ID   CHTB_VIBCH              Reviewed;         124 AA.
AC   P01556; Q9JQ02;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   27-MAR-2024, entry version 158.
DE   RecName: Full=Cholera enterotoxin subunit B;
DE   AltName: Full=Cholera enterotoxin B chain;
DE   AltName: Full=Cholera enterotoxin gamma chain;
DE   AltName: Full=Choleragenoid;
DE   Flags: Precursor;
GN   Name=ctxB; Synonyms=toxB; OrderedLocusNames=VC_1456;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6315707; DOI=10.1016/s0021-9258(17)43977-9;
RA   Lockman H., Kaper J.B.;
RT   "Nucleotide sequence analysis of the A2 and B subunits of Vibrio cholerae
RT   enterotoxin.";
RL   J. Biol. Chem. 258:13722-13726(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 39050 / El Tor Inaba 2125 / Serotype O1;
RX   PubMed=6646234; DOI=10.1038/306551a0;
RA   Mekalanos J.J., Swartz D.J., Pearson G.D.N., Harford N., Groyne F.,
RA   de Wilde M.;
RT   "Cholera toxin genes: nucleotide sequence, deletion analysis and vaccine
RT   development.";
RL   Nature 306:551-557(1983).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=4260B / Serotype O139;
RX   PubMed=8181723; DOI=10.1111/j.1574-6968.1994.tb06764.x;
RA   Lebens M., Holmgren J.;
RT   "Structure and arrangement of the cholera toxin genes in Vibrio cholerae
RT   O139.";
RL   FEMS Microbiol. Lett. 117:197-202(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 39050 / El Tor Inaba 2125 / Serotype O1;
RA   Dams E., de Wolf M., Dierick W.;
RL   Submitted (MAY-1991) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=1854 / O139-Bengal;
RA   Yamamoto K., Do V.G.R.F., Xu M., Iida T., Miwatani T., Albert M.J.,
RA   Honda T.;
RL   Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
RN   [7]
RP   PROTEIN SEQUENCE OF 22-124.
RX   PubMed=903363; DOI=10.1016/s0021-9258(19)66963-2;
RA   Kurosky A., Markel D.E., Peterson J.W.;
RT   "Covalent structure of the beta chain of cholera enterotoxin.";
RL   J. Biol. Chem. 252:7257-7264(1977).
RN   [8]
RP   PROTEIN SEQUENCE OF 22-124.
RX   PubMed=903362; DOI=10.1016/s0021-9258(19)66962-0;
RA   Lai C.-Y.;
RT   "Determination of the primary structure of cholera toxin B subunit.";
RL   J. Biol. Chem. 252:7249-7256(1977).
RN   [9]
RP   SUBUNIT.
RX   PubMed=3214; DOI=10.1021/bi00651a011;
RA   Gill D.M.;
RT   "The arrangement of subunits in cholera toxin.";
RL   Biochemistry 15:1242-1248(1976).
RN   [10]
RP   TRANSPORT OF CHOLERA TOXIN WITHIN THE INTESTINAL CELL.
RX   PubMed=13679513; DOI=10.1091/mbc.e03-06-0354;
RA   Fujinaga Y., Wolf A.A., Rodighiero C., Wheeler H., Tsai B., Allen L.,
RA   Jobling M.G., Rapoport T., Holmes R.K., Lencer W.I.;
RT   "Gangliosides that associate with lipid rafts mediate transport of cholera
RT   and related toxins from the plasma membrane to endoplasmic reticulum.";
RL   Mol. Biol. Cell 14:4783-4793(2003).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX   PubMed=8003954; DOI=10.1002/pro.5560030202;
RA   Merritt E.A., Sarfaty S., van den Akker F., L'Hoir C., Martial J.A.,
RA   Hol W.G.J.;
RT   "Crystal structure of cholera toxin B-pentamer bound to receptor GM1
RT   pentasaccharide.";
RL   Protein Sci. 3:166-175(1994).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX   PubMed=7658472; DOI=10.1006/jmbi.1995.0455;
RA   Zhang R.-G., Westbrook M.L., Westbrook E.M., Scott D.L., Otwinowski Z.,
RA   Maulik P.R., Reed R.A., Shipley G.G.;
RT   "The 2.4 A crystal structure of cholera toxin B subunit pentamer:
RT   choleragenoid.";
RL   J. Mol. Biol. 251:550-562(1995).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS).
RC   STRAIN=Ogawa 41 / Classical biotype;
RX   PubMed=9232653; DOI=10.1002/pro.5560060716;
RA   Merritt E.A., Sarfaty S., Jobling M.G., Chang T., Holmes R.K., Hirst T.R.,
RA   Hol W.G.J.;
RT   "Structural studies of receptor binding by cholera toxin mutants.";
RL   Protein Sci. 6:1516-1528(1997).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT ALA-57.
