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Cholera enterotoxin subunit A (Cholera enterotoxin, A chain) [Cleaved into: Cholera enterotoxin subunit A1 (EC 2.4.2.-) (Cholera enterotoxin A1 chain) (Cholera enterotoxin alpha chain) (NAD( )--diphthamide ADP-ribosyltransferase); Cholera enterotoxin subunit A2 (Cholera enterotoxin A2 chain) (Cholera enterotoxin gamma chain)]

 CHTA_VIBCH              Reviewed;         258 AA.
P01555; Q56634; Q9JPV1;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-OCT-1986, sequence version 1.
18-JUL-2018, entry version 140.
RecName: Full=Cholera enterotoxin subunit A;
AltName: Full=Cholera enterotoxin, A chain;
Contains:
RecName: Full=Cholera enterotoxin subunit A1;
EC=2.4.2.-;
AltName: Full=Cholera enterotoxin A1 chain;
AltName: Full=Cholera enterotoxin alpha chain;
AltName: Full=NAD(+)--diphthamide ADP-ribosyltransferase;
Contains:
RecName: Full=Cholera enterotoxin subunit A2;
AltName: Full=Cholera enterotoxin A2 chain;
AltName: Full=Cholera enterotoxin gamma chain;
Flags: Precursor;
Name=ctxA; Synonyms=toxA; OrderedLocusNames=VC_1457;
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
Vibrionaceae; Vibrio.
NCBI_TaxID=243277;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 39050 / El Tor Inaba 2125 / Serotype O1;
PubMed=6646234; DOI=10.1038/306551a0;
Mekalanos J.J., Swartz D.J., Pearson G.D.N., Harford N., Groyne F.,
de Wilde M.;
"Cholera toxin genes: nucleotide sequence, deletion analysis and
vaccine development.";
Nature 306:551-557(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 25870 / Classical Inaba 569B / Serotype O1;
PubMed=1883840; DOI=10.1016/0167-4781(91)90050-V;
Dams E., de Wolf M., Dierick W.;
"Nucleotide sequence analysis of the CT operon of the Vibrio cholerae
classical strain 569B.";
Biochim. Biophys. Acta 1090:139-141(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=1854 / O139-Bengal;
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.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 39050 / El Tor Inaba 2125 / Serotype O1;
Dams E., de Wolf M., Dierick W.;
Submitted (MAY-1991) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=KNIH002;
Shin H.J., Park Y.C., Kim Y.C.;
"Cloning and nucleotide sequence analysis of the virulence gene
cassette from Vibrio cholerae KNIH002 isolated in Korea.";
Misainmurhag Hoiji 35:205-210(1999).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 39315 / El Tor Inaba N16961;
PubMed=10952301; DOI=10.1038/35020000;
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., 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.;
"DNA sequence of both chromosomes of the cholera pathogen Vibrio
cholerae.";
Nature 406:477-483(2000).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-212.
STRAIN=ATCC 25870 / Classical Inaba 569B / Serotype O1;
PubMed=6090390;
Lockman H.A., Galen J.E., Kaper J.B.;
"Vibrio cholerae enterotoxin genes: nucleotide sequence analysis of
DNA encoding ADP-ribosyltransferase.";
J. Bacteriol. 159:1086-1089(1984).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 213-258.
PubMed=6315707;
Lockman H., Kaper J.B.;
"Nucleotide sequence analysis of the A2 and B subunits of Vibrio
cholerae enterotoxin.";
J. Biol. Chem. 258:13722-13726(1983).
[9]
PROTEIN SEQUENCE OF 19-27.
PubMed=7238869; DOI=10.1016/0014-5793(81)80238-4;
Duffy L.K., Peterson J.W., Kurosky A.;
"Isolation and characterization of a precursor form of the 'A' subunit
of cholera toxin.";
FEBS Lett. 126:187-190(1981).
[10]
PROTEIN SEQUENCE OF 19-38 AND 213-232.
PubMed=955672; DOI=10.1016/0019-2791(76)90173-7;
Klapper D.G., Finkelstein R.A., Capra J.D.;
"Subunit structure and N-terminal amino acid sequence of the three
chains of cholera enterotoxin.";
Immunochemistry 13:605-611(1976).
