR   TCDB; 3.A.7.3.1; the type iv (conjugal dna-protein transfer or virb) secretory pathway (ivsp) family.
DR   PRIDE; Q7VSX9; -.
DR   KEGG; bpe:BP3790; -.
DR   PATRIC; fig|257313.5.peg.4094; -.
DR   eggNOG; COG3451; Bacteria.
DR   HOGENOM; CLU_008341_3_0_4; -.
DR   OMA; MFMDEFW; -.
DR   Proteomes; UP000002676; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR004346; CagE_TrbE_VirB.
DR   InterPro; IPR018145; CagE_TrbE_VirB_cntrl_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF03135; CagE_TrbE_VirB; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00929; VirB4_CagE; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW   Reference proteome; Transport.
FT   CHAIN           1..824
FT                   /note="Type IV secretion system protein PtlC"
FT                   /id="PRO_0000262574"
FT   BINDING         456..463
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         462
FT                   /note="K->R: Strongly reduces PTX secretion."
FT                   /evidence="ECO:0000269|PubMed:9916087"
SQ   SEQUENCE   824 AA;  92638 MW;  DF95636ECF8964D8 CRC64;
     MNRRGGQTAF AAIARNERAI AAFIPYSSHL TDTTLITHGA DLVRTWRVQG IAFESAEPEL
     VSQRHEQLNG LWRAISCEQV ALWIHCIRRK TQAGLDARYE NPFCRALDAS YNARLNARQA
     MTNEFYLTLV YRPGHAALGK RAHHGQAEVR RQLLAHVRRM DEIGSLIETT LRSHGENHEQ
     AITVLGCETD SAGRRYSRTL TLLEFLLTGH WQPVRVPAGP VDAYLGSSRI LAGAEMMELR
     APTCRRYAQF IDFKEYGTHT EPGMLNALLY EDYEYVITHS FSAVGKRQAL AYLQRQRAQL
     ANVQDAAYSQ IDDLAHAEDA LVNGDFVIGE YHFSMMILGA DPRQLRRDVS SAMTRIQERG
     FLATPVTLAL DAAFYAQLPA NWAYRSRKAM LTSRNFAGLC SFHNFYGGKR DGNPWGPALS
     LLSTPSGQPF YFNFHHSGLD EDCRGQMMLG NTRIIGQSGS GKTVLLNFLL CQLQKFRSAD
     ADGLTTIFFD KDRGAEICIR ALDGQYLRIR DGEPTGFNPL QLPCTDRNVM FLDSLLAMLA
     RAHDSPLTSA QHATLATAVR TVLRMPASLR RMSTLLQNIT QATSEQRELV RRLGRWCRDD
     GAGGTGMLWW VFDNPNDCLD FSRPGNYGID GTAFLDNAET RTPISMYLLH RMNEAMDGRR
     FVYLMDEAWK WIDDPAFAEF AGDQQLTIRK KNGLGVFSTQ MPSSLLGARV AASLVQQCAT
     EIYLPNPRAD RAEYLDGFKC TETEYQLIRS MAEDSHLFLV KQGRQAVVAQ LDLSGMDDEL
     AILSGNARNL RCFEQALALT RERDPNDWIA VFHRLRREAS AGLR
 
 
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