RX   PubMed=11447291; DOI=10.1073/pnas.161273098;
RA   Aman A.T., Fraser S., Merritt E.A., Rodigherio C., Kenny M., Ahn M.,
RA   Hol W.G.J., Williams N.A., Lencer W.I., Hirst T.R.;
RT   "A mutant cholera toxin B subunit that binds GM1-ganglioside but lacks
RT   immunomodulatory or toxic activity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:8536-8541(2001).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
RX   PubMed=11880036; DOI=10.1016/s1074-5521(02)00097-2;
RA   Pickens J.C., Merritt E.A., Ahn M., Verlinde C.L.M.J., Hol W.G.J., Fan E.;
RT   "Anchor-based design of improved cholera toxin and E. coli heat-labile
RT   enterotoxin receptor binding antagonists that display multiple binding
RT   modes.";
RL   Chem. Biol. 9:215-224(2002).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
RX   PubMed=12405825; DOI=10.1021/ja027584k;
RA   Zhang Z., Merritt E.A., Ahn M., Roach C., Hou Z., Verlinde C.L.M.J.,
RA   Hol W.G.J., Fan E.;
RT   "Solution and crystallographic studies of branched multivalent ligands that
RT   inhibit the receptor-binding of cholera toxin.";
RL   J. Am. Chem. Soc. 124:12991-12998(2002).
CC   -!- FUNCTION: The B subunit pentameric ring directs the A subunit to its
CC       target by binding to the GM1 gangliosides present on the surface of the
CC       intestinal epithelial cells. It can bind five GM1 gangliosides. It has
CC       no toxic activity by itself.
CC   -!- SUBUNIT: The holotoxin (choleragen) consists of a pentameric ring of B
CC       subunits whose central pore is occupied by the A subunit. The A subunit
CC       contains two chains, A1 and A2, linked by a disulfide bridge.
CC       {ECO:0000269|PubMed:11880036, ECO:0000269|PubMed:3214}.
CC   -!- INTERACTION:
CC       P01556; P01555: ctxA; NbExp=5; IntAct=EBI-1038383, EBI-1038392;
CC   -!- SUBCELLULAR LOCATION: Secreted. Host cell membrane {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; K01170; AAA27573.1; -; Genomic_DNA.
DR   EMBL; X00171; CAA24996.1; -; Genomic_DNA.
DR   EMBL; X76390; CAA53973.1; -; Genomic_DNA.
DR   EMBL; X76391; CAA53976.1; -; Genomic_DNA.
DR   EMBL; X58786; CAA41593.1; -; Genomic_DNA.
DR   EMBL; D30053; BAA06291.1; -; Genomic_DNA.
DR   EMBL; AE003852; AAF94613.1; -; Genomic_DNA.
DR   PIR; S14624; XVVCB.
DR   RefSeq; NP_231099.1; NC_002505.1.
DR   RefSeq; WP_000593522.1; NZ_LT906614.1.
DR   PDB; 1CHP; X-ray; 2.00 A; D/E/F/G/H=22-124.
DR   PDB; 1CHQ; X-ray; 2.10 A; D/E/F/G/H=22-124.
DR   PDB; 1CT1; X-ray; 2.30 A; D/E/F/G/H=22-124.
DR   PDB; 1FGB; X-ray; 2.40 A; D/E/F/G/H=22-124.
DR   PDB; 1G8Z; X-ray; 2.00 A; D/E/F/G/H=22-124.
DR   PDB; 1JR0; X-ray; 1.30 A; D/E/F/G/H=22-124.
DR   PDB; 1MD2; X-ray; 1.45 A; D/E/F/G/H=22-124.
DR   PDB; 1RCV; X-ray; 1.60 A; D/E/F/G/H=22-124.
DR   PDB; 1RD9; X-ray; 1.44 A; D/E/F/G/H=22-124.
DR   PDB; 1RDP; X-ray; 1.35 A; D/E/F/G/H=22-124.
DR   PDB; 1RF2; X-ray; 1.35 A; D/E/F/G/H=22-124.
DR   PDB; 1S5B; X-ray; 2.13 A; D/E/F/G/H=22-124.
DR   PDB; 1S5C; X-ray; 2.50 A; D/E/F/G/H=22-124.
DR   PDB; 1S5D; X-ray; 1.75 A; D/E/F/G/H=22-124.
DR   PDB; 1S5E; X-ray; 1.90 A; D/E/F/G/H/J/K/L/M/N=22-124.
DR   PDB; 1S5F; X-ray; 2.60 A; D/E/F/G/H=22-124.
