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TOX4_BORPA
ID   TOX4_BORPA              Reviewed;         152 AA.
AC   P0A3R6; P04980;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=BPP4306;
OS   Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12822 / ATCC BAA-587 / NCTC 13253;
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).
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. {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted. Host cell membrane {ECO:0000305}.
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DR   EMBL; BX640436; CAE39584.1; -; Genomic_DNA.
DR   RefSeq; WP_010929491.1; NC_002928.3.
DR   AlphaFoldDB; P0A3R6; -.
DR   SMR; P0A3R6; -.
DR   EnsemblBacteria; CAE39584; CAE39584; BPP4306.
DR   KEGG; bpa:BPP4306; -.
DR   HOGENOM; CLU_1718794_0_0_4; -.
DR   OMA; EVNPTRM; -.
DR   Proteomes; UP000001421; 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   3: Inferred from homology;
KW   Disulfide bond; Host cell membrane; Host membrane; Membrane; Secreted;
KW   Signal; Toxin; Virulence; Whooping cough.
FT   SIGNAL          1..42
FT                   /evidence="ECO:0000250"
FT   CHAIN           43..152
FT                   /note="Pertussis toxin subunit 4"
FT                   /id="PRO_0000019363"
FT   DISULFID        73..93
FT                   /evidence="ECO:0000250"
FT   DISULFID        145..151
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   152 AA;  16544 MW;  04F135C32DA5DDA1 CRC64;
     MLRRFPTRTT APGQGGARRS RVRALAWLLA SGAMTHLSPA LADVPYVLVK TNMVVTSVAM
     KPYEVTPTRM LVCGIAAKLG AAASSPDAHV PFCFGKDLKR PGSSPMEVML RAVFMQQRPL
     RMFLGPKQLT FEGKPALELI RMVECSGKQD CP
 
 
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