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P01556

- CHTB_VIBCH

UniProt

P01556 - CHTB_VIBCH

Protein

Cholera enterotoxin subunit B

Gene

ctxB

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      Previous versions | rss
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    Functioni

    The B subunit pentameric ring directs the A subunit to its target by binding to the GM1 gangliosides present on the surface of the intestinal epithelial cells. It can bind five GM1 gangliosides. It has no toxic activity by itself.

    GO - Molecular functioni

    1. host cell surface binding Source: TIGR
    2. protein binding Source: IntAct

    GO - Biological processi

    1. killing of cells of other organism Source: TIGR
    2. pathogenesis Source: TIGR
    3. positive regulation of tyrosine phosphorylation of Stat3 protein Source: CACAO
    4. protein ADP-ribosylation Source: TIGR

    Keywords - Molecular functioni

    Enterotoxin, Toxin

    Enzyme and pathway databases

    BioCyciVCHO:VC1456-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cholera enterotoxin subunit B
    Alternative name(s):
    Cholera enterotoxin B chain
    Cholera enterotoxin gamma chain
    Choleragenoid
    Gene namesi
    Name:ctxB
    Synonyms:toxB
    Ordered Locus Names:VC_1456
    OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
    Taxonomic identifieri243277 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
    ProteomesiUP000000584: Chromosome 1

    Subcellular locationi

    GO - Cellular componenti

    1. host cell plasma membrane Source: UniProtKB-SubCell
    2. membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Host cell membrane, Host membrane, Membrane, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi78 – 781H → A: Loss of toxicity.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 21212 PublicationsAdd
    BLAST
    Chaini22 – 124103Cholera enterotoxin subunit BPRO_0000019344Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi30 ↔ 1071 Publication

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    The holotoxin (choleragen) consists of a pentameric ring of B subunits whose central pore is occupied by the A subunit. The A subunit contains two chains, A1 and A2, linked by a disulfide bridge.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ctxAP015555EBI-1038383,EBI-1038392

    Protein-protein interaction databases

    DIPiDIP-6256N.
    IntActiP01556. 3 interactions.
    MINTiMINT-7040506.
    STRINGi243277.VC1456.

    Structurei

    Secondary structure

    1
    124
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi26 – 305
    Beta strandi36 – 438
    Beta strandi46 – 516
    Beta strandi58 – 625
    Beta strandi68 – 714
    Helixi82 – 9918
    Beta strandi103 – 1097
    Beta strandi112 – 12312

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CHPX-ray2.00D/E/F/G/H22-124[»]
    1CHQX-ray2.10D/E/F/G/H22-124[»]
    1CT1X-ray2.30D/E/F/G/H22-124[»]
    1FGBX-ray2.40D/E/F/G/H22-124[»]
    1G8ZX-ray2.00D/E/F/G/H22-124[»]
    1JR0X-ray1.30D/E/F/G/H22-124[»]
    1MD2X-ray1.45D/E/F/G/H22-124[»]
    1RCVX-ray1.60D/E/F/G/H22-124[»]
    1RD9X-ray1.44D/E/F/G/H22-124[»]
    1RDPX-ray1.35D/E/F/G/H22-124[»]
    1RF2X-ray1.35D/E/F/G/H22-124[»]
    1S5BX-ray2.13D/E/F/G/H22-124[»]
    1S5CX-ray2.50D/E/F/G/H22-124[»]
    1S5DX-ray1.75D/E/F/G/H22-124[»]
    1S5EX-ray1.90D/E/F/G/H/J/K/L/M/N22-124[»]
    1S5FX-ray2.60D/E/F/G/H22-124[»]
    1XTCX-ray2.40D/E/F/G/H22-124[»]
    2CHBX-ray2.00D/E/F/G/H22-124[»]
    3CHBX-ray1.25D/E/F/G/H22-124[»]
    3EFXX-ray1.94D/E/F/G/H/I/J/K/L/M23-124[»]
    ProteinModelPortaliP01556.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP01556.

    Family & Domainsi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    KOiK10929.
    OMAiHIDSQKK.
    OrthoDBiEOG6FV8CW.

