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P01556 (CHTB_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cholera enterotoxin subunit B
Alternative name(s):
Cholera enterotoxin B chain
Cholera enterotoxin gamma chain
Choleragenoid
Gene names
Name:ctxB
Synonyms:toxB
Ordered Locus Names:VC_1456
OrganismVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP]
Taxonomic identifier243277 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length124 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.9

Subcellular location

Secreted. Host cell membrane Potential.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ctxAP015555EBI-1038383,EBI-1038392

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Ref.7 Ref.8
Chain22 – 124103Cholera enterotoxin subunit B
PRO_0000019344

Amino acid modifications

Disulfide bond30 ↔ 107 Ref.7

Experimental info

Mutagenesis781H → A: Loss of toxicity.
Sequence conflict331Y → S in CAA24996. Ref.2
Sequence conflict391Y → H AA sequence Ref.7
Sequence conflict391Y → H AA sequence Ref.8
Sequence conflict431D → N AA sequence Ref.7
Sequence conflict431D → N AA sequence Ref.8
Sequence conflict681I → T AA sequence Ref.7
Sequence conflict681I → T AA sequence Ref.8
Sequence conflict701Q → E AA sequence Ref.8
Sequence conflict751G → S in CAA24996. Ref.2
Sequence conflict911D → N AA sequence Ref.7
Sequence conflict911D → N AA sequence Ref.8

Secondary structure

................. 124
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P01556 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 9AA393E3EA8E3EBF

FASTA12413,957
        10         20         30         40         50         60 
MIKLKFGVFF TVLLSSAYAH GTPQNITDLC AEYHNTQIYT LNDKIFSYTE SLAGKREMAI 

        70         80         90        100        110        120 
ITFKNGAIFQ VEVPGSQHID SQKKAIERMK DTLRIAYLTE AKVEKLCVWN NKTPHAIAAI 


SMAN 

« Hide

References

« Hide 'large scale' references
[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]"DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae."
Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D., Vamathevan J.J., Bass S. expand/collapse author list , Qin H., Dragoi I., Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.
Nature 406:477-483(2000) [PubMed] [Europe PMC] [Abstract]
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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRXVVCB. S14624.
RefSeqNP_231099.1. NC_002505.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP01556.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6256N.
IntActP01556. 3 interactions.
MINTMINT-7040506.
STRING243277.VC1456.

Protocols and materials databases

DNASU2613962.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF94613; AAF94613; VC_1456.
GeneID2613962.
KEGGvch:VC1456.
PATRIC20081974. VBIVibCho83274_1386.

Phylogenomic databases

KOK10929.
OMAGKREMAI.
OrthoDBEOG6FV8CW.
ProtClustDBCLSK2484299.

Enzyme and pathway databases

BioCycVCHO:VC1456-MONOMER.

Family and domain databases

InterProIPR001835. Enterotoxin_B.
IPR008992. Enterotoxin_bac.
[Graphical view]
PfamPF01376. Enterotoxin_b. 1 hit.
[Graphical view]
PRINTSPR00772. ENTEROTOXINB.
ProDomPD012805. Enterotoxin_B. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF50203. SSF50203. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP01556.
PROP01556.

Entry information

Entry nameCHTB_VIBCH
AccessionPrimary (citable) accession number: P01556
Secondary accession number(s): Q9JQ02
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 13, 1987
Last modified: December 11, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references