ELAP_ECOLX
ID ELAP_ECOLX Reviewed; 258 AA.
AC P06717; P01554;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Heat-labile enterotoxin A chain;
DE AltName: Full=LT-A, porcine;
DE AltName: Full=LTP-A;
DE Flags: Precursor;
GN Name=eltA; Synonyms=ltpA;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate P307 / ETEC, and Isolate PCG86 / ETEC;
RX PubMed=3546273; DOI=10.1128/jb.169.3.1352-1357.1987;
RA Yamamoto T., Gojobori T., Yokota T.;
RT "Evolutionary origin of pathogenic determinants in enterotoxigenic
RT Escherichia coli and Vibrio cholerae O1.";
RL J. Bacteriol. 169:1352-1357(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate P307 / ETEC;
RA Dykes C.W., Halliday I.J., Hobden A.N., Read M.J., Harford S.;
RT "A comparison of the nucleotide sequence of the A subunit of heat-labile
RT enterotoxin and cholera toxin.";
RL FEMS Microbiol. Lett. 26:171-174(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate P307 / ETEC;
RX PubMed=6279611; DOI=10.1016/s0021-9258(19)83837-1;
RA Spicer E.K., Noble J.A.;
RT "Escherichia coli heat-labile enterotoxin. Nucleotide sequence of the A
RT subunit gene.";
RL J. Biol. Chem. 257:5716-5721(1982).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 19-258.
RC STRAIN=Isolate P307 / ETEC;
RX PubMed=2266142; DOI=10.1016/s0021-9258(18)45736-5;
RA Tsuji T., Inoue T., Miyama A., Okamoto K., Honda T., Miwatani T.;
RT "A single amino acid substitution in the A subunit of Escherichia coli
RT enterotoxin results in a loss of its toxic activity.";
RL J. Biol. Chem. 265:22520-22525(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
RA Trachman J.D., Maas W.K.;
RL Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=2034287; DOI=10.1038/351371a0;
RA Sixma T.K., Pronk S.E., Kalk K.H., Wartna E.S., van Zanten B.A.M.,
RA Witholt B., Hol W.G.J.;
RT "Crystal structure of a cholera toxin-related heat-labile enterotoxin from
RT E. coli.";
RL Nature 351:371-377(1991).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
RX PubMed=8478941; DOI=10.1006/jmbi.1993.1209;
RA Sixma T.K., van Zanten B.A.M., Dauter Z., Hol W.G.J.;
RT "Refined structure of Escherichia coli heat-labile enterotoxin, a close
RT relative of cholera toxin.";
RL J. Mol. Biol. 230:890-918(1993).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 19-258, AND MUTAGENESIS OF ARG-25;
RP VAL-71; ARG-72; TYR-77; SER-81; ALA-90; VAL-115; TYR-122; HIS-125; GLU-128;
RP GLU-130; SER-132 AND ARG-210.
RX PubMed=7830560; DOI=10.1111/j.1365-2958.1994.tb01266.x;
RA Pizza M., Domenighini M., Hol W.G.J., Giannelli V., Fontana M.R.,
RA Giuliani M.M., Magagnoli C., Peppoloni S., Manetti R., Rappuoli R.;
RT "Probing the structure-activity relationship of Escherichia coli LT-A by
RT site-directed mutagenesis.";
RL Mol. Microbiol. 14:51-60(1994).
RN [9]
RP DISCUSSION OF SEQUENCE.
RX PubMed=7623669; DOI=10.1111/j.1365-2958.1995.tb02289.x;
RA Domenighini M., Pizza M., Jobling M.G., Holmes R.K., Rappuoli R.;
RT "Identification of errors among database sequence entries and comparison of
RT correct amino acid sequences for the heat-labile enterotoxins of
RT Escherichia coli and Vibrio cholerae.";
RL Mol. Microbiol. 15:1165-1167(1995).
CC -!- FUNCTION: The biological activity of the toxin is produced by the A
CC chain, which activates intracellular adenyl cyclase.
CC -!- SUBUNIT: Heterohexamer of one A chain and of five B chains.
CC -!- SIMILARITY: Belongs to the enterotoxin A family. {ECO:0000305}.
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DR EMBL; M15361; AAA24791.1; -; Genomic_DNA.
DR EMBL; M15362; AAA24793.1; -; Genomic_DNA.
DR EMBL; M35581; AAA98202.1; -; Genomic_DNA.
DR EMBL; V00275; CAA23532.1; -; Genomic_DNA.
DR EMBL; M57244; AAB59161.1; -; Genomic_DNA.
DR EMBL; M61015; AAA24335.1; -; Genomic_DNA.
DR PIR; I55231; QLECA.
DR RefSeq; WP_042634421.1; NZ_UGAN01000003.1.