DR   PDB; 1XTC; X-ray; 2.40 A; D/E/F/G/H=22-124.
DR   PDB; 2CHB; X-ray; 2.00 A; D/E/F/G/H=22-124.
DR   PDB; 3CHB; X-ray; 1.25 A; D/E/F/G/H=22-124.
DR   PDB; 3EFX; X-ray; 1.94 A; D/E/F/G/H/I/J/K/L/M=23-124.
DR   PDB; 5ELC; X-ray; 1.50 A; A/B/C/D/E/F/G/H/I/J=22-124.
DR   PDB; 5ELE; X-ray; 1.60 A; A/B/C/D/E/F/G/H/I/J=22-124.
DR   PDB; 5ELF; X-ray; 1.55 A; A/B/C/D/E/F/G/H/I/J=22-124.
DR   PDB; 5LZG; X-ray; 1.13 A; A/B/C/D/E=22-124.
DR   PDB; 5LZJ; X-ray; 1.20 A; A/B/C/D/E=22-124.
DR   PDB; 6HJD; X-ray; 1.54 A; A/B/C/D/E/F/G/H/I/J=22-124.
DR   PDB; 6HMW; X-ray; 1.95 A; A/B/C/D/E/F/G/H/I/J=22-124.
DR   PDB; 6HMY; X-ray; 1.60 A; A/B/C/D/E/F/G/H/I/J=22-124.
DR   PDB; 6HSV; X-ray; 2.45 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=22-124.
DR   PDB; 7LVB; X-ray; 2.25 A; A/B/C/D/E/F/G/H/I/J=22-124.
DR   PDBsum; 1CHP; -.
DR   PDBsum; 1CHQ; -.
DR   PDBsum; 1CT1; -.
DR   PDBsum; 1FGB; -.
DR   PDBsum; 1G8Z; -.
DR   PDBsum; 1JR0; -.
DR   PDBsum; 1MD2; -.
DR   PDBsum; 1RCV; -.
DR   PDBsum; 1RD9; -.
DR   PDBsum; 1RDP; -.
DR   PDBsum; 1RF2; -.
DR   PDBsum; 1S5B; -.
DR   PDBsum; 1S5C; -.
DR   PDBsum; 1S5D; -.
DR   PDBsum; 1S5E; -.
DR   PDBsum; 1S5F; -.
DR   PDBsum; 1XTC; -.
DR   PDBsum; 2CHB; -.
DR   PDBsum; 3CHB; -.
DR   PDBsum; 3EFX; -.
DR   PDBsum; 5ELC; -.
DR   PDBsum; 5ELE; -.
DR   PDBsum; 5ELF; -.
DR   PDBsum; 5LZG; -.
DR   PDBsum; 5LZJ; -.
DR   PDBsum; 6HJD; -.
DR   PDBsum; 6HMW; -.
DR   PDBsum; 6HMY; -.
DR   PDBsum; 6HSV; -.
DR   PDBsum; 7LVB; -.
DR   AlphaFoldDB; P01556; -.
DR   SMR; P01556; -.
DR   ComplexPortal; CPX-2345; Cholera toxin.
DR   DIP; DIP-6256N; -.
DR   IntAct; P01556; 5.
DR   MINT; P01556; -.
DR   STRING; 243277.VC_1456; -.
DR   DrugBank; DB02572; 1,3-bis-([3-[3-[3-(4-{3-[3-nitro-5-(galactopyranosyloxy)-benzoylamino]-propyl}-piperazin-1-yl)-propylamino-3,4-dioxo-cyclobutenyl]-amino-propoxy-ethoxy-ethoxy]-propyl-]amino-carbonyloxy)-2-amino-propane.
DR   DrugBank; DB02903; 1,3-bis-([[3-(4-{3-[3-nitro-5-(galactopyranosyloxy)-benzoylamino]-propyl}-piperazin-1-yl)-propylamino-3,4-dioxo-cyclobutenyl]-amino-ethyl]-amino-carbonyloxy)-2-amino-propane.
DR   DrugBank; DB02802; 3-(alpha-D-Galactopyranosyloxy)-5-nitrobenzamide.
DR   DrugBank; DB04210; 3-(alpha-D-galactopyranosyloxy)-N-(3-{4-[3-({2-[(3-{4-[3-({[3-(hexopyranosyloxy)-5-nitrophenyl]carbonyl}amino)propyl]piperazin-1-yl}propyl)amino]-3,4-dioxocyclobut-1-en-1-yl}amino)propyl]piperazin-1-yl}propyl)-5-nitrobenzamide.
DR   DrugBank; DB03077; 3-Amino-4-{3-[2-(2-Propoxy-Ethoxy)-Ethoxy]-Propylamino}-Cyclobut-3-Ene-1,2-Dione.