    Family and domain databases

    InterProiIPR008992. Enterotoxin.
    IPR001835. Enterotoxin_B.
    [Graphical view]
    PfamiPF01376. Enterotoxin_b. 1 hit.
    [Graphical view]
    PRINTSiPR00772. ENTEROTOXINB.
    ProDomiPD012805. Enterotoxin_B. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF50203. SSF50203. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P01556-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIKLKFGVFF TVLLSSAYAH GTPQNITDLC AEYHNTQIYT LNDKIFSYTE    50
    SLAGKREMAI ITFKNGAIFQ VEVPGSQHID SQKKAIERMK DTLRIAYLTE 100
    AKVEKLCVWN NKTPHAIAAI SMAN 124
    Length:124
    Mass (Da):13,957
    Last modified:August 13, 1987 - v1
    Checksum:i9AA393E3EA8E3EBF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti33 – 331Y → S in CAA24996. (PubMed:6646234)Curated
    Sequence conflicti39 – 391Y → H AA sequence (PubMed:903363)Curated
    Sequence conflicti39 – 391Y → H AA sequence (PubMed:903362)Curated
    Sequence conflicti43 – 431D → N AA sequence (PubMed:903363)Curated
    Sequence conflicti43 – 431D → N AA sequence (PubMed:903362)Curated
    Sequence conflicti68 – 681I → T AA sequence (PubMed:903363)Curated
    Sequence conflicti68 – 681I → T AA sequence (PubMed:903362)Curated
    Sequence conflicti70 – 701Q → E AA sequence (PubMed:903362)Curated
    Sequence conflicti75 – 751G → S in CAA24996. (PubMed:6646234)Curated
    Sequence conflicti91 – 911D → N AA sequence (PubMed:903363)Curated
    Sequence conflicti91 – 911D → N AA sequence (PubMed:903362)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K01170 Genomic DNA. Translation: AAA27573.1.
    X00171 Genomic DNA. Translation: CAA24996.1.
    X76390 Genomic DNA. Translation: CAA53973.1.
    X76391 Genomic DNA. Translation: CAA53976.1.
    X58786 Genomic DNA. Translation: CAA41593.1.
    D30053 Genomic DNA. Translation: BAA06291.1.
    AE003852 Genomic DNA. Translation: AAF94613.1.
    PIRiS14624. XVVCB.
    RefSeqiNP_231099.1. NC_002505.1.
    WP_000593522.1. NC_002505.1.

    Genome annotation databases

    EnsemblBacteriaiAAF94613; AAF94613; VC_1456.
    GeneIDi2613962.
    KEGGivch:VC1456.
    PATRICi20081974. VBIVibCho83274_1386.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K01170 Genomic DNA. Translation: AAA27573.1 .
    X00171 Genomic DNA. Translation: CAA24996.1 .
    X76390 Genomic DNA. Translation: CAA53973.1 .
    X76391 Genomic DNA. Translation: CAA53976.1 .
    X58786 Genomic DNA. Translation: CAA41593.1 .
    D30053 Genomic DNA. Translation: BAA06291.1 .
    AE003852 Genomic DNA. Translation: AAF94613.1 .
    PIRi S14624. XVVCB.
    RefSeqi NP_231099.1. NC_002505.1.
    WP_000593522.1. NC_002505.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CHP X-ray 2.00 D/E/F/G/H 22-124 [» ]
    1CHQ X-ray 2.10 D/E/F/G/H 22-124 [» ]
    1CT1 X-ray 2.30 D/E/F/G/H 22-124 [» ]
    1FGB X-ray 2.40 D/E/F/G/H 22-124 [» ]
    1G8Z X-ray 2.00 D/E/F/G/H 22-124 [» ]
    1JR0 X-ray 1.30 D/E/F/G/H 22-124 [» ]
    1MD2 X-ray 1.45 D/E/F/G/H 22-124 [» ]
    1RCV X-ray 1.60 D/E/F/G/H 22-124 [» ]
    1RD9 X-ray 1.44 D/E/F/G/H 22-124 [» ]
    1RDP X-ray 1.35 D/E/F/G/H 22-124 [» ]
    1RF2 X-ray 1.35 D/E/F/G/H 22-124 [» ]
    1S5B X-ray 2.13 D/E/F/G/H 22-124 [» ]
    1S5C X-ray 2.50 D/E/F/G/H 22-124 [» ]
    1S5D X-ray 1.75 D/E/F/G/H 22-124 [» ]
    1S5E X-ray 1.90 D/E/F/G/H/J/K/L/M/N 22-124 [» ]
    1S5F X-ray 2.60 D/E/F/G/H 22-124 [» ]
    1XTC X-ray 2.40 D/E/F/G/H 22-124 [» ]
    2CHB X-ray 2.00 D/E/F/G/H 22-124 [» ]
    3CHB X-ray 1.25 D/E/F/G/H 22-124 [» ]
    3EFX X-ray 1.94 D/E/F/G/H/I/J/K/L/M 23-124 [» ]
    ProteinModelPortali P01556.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-6256N.
    IntActi P01556. 3 interactions.
    MINTi MINT-7040506.
    STRINGi 243277.VC1456.

    Protocols and materials databases

    DNASUi 2613962.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAF94613 ; AAF94613 ; VC_1456 .
    GeneIDi 2613962.
    KEGGi vch:VC1456.
    PATRICi 20081974. VBIVibCho83274_1386.

