TOX2_BORPE
ID TOX2_BORPE Reviewed; 226 AA.
AC P04978;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2003, sequence version 2.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=Pertussis toxin subunit 2;
DE Short=PTX S2;
DE AltName: Full=Islet-activating protein S2;
DE Short=IAP S2;
DE Flags: Precursor;
GN Name=ptxB; OrderedLocusNames=BP3784;
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; AAA83981.1; -; Genomic_DNA.
DR EMBL; M13223; AAA22982.1; -; Genomic_DNA.
DR EMBL; BX640422; CAE44039.1; -; Genomic_DNA.
DR PIR; B24144; WEBR2P.
DR RefSeq; NP_882283.1; NC_002929.2.
DR RefSeq; WP_010931649.1; NZ_CP039022.1.
DR PDB; 1BCP; X-ray; 2.70 A; B/H=28-226.
DR PDB; 1PRT; X-ray; 2.90 A; B/H=31-226.
DR PDB; 1PTO; X-ray; 3.50 A; B=31-226, H=29-226.
DR PDB; 6RO0; X-ray; 2.13 A; B/H=1-226.
DR PDBsum; 1BCP; -.
DR PDBsum; 1PRT; -.
DR PDBsum; 1PTO; -.
DR PDBsum; 6RO0; -.
DR AlphaFoldDB; P04978; -.
DR SMR; P04978; -.
DR STRING; 257313.BP3784; -.
DR TCDB; 1.C.72.1.1; the pertussis toxin (ptx) family.
DR GeneID; 45390930; -.
DR KEGG; bpe:BP3784; -.
DR PATRIC; fig|257313.5.peg.4088; -.
DR HOGENOM; CLU_106184_0_0_4; -.
DR OMA; SPYGRCA; -.
DR EvolutionaryTrace; P04978; -.
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..27
FT CHAIN 28..226
FT /note="Pertussis toxin subunit 2"
FT /id="PRO_0000019360"
FT DISULFID 50..114
FT DISULFID 147..161
FT DISULFID 219..226
FT CONFLICT 45
FT /note="G -> S (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:6RO0"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:6RO0"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:6RO0"
FT HELIX 59..63
FT /evidence="ECO:0007829|PDB:6RO0"
FT HELIX 66..75
FT /evidence="ECO:0007829|PDB:6RO0"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:6RO0"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:6RO0"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:6RO0"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:6RO0"
FT TURN 103..108
FT /evidence="ECO:0007829|PDB:6RO0"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:6RO0"
FT STRAND 128..141
FT /evidence="ECO:0007829|PDB:6RO0"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:6RO0"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:6RO0"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:6RO0"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:6RO0"
FT HELIX 173..186
FT /evidence="ECO:0007829|PDB:6RO0"
FT STRAND 190..200
FT /evidence="ECO:0007829|PDB:6RO0"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:1BCP"
FT STRAND 210..218
FT /evidence="ECO:0007829|PDB:6RO0"
SQ SEQUENCE 226 AA; 24799 MW; EF9FAF00FB694965 CRC64;
MPIDRKTLCH LLSVLPLALL GSHVARASTP GIVIPPQEQI TQHGGPYGRC ANKTRALTVA
ELRGSGDLQE YLRHVTRGWS IFALYDGTYL GGEYGGVIKD GTPGGAFDLK TTFCIMTTRN
TGQPATDHYY SNVTATRLLS STNSRLCAVF VRSGQPVIGA CTSPYDGKYW SMYSRLRKML
YLIYVAGISV RVHVSKEEQY YDYEDATFET YALTGISICN PGSSLC
