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P01556

- CHTB_VIBCH

UniProt

P01556 - CHTB_VIBCH

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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

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

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
Complete GO annotation...

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-KW
  2. membrane Source: UniProtKB-KW
Complete GO annotation...

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 – 305Combined sources
Beta strandi36 – 438Combined sources
Beta strandi46 – 516Combined sources
Beta strandi58 – 625Combined sources
Beta strandi68 – 714Combined sources
Helixi82 – 9918Combined sources
Beta strandi103 – 1097Combined sources
Beta strandi112 – 12312Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MIKLKFGVFF TVLLSSAYAH GTPQNITDLC AEYHNTQIYT LNDKIFSYTE
60 70 80 90 100
SLAGKREMAI ITFKNGAIFQ VEVPGSQHID SQKKAIERMK DTLRIAYLTE
110 120
AKVEKLCVWN NKTPHAIAAI SMAN
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 119 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