    Phylogenomic databases

    KOi K10929.
    OMAi HIDSQKK.
    OrthoDBi EOG6FV8CW.

    Enzyme and pathway databases

    BioCyci VCHO:VC1456-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P01556.
    PROi P01556.

    Family and domain databases

    InterProi IPR008992. Enterotoxin.
    IPR001835. Enterotoxin_B.
    [Graphical view ]
    Pfami PF01376. Enterotoxin_b. 1 hit.
    [Graphical view ]
    PRINTSi PR00772. ENTEROTOXINB.
    ProDomi PD012805. Enterotoxin_B. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF50203. SSF50203. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence analysis of the A2 and B subunits of Vibrio cholerae enterotoxin."
      Lockman H., Kaper J.B.
      J. Biol. Chem. 258:13722-13726(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Cholera toxin genes: nucleotide sequence, deletion analysis and vaccine development."
      Mekalanos J.J., Swartz D.J., Pearson G.D.N., Harford N., Groyne F., de Wilde M.
      Nature 306:551-557(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 39050 / El Tor Inaba 2125 / Serotype O1.
    3. "Structure and arrangement of the cholera toxin genes in Vibrio cholerae O139."
      Lebens M., Holmgren J.
      FEMS Microbiol. Lett. 117:197-202(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 4260B / Serotype O139.
    4. Dams E., de Wolf M., Dierick W.
      Submitted (MAY-1991) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 39050 / El Tor Inaba 2125 / Serotype O1.
    5. Yamamoto K., Do V.G.R.F., Xu M., Iida T., Miwatani T., Albert M.J., Honda T.
      Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 1854 / O139-Bengal.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 39315 / El Tor Inaba N16961.
    7. "Covalent structure of the beta chain of cholera enterotoxin."
      Kurosky A., Markel D.E., Peterson J.W.
      J. Biol. Chem. 252:7257-7264(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 22-124.
    8. "Determination of the primary structure of cholera toxin B subunit."
      Lai C.-Y.
      J. Biol. Chem. 252:7249-7256(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 22-124.
    9. "The arrangement of subunits in cholera toxin."
      Gill D.M.
      Biochemistry 15:1242-1248(1976) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    10. "Gangliosides that associate with lipid rafts mediate transport of cholera and related toxins from the plasma membrane to endoplasmic reticulm."
      Fujinaga Y., Wolf A.A., Rodighiero C., Wheeler H., Tsai B., Allen L., Jobling M.G., Rapoport T., Holmes R.K., Lencer W.I.
      Mol. Biol. Cell 14:4783-4793(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: TRANSPORT OF CHOLERA TOXIN WITHIN THE INTESTINAL CELL.
    11. "Crystal structure of cholera toxin B-pentamer bound to receptor GM1 pentasaccharide."
      Merritt E.A., Sarfaty S., van den Akker F., L'Hoir C., Martial J.A., Hol W.G.J.
      Protein Sci. 3:166-175(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
    12. "The 2.4 A crystal structure of cholera toxin B subunit pentamer: choleragenoid."
      Zhang R.-G., Westbrook M.L., Westbrook E.M., Scott D.L., Otwinowski Z., Maulik P.R., Reed R.A., Shipley G.G.
      J. Mol. Biol. 251:550-562(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
    13. "Structural studies of receptor binding by cholera toxin mutants."
      Merritt E.A., Sarfaty S., Jobling M.G., Chang T., Holmes R.K., Hirst T.R., Hol W.G.J.
      Protein Sci. 6:1516-1528(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS).
      Strain: Ogawa 41 / Classical biotype.
    14. "A mutant cholera toxin B subunit that binds GM1-ganglioside but lacks immunomodulatory or toxic activity."
      Aman A.T., Fraser S., Merritt E.A., Rodigherio C., Kenny M., Ahn M., Hol W.G.J., Williams N.A., Lencer W.I., Hirst T.R.
      Proc. Natl. Acad. Sci. U.S.A. 98:8536-8541(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT ALA-57.
    15. "Anchor-based design of improved cholera toxin and E. coli heat-labile enterotoxin receptor binding antagonists that display multiple binding modes."
      Pickens J.C., Merritt E.A., Ahn M., Verlinde C.L.M.J., Hol W.G.J., Fan E.
      Chem. Biol. 9:215-224(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
    16. "Solution and crystallographic studies of branched multivalent ligands that inhibit the receptor-binding of cholera toxin."
      Zhang Z., Merritt E.A., Ahn M., Roach C., Hou Z., Verlinde C.L.M.J., Hol W.G.J., Fan E.
      J. Am. Chem. Soc. 124:12991-12998(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).

    Entry informationi

    Entry nameiCHTB_VIBCH
    AccessioniPrimary (citable) accession number: P01556
    Secondary accession number(s): Q9JQ02
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 117 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

    Dasty 3