[11]
PROTEIN SEQUENCE OF 27-72 AND 111-139.
PubMed=437113; DOI=10.1016/0014-5793(79)81136-9;
Lai C.-Y., Cancedda F., Chang D.;
"Primary structure of cholera toxin subunit A1: isolation, partial
sequences and alignment of the BrCN fragments.";
FEBS Lett. 100:85-89(1979).
[12]
PROTEIN SEQUENCE OF 213-258.
PubMed=7028752;
Duffy L.K., Peterson J.W., Kurosky A.;
"Covalent structure of the gamma chain of the A subunit of cholera
toxin.";
J. Biol. Chem. 256:12252-12256(1981).
[13]
INTERACTION BETWEEN CHOLERA TOXIN AND ADENYLATE CYCLASE.
PubMed=4323551; DOI=10.1038/229266a0;
Sharp G.W., Hynie S.;
"Stimulation of intestinal adenyl cyclase by cholera toxin.";
Nature 229:266-269(1971).
[14]
SUBUNIT.
PubMed=3214; DOI=10.1021/bi00651a011;
Gill D.M.;
"The arrangement of subunits in cholera toxin.";
Biochemistry 15:1242-1248(1976).
[15]
TRANSPORT OF CHOLERA TOXIN WITHIN THE INTESTINAL CELL.
PubMed=13679513; DOI=10.1091/mbc.E03-06-0354;
Fujinaga Y., Wolf A.A., Rodighiero C., Wheeler H., Tsai B., Allen L.,
Jobling M.G., Rapoport T., Holmes R.K., Lencer W.I.;
"Gangliosides that associate with lipid rafts mediate transport of
cholera and related toxins from the plasma membrane to endoplasmic
reticulm.";
Mol. Biol. Cell 14:4783-4793(2003).
[16]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
PubMed=7658473; DOI=10.1006/jmbi.1995.0456;
Zhang R.-G., Scott D.L., Westbrook M.L., Nance S., Spangler B.D.,
Shipley G.G., Westbrook E.M.;
"The three-dimensional crystal structure of cholera toxin.";
J. Mol. Biol. 251:563-573(1995).
[17]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 19-210 IN COMPLEX WITH NAD
AND HUMAN ARF6, AND SUBUNIT.
PubMed=16099990; DOI=10.1126/science.1113398;
O'Neal C.J., Jobling M.G., Holmes R.K., Hol W.G.;
"Structural basis for the activation of cholera toxin by human ARF6-
GTP.";
Science 309:1093-1096(2005).
-!- FUNCTION: The A1 chain catalyzes the ADP-ribosylation of Gs alpha,
a GTP-binding regulatory protein, to activate the adenylate
cyclase. This leads to an overproduction of cAMP and eventually to
a hypersecretion of chloride and bicarbonate followed by water,
resulting in the characteristic cholera stool. The A2 chain
tethers A1 to the pentameric ring.
-!- SUBUNIT: 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. Interaction with the host protein ARF6 causes a
conformation change so that the enterotoxin subunit A1 can bind
NAD and catalyze the ADP-ribosylation of the host Gs alpha.
{ECO:0000269|PubMed:16099990, ECO:0000269|PubMed:3214}.
-!- INTERACTION:
P01556:ctxB; NbExp=5; IntAct=EBI-1038392, EBI-1038383;
-!- DOMAIN: The four C-terminal residues of the A2 chain occupy the
central pore of the holotoxin. Deletion of these residues weakens
the interaction between the A subunit and the B pentamer without
impairing the pentamer formation.
-!- MISCELLANEOUS: After binding to gangliosides GM1 in lipid rafts,
through the subunit B pentamer, the holotoxin and the gangliosides
are internalized. The holotoxin remains bound to GM1 until arrival
in the ER. The A subunit has previously been cleaved in the
intestinal lumen but the A1 and A2 chains have remained
associated. In the ER, the A subunit disulfide bridge is reduced,
the A1 chain is unfolded by the PDI and disassembled from the rest
of the toxin. Then, the membrane-associated ER oxidase ERO1
oxidizes PDI, which releases the unfolded A1 chain. The next step
is the retrotranslocation of A1 into the cytosol. This might be
mediated by the protein-conducting pore SEC61. Upon arrival in the
cytosol, A1 refolds and avoids proteasome degradation. In one way
or another, A1 finally reaches its target and induces toxicity.
