TOX4_BORPE
ID TOX4_BORPE Reviewed; 152 AA.
AC P0A3R5; P04980;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Pertussis toxin subunit 4;
DE Short=PTX S4;
DE AltName: Full=Islet-activating protein S4;
DE Short=IAP S4;
DE Flags: Precursor;
GN Name=ptxD; OrderedLocusNames=BP3785;
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].
RC STRAIN=BP165;
RX PubMed=2873570; DOI=10.1073/pnas.83.13.4631;
RA Nicosia A., Perugini M., Franzini C., Casagli M.C., Borri M.G., Antoni G.,
RA Almoni M., Neri P., Ratti G., Rappuoli R.;
RT "Cloning and sequencing of the pertussis toxin genes: operon structure and
RT gene duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:4631-4635(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3704651; DOI=10.1126/science.3704651;
RA Locht C., Keith J.M.;
RT "Pertussis toxin gene: nucleotide sequence and genetic organization.";
RL Science 232:1258-1264(1986).
RN [3]
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 [4]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RC STRAIN=10536;
RX PubMed=8075982; DOI=10.1016/s0969-2126(00)00007-1;
RA Stein P.E., Boodhoo A., Armstrong G.D., Cockle S.A., Klein M.H., Read R.J.;
RT "The crystal structure of pertussis toxin.";
RL Structure 2:45-57(1994).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=8637000; DOI=10.1006/jmbi.1996.0277;
RA Hazes B., Boodhoo A., Cockle S.A., Read R.J.;
RT "Crystal structure of the pertussis toxin-ATP complex: a molecular
RT sensor.";
RL J. Mol. Biol. 258:661-671(1996).
CC -!- FUNCTION: PTX oligomer B binds to receptors on the eukaryotic cell
CC surface and facilitates the translocation of the toxic subunit across
CC the cell membrane.
CC -!- SUBUNIT: Pertussis toxin contains five different chains, S1-S5. They
CC are organized into 2 functional subunits: A, composed of S1 (which is
CC toxic) and B, containing S2, S3, S5, and two copies of S4 (B binds to
CC the membrane receptors). Dimers of S2-S4 and S3-S4 are held together by
CC S5.
CC -!- SUBCELLULAR LOCATION: Secreted. Host cell membrane {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA22983.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M14378; AAA83982.1; -; Genomic_DNA.
DR EMBL; M13223; AAA22983.1; ALT_INIT; Genomic_DNA.
DR EMBL; BX640422; CAE44040.1; -; Genomic_DNA.
DR PIR; D24394; WEBR41.
DR RefSeq; NP_882284.1; NC_002929.2.
DR RefSeq; WP_010929491.1; NZ_CP039022.1.
DR PDB; 1BCP; X-ray; 2.70 A; D/E/J/K=43-152.
DR PDB; 1PRT; X-ray; 2.90 A; D/E/J/K=43-152.
DR PDB; 1PTO; X-ray; 3.50 A; D/E/J/K=43-152.
DR PDB; 6RO0; X-ray; 2.13 A; D/E/J/K=1-152.
DR PDBsum; 1BCP; -.
DR PDBsum; 1PRT; -.
DR PDBsum; 1PTO; -.
DR PDBsum; 6RO0; -.
DR AlphaFoldDB; P0A3R5; -.
DR SMR; P0A3R5; -.
DR STRING; 257313.BP3785; -.
DR TCDB; 1.C.72.1.1; the pertussis toxin (ptx) family.
DR UniLectin; P0A3R5; -.
DR KEGG; bpe:BP3785; -.
DR PATRIC; fig|257313.5.peg.4089; -.
DR HOGENOM; CLU_1718794_0_0_4; -.
DR OMA; EVNPTRM; -.
DR EvolutionaryTrace; P0A3R5; -.
DR Proteomes; UP000002676; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR008992; Enterotoxin.
DR InterPro; IPR015355; Pertussis_toxin_subS4.
DR Pfam; PF09275; Pertus-S4-tox; 1.
DR SUPFAM; SSF50203; SSF50203; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Host cell membrane; Host membrane; Membrane;
KW Reference proteome; Secreted; Signal; Toxin; Virulence; Whooping cough.
FT SIGNAL 1..42
FT CHAIN 43..152
FT /note="Pertussis toxin subunit 4"
FT /id="PRO_0000019362"
FT DISULFID 73..93
FT DISULFID 145..151
FT STRAND 48..62
FT /evidence="ECO:0007829|PDB:6RO0"
FT STRAND 69..78
FT /evidence="ECO:0007829|PDB:6RO0"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:1BCP"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:6RO0"
FT STRAND 89..100
FT /evidence="ECO:0007829|PDB:6RO0"
FT HELIX 105..116
FT /evidence="ECO:0007829|PDB:6RO0"
FT STRAND 120..131
FT /evidence="ECO:0007829|PDB:6RO0"
FT STRAND 134..144
FT /evidence="ECO:0007829|PDB:6RO0"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:6RO0"
SQ SEQUENCE 152 AA; 16544 MW; 04F135C32DA5DDA1 CRC64;
MLRRFPTRTT APGQGGARRS RVRALAWLLA SGAMTHLSPA LADVPYVLVK TNMVVTSVAM
KPYEVTPTRM LVCGIAAKLG AAASSPDAHV PFCFGKDLKR PGSSPMEVML RAVFMQQRPL
RMFLGPKQLT FEGKPALELI RMVECSGKQD CP