CHTB_VIBCH
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 03-AUG-2022, entry version 152.
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; Proteobacteria; 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}.
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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 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 AlphaFoldDB; P01556; -.
DR SMR; P01556; -.
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 GeneID; 57740119; -.
DR KEGG; vch:VC_1456; -.
DR PATRIC; fig|243277.26.peg.1386; -.
DR HOGENOM; CLU_2002942_0_0_6; -.
DR OMA; HIDSQKK; -.
DR BioCyc; MetaCyc:VC1456-MON; -.
DR BioCyc; VCHO:VC1456-MON; -.
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 InterPro; IPR008992; Enterotoxin.
DR InterPro; IPR001835; Enterotoxin_B.
DR Pfam; PF01376; Enterotoxin_b; 1.
DR PRINTS; PR00772; ENTEROTOXINB.
DR SUPFAM; SSF50203; SSF50203; 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