TOX3_BORPE
ID TOX3_BORPE Reviewed; 227 AA.
AC P04979;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=Pertussis toxin subunit 3;
DE Short=PTX S3;
DE AltName: Full=Islet-activating protein S3;
DE Short=IAP S3;
DE Flags: Precursor;
GN Name=ptxC; OrderedLocusNames=BP3787;
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 -!- SIMILARITY: Belongs to the pertussis toxin S2/S3 subunits family.
CC {ECO:0000305}.
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DR EMBL; M14378; AAA83984.1; -; Genomic_DNA.
DR EMBL; M13223; AAA22985.1; -; Genomic_DNA.
DR EMBL; BX640422; CAE44042.1; -; Genomic_DNA.
DR PIR; C24394; WEBR31.
DR RefSeq; NP_882286.1; NC_002929.2.
DR RefSeq; WP_010931651.1; NZ_CP039022.1.
DR PDB; 1BCP; X-ray; 2.70 A; C/I=29-227.
DR PDB; 1PRT; X-ray; 2.90 A; C/I=32-227.
DR PDB; 1PTO; X-ray; 3.50 A; C/I=32-227.
DR PDB; 6RO0; X-ray; 2.13 A; C/I=1-227.
DR PDBsum; 1BCP; -.
DR PDBsum; 1PRT; -.
DR PDBsum; 1PTO; -.
DR PDBsum; 6RO0; -.
DR AlphaFoldDB; P04979; -.
DR SMR; P04979; -.
DR STRING; 257313.BP3787; -.
DR TCDB; 1.C.72.1.1; the pertussis toxin (ptx) family.
DR GeneID; 45390933; -.
DR KEGG; bpe:BP3787; -.
DR PATRIC; fig|257313.5.peg.4091; -.
DR HOGENOM; CLU_106184_0_0_4; -.
DR OMA; MYDVLRR; -.
DR EvolutionaryTrace; P04979; -.
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 Gene3D; 3.10.40.10; -; 1.
DR InterPro; IPR005138; APT_dom.
DR InterPro; IPR037015; APT_N_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR008992; Enterotoxin.
DR InterPro; IPR003899; ToxinB_BORPE.
DR InterPro; IPR020063; ToxinB_su2/3_C_BORPE.
DR Pfam; PF03440; APT; 1.
DR Pfam; PF02918; Pertussis_S2S3; 1.
DR PRINTS; PR01396; BORPETOXINB.
DR SUPFAM; SSF50203; SSF50203; 1.
DR SUPFAM; SSF56436; SSF56436; 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..28
FT CHAIN 29..227
FT /note="Pertussis toxin subunit 3"
FT /id="PRO_0000019361"
FT DISULFID 51..115
FT DISULFID 148..162
FT DISULFID 220..227
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:6RO0"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:6RO0"
FT HELIX 60..64
FT /evidence="ECO:0007829|PDB:6RO0"
FT HELIX 67..76
FT /evidence="ECO:0007829|PDB:6RO0"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:6RO0"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:6RO0"
FT TURN 93..96
FT /evidence="ECO:0007829|PDB:6RO0"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:6RO0"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:6RO0"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:6RO0"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:6RO0"
FT STRAND 128..142
FT /evidence="ECO:0007829|PDB:6RO0"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:1BCP"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:6RO0"
FT STRAND 156..163
FT /evidence="ECO:0007829|PDB:6RO0"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:6RO0"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:6RO0"
FT HELIX 174..187
FT /evidence="ECO:0007829|PDB:6RO0"
FT STRAND 191..201
FT /evidence="ECO:0007829|PDB:6RO0"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:1BCP"
FT STRAND 211..219
FT /evidence="ECO:0007829|PDB:6RO0"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:6RO0"
SQ SEQUENCE 227 AA; 24988 MW; 8E15848065BBAB7D CRC64;
MLINNKKLLH HILPILVLAL LGMRTAQAVA PGIVIPPKAL FTQQGGAYGR CPNGTRALTV
AELRGNAELQ TYLRQITPGW SIYGLYDGTY LGQAYGGIIK DAPPGAGFIY RETFCITTIY
KTGQPAADHY YSKVTATRLL ASTNSRLCAV FVRDGQSVIG ACASPYEGRY RDMYDALRRL
LYMIYMSGLA VRVHVSKEEQ YYDYEDATFQ TYALTGISLC NPAASIC