DR   DrugBank; DB02379; Beta-D-Glucose.
DR   DrugBank; DB02474; BMSC-0013.
DR   DrugBank; DB02574; BV2.
DR   DrugBank; DB02213; Metanitrophenyl-Alpha-D-Galactoside.
DR   DrugBank; DB03524; N-[3-[4-(3-aminopropyl)piperazin-1-yl]propyl]-3-[(2-thiophen-2-ylacetyl)amino]-5-[(2R,3R,4S,5R,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxybenzamide.
DR   DrugBank; DB03721; N-acetyl-alpha-neuraminic acid.
DR   DrugBank; DB04073; N-{3-[4-(3-amino-propyl)-piperazin-1-yl]-propyl}-3-nitro-5-(galactopyranosyl)-beta-benzamide.
DR   DrugBank; DB03235; N-{3-[4-(3-aminopropyl)piperazin-1-yl]propyl}-3-(alpha-D-galactopyranosyloxy)-5-nitrobenzamide.
DR   UniLectin; P01556; -.
DR   ABCD; P01556; 1 sequenced antibody.
DR   DNASU; 2613962; -.
DR   EnsemblBacteria; AAF94613; AAF94613; VC_1456.
DR   KEGG; vch:VC_1456; -.
DR   PATRIC; fig|243277.26.peg.1386; -.
DR   HOGENOM; CLU_2002942_0_0_6; -.
DR   BioCyc; MetaCyc:FY484_RS07325-MONOMER; -.
DR   EvolutionaryTrace; P01556; -.
DR   PHI-base; PHI:699; -.
DR   PRO; PR:P01556; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:1902494; C:catalytic complex; IMP:CAFA.
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:0042597; C:periplasmic space; IMP:CAFA.
DR   GO; GO:0005534; F:galactose binding; IMP:CAFA.
DR   GO; GO:0046812; F:host cell surface binding; IDA:TIGR.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IDA:CACAO.
DR   Gene3D; 2.40.50.110; -; 1.
DR   InterPro; IPR008992; Enterotoxin.
DR   InterPro; IPR001835; Enterotoxin_B.
DR   Pfam; PF01376; Enterotoxin_b; 1.
DR   PRINTS; PR00772; ENTEROTOXINB.
DR   SUPFAM; SSF50203; Bacterial enterotoxins; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Enterotoxin;
KW   Host cell membrane; Host membrane; Membrane; Reference proteome; Secreted;
KW   Signal; Toxin; Virulence.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:903362,
FT                   ECO:0000269|PubMed:903363"
FT   CHAIN           22..124
FT                   /note="Cholera enterotoxin subunit B"
FT                   /id="PRO_0000019344"
FT   DISULFID        30..107
FT                   /evidence="ECO:0000269|PubMed:903363"
FT   MUTAGEN         78
FT                   /note="H->A: Loss of toxicity."
FT   CONFLICT        33
FT                   /note="Y -> S (in Ref. 2; CAA24996)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        39
FT                   /note="Y -> H (in Ref. 7; AA sequence and 8; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        43
FT                   /note="D -> N (in Ref. 7; AA sequence and 8; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        68
FT                   /note="I -> T (in Ref. 7; AA sequence and 8; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        70
FT                   /note="Q -> E (in Ref. 8; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        75
FT                   /note="G -> S (in Ref. 2; CAA24996)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        91
FT                   /note="D -> N (in Ref. 7; AA sequence and 8; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           26..30
FT                   /evidence="ECO:0007829|PDB:5LZG"
FT   STRAND          36..43
FT                   /evidence="ECO:0007829|PDB:5LZG"
FT   STRAND          46..51
FT                   /evidence="ECO:0007829|PDB:5LZG"
FT   STRAND          58..62
FT                   /evidence="ECO:0007829|PDB:5LZG"
FT   STRAND          68..71
FT                   /evidence="ECO:0007829|PDB:5LZG"
FT   TURN            75..77
FT                   /evidence="ECO:0007829|PDB:5LZJ"
FT   HELIX           82..99
FT                   /evidence="ECO:0007829|PDB:5LZG"
FT   STRAND          103..123
FT                   /evidence="ECO:0007829|PDB:5LZG"
SQ   SEQUENCE   124 AA;  13957 MW;  9AA393E3EA8E3EBF CRC64;
     MIKLKFGVFF TVLLSSAYAH GTPQNITDLC AEYHNTQIYT LNDKIFSYTE SLAGKREMAI
     ITFKNGAIFQ VEVPGSQHID SQKKAIERMK DTLRIAYLTE AKVEKLCVWN NKTPHAIAAI
     SMAN
//