-!- SIMILARITY: Belongs to the enterotoxin A family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X00171; CAA24995.1; -; Genomic_DNA.
EMBL; X58785; CAA41590.1; -; Genomic_DNA.
EMBL; D30053; BAA06290.1; -; Genomic_DNA.
EMBL; X58786; CAA41592.1; -; Genomic_DNA.
EMBL; K02679; AAA27514.1; -; Genomic_DNA.
EMBL; AF175708; AAD51359.1; -; Genomic_DNA.
EMBL; AE003852; AAF94614.1; -; Genomic_DNA.
EMBL; K01170; AAA27572.1; -; Genomic_DNA.
EMBL; D30052; BAA06288.1; -; Genomic_DNA.
PIR; A05129; XVVCA.
RefSeq; NP_231100.1; NC_002505.1.
RefSeq; WP_001881225.1; NC_002505.1.
PDB; 1S5B; X-ray; 2.13 A; A=19-258.
PDB; 1S5C; X-ray; 2.50 A; A=19-258.
PDB; 1S5D; X-ray; 1.75 A; A=19-258.
PDB; 1S5E; X-ray; 1.90 A; A/B=19-258.
PDB; 1S5F; X-ray; 2.60 A; A=19-258.
PDB; 1XTC; X-ray; 2.40 A; A=19-212, C=213-258.
PDB; 2A5D; X-ray; 1.80 A; B=19-210.
PDB; 2A5F; X-ray; 2.02 A; B=19-210.
PDB; 2A5G; X-ray; 2.66 A; B=19-210.
PDBsum; 1S5B; -.
PDBsum; 1S5C; -.
PDBsum; 1S5D; -.
PDBsum; 1S5E; -.
PDBsum; 1S5F; -.
PDBsum; 1XTC; -.
PDBsum; 2A5D; -.
PDBsum; 2A5F; -.
PDBsum; 2A5G; -.
DisProt; DP00250; -.
ProteinModelPortal; P01555; -.
SMR; P01555; -.
DIP; DIP-6255N; -.
ELM; P01555; -.
IntAct; P01555; 2.
STRING; 243277.VC1457; -.
DNASU; 2613963; -.
EnsemblBacteria; AAF94614; AAF94614; VC_1457.
GeneID; 2613963; -.
KEGG; vch:VC1457; -.
PATRIC; fig|243277.26.peg.1387; -.
eggNOG; ENOG4107927; Bacteria.
eggNOG; ENOG410Y5VZ; LUCA.
KO; K10928; -.
OMA; PRGHNEY; -.
BioCyc; MetaCyc:VC1457-MONOMER; -.
BioCyc; VCHO:VC1457-MONOMER; -.
EvolutionaryTrace; P01555; -.
PRO; PR:P01555; -.
Proteomes; UP000000584; Chromosome 1.
GO; GO:1902494; C:catalytic complex; IMP:CAFA.
GO; GO:0005615; C:extracellular space; IEA:InterPro.
GO; GO:0042597; C:periplasmic space; IMP:CAFA.
GO; GO:0005534; F:galactose binding; IMP:CAFA.
GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IMP:TIGR.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0031640; P:killing of cells of other organism; IMP:TIGR.
GO; GO:0009405; P:pathogenesis; IMP:TIGR.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IDA:CACAO.
GO; GO:0006471; P:protein ADP-ribosylation; IMP:TIGR.
InterPro; IPR001144; Enterotoxin_A.
Pfam; PF01375; Enterotoxin_a; 1.
PRINTS; PR00771; ENTEROTOXINA.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disulfide bond; Enterotoxin; Glycosyltransferase; NAD;
Reference proteome; Signal; Toxin; Transferase.
SIGNAL 1 18 {ECO:0000269|PubMed:7238869,
ECO:0000269|PubMed:955672}.
CHAIN 19 212 Cholera enterotoxin subunit A1.
/FTId=PRO_0000019342.
CHAIN 213 258 Cholera enterotoxin subunit A2.
/FTId=PRO_0000019343.
NP_BIND 25 28 NAD. {ECO:0000269|PubMed:16099990}.
NP_BIND 41 43 NAD. {ECO:0000269|PubMed:16099990}.
ACT_SITE 130 130 {ECO:0000250}.
DISULFID 205 217 Interchain (between A1 and A2 chains).
CONFLICT 20 20 D -> N (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 37 37 S -> R (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 39 39 G -> L (in Ref. 11; AA sequence).
{ECO:0000305}.
CONFLICT 45 46 QS -> SE (in Ref. 11; AA sequence).
{ECO:0000305}.
CONFLICT 111 111 N -> L (in Ref. 11; AA sequence).
{ECO:0000305}.
CONFLICT 132 132 S -> A (in Ref. 11; AA sequence).
{ECO:0000305}.
CONFLICT 213 213 M -> I (in Ref. 1; CAA24995).
{ECO:0000305}.
CONFLICT 247 248 DI -> ID (in Ref. 12; AA sequence).
{ECO:0000305}.
CONFLICT 256 256 D -> N (in Ref. 12; AA sequence).
{ECO:0000305}.
STRAND 22 29 {ECO:0000244|PDB:1S5D}.
HELIX 31 37 {ECO:0000244|PDB:1S5D}.
HELIX 43 45 {ECO:0000244|PDB:1S5D}.
STRAND 51 53 {ECO:0000244|PDB:1XTC}.
HELIX 59 64 {ECO:0000244|PDB:1S5D}.
STRAND 70 72 {ECO:0000244|PDB:1S5D}.
STRAND 77 83 {ECO:0000244|PDB:1S5D}.
HELIX 84 94 {ECO:0000244|PDB:1S5D}.
TURN 95 97 {ECO:0000244|PDB:2A5D}.
STRAND 99 107 {ECO:0000244|PDB:1S5D}.
STRAND 112 114 {ECO:0000244|PDB:1S5D}.
HELIX 115 119 {ECO:0000244|PDB:1S5D}.
HELIX 120 122 {ECO:0000244|PDB:1S5D}.
HELIX 126 128 {ECO:0000244|PDB:1S5D}.
STRAND 131 134 {ECO:0000244|PDB:1S5D}.
HELIX 139 141 {ECO:0000244|PDB:1S5D}.
STRAND 142 149 {ECO:0000244|PDB:1S5D}.
STRAND 152 154 {ECO:0000244|PDB:1S5B}.
STRAND 156 159 {ECO:0000244|PDB:1S5B}.
HELIX 165 169 {ECO:0000244|PDB:1S5D}.
HELIX 176 178 {ECO:0000244|PDB:1S5D}.
HELIX 180 182 {ECO:0000244|PDB:1S5D}.
HELIX 190 193 {ECO:0000244|PDB:1S5D}.
HELIX 197 200 {ECO:0000244|PDB:1S5D}.
HELIX 217 244 {ECO:0000244|PDB:1S5D}.
TURN 245 247 {ECO:0000244|PDB:1S5D}.
TURN 250 252 {ECO:0000244|PDB:1S5D}.
HELIX 254 257 {ECO:0000244|PDB:1XTC}.
SEQUENCE 258 AA; 29336 MW; 0F7EBAE62069A5D0 CRC64;
MVKIIFVFFI FLSSFSYAND DKLYRADSRP PDEIKQSGGL MPRGQSEYFD RGTQMNINLY
DHARGTQTGF VRHDDGYVST SISLRSAHLV GQTILSGHST YYIYVIATAP NMFNVNDVLG
AYSPHPDEQE VSALGGIPYS QIYGWYRVHF GVLDEQLHRN RGYRDRYYSN LDIAPAADGY
GLAGFPPEHR AWREEPWIHH APPGCGNAPR SSMSNTCDEK TQSLGVKFLD EYQSKVKRQI
FSGYQSDIDT HNRIKDEL


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