DR PDB; 1HTL; X-ray; 2.50 A; A=19-209, C=210-258.
DR PDB; 1LT3; X-ray; 2.00 A; A=19-258.
DR PDB; 1LT4; X-ray; 2.00 A; A=19-251.
DR PDB; 1LTA; X-ray; 2.20 A; A=19-206, C=210-258.
DR PDB; 1LTB; X-ray; 2.60 A; A=22-206, C=210-254.
DR PDB; 1LTG; X-ray; 2.40 A; A=19-209, C=210-258.
DR PDB; 1LTI; X-ray; 2.13 A; A=19-210, C=211-258.
DR PDB; 1LTS; X-ray; 1.95 A; A=22-206, C=214-254.
DR PDB; 1LTT; X-ray; 2.30 A; A=22-206, C=214-254.
DR PDBsum; 1HTL; -.
DR PDBsum; 1LT3; -.
DR PDBsum; 1LT4; -.
DR PDBsum; 1LTA; -.
DR PDBsum; 1LTB; -.
DR PDBsum; 1LTG; -.
DR PDBsum; 1LTI; -.
DR PDBsum; 1LTS; -.
DR PDBsum; 1LTT; -.
DR AlphaFoldDB; P06717; -.
DR SMR; P06717; -.
DR IntAct; P06717; 1.
DR EvolutionaryTrace; P06717; -.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR001144; Enterotoxin_A.
DR Pfam; PF01375; Enterotoxin_a; 1.
DR PRINTS; PR00771; ENTEROTOXINA.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Enterotoxin; Signal; Toxin; Virulence.
FT SIGNAL 1..18
FT CHAIN 19..258
FT /note="Heat-labile enterotoxin A chain"
FT /id="PRO_0000019351"
FT ACT_SITE 130
FT BINDING 25..39
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT DISULFID 205..217
FT VARIANT 130
FT /note="E -> K (in inactive mutant)"
FT MUTAGEN 25
FT /note="R->K: Abolishes toxicity."
FT /evidence="ECO:0000269|PubMed:7830560"
FT MUTAGEN 71
FT /note="V->D,E: Abolishes toxicity."
FT /evidence="ECO:0000269|PubMed:7830560"
FT MUTAGEN 72
FT /note="R->A,K: No effect."
FT /evidence="ECO:0000269|PubMed:7830560"
FT MUTAGEN 77
FT /note="Y->M: No effect."
FT /evidence="ECO:0000269|PubMed:7830560"
FT MUTAGEN 81
FT /note="S->K: Abolishes toxicity."
FT /evidence="ECO:0000269|PubMed:7830560"
FT MUTAGEN 90
FT /note="A->E,H,R: No effect."
FT /evidence="ECO:0000269|PubMed:7830560"
FT MUTAGEN 115
FT /note="V->K: Abolishes toxicity."
FT /evidence="ECO:0000269|PubMed:7830560"
FT MUTAGEN 122
FT /note="Y->D,K: Abolishes toxicity."
FT /evidence="ECO:0000269|PubMed:7830560"
FT MUTAGEN 125
FT /note="H->E: Strongly reduces toxicity."
FT /evidence="ECO:0000269|PubMed:7830560"
FT MUTAGEN 128
FT /note="E->S: Abolishes toxicity."
FT /evidence="ECO:0000269|PubMed:7830560"
FT MUTAGEN 130
FT /note="E->S: Abolishes toxicity."
FT /evidence="ECO:0000269|PubMed:7830560"
FT MUTAGEN 132
FT /note="S->E,K: Abolishes toxicity."
FT /evidence="ECO:0000269|PubMed:7830560"
FT MUTAGEN 210
FT /note="R->N: No effect."
FT /evidence="ECO:0000269|PubMed:7830560"
FT CONFLICT 37..39
FT /note="SGG -> FRS (in Ref. 3; CAA23532)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="Missing (in Ref. 3; CAA23532)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="S -> Y (in Ref. 3; CAA23532)"
FT /evidence="ECO:0000305"
FT CONFLICT 100..110
FT /note="TYYIYVIATAP -> LTIYIVIA (in Ref. 3; CAA23532)"
FT /evidence="ECO:0000305"
FT CONFLICT 119..120
FT /note="LG -> IS (in Ref. 3; CAA23532)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="R -> G (in Ref. 4; AAB59161)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="N -> D (in Ref. 3; CAA23532)"
FT /evidence="ECO:0000305"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:1LTS"
FT HELIX 31..37
FT /evidence="ECO:0007829|PDB:1LTS"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:1LTI"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:1LTA"
FT HELIX 59..64
FT /evidence="ECO:0007829|PDB:1LTS"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:1LTS"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:1LTS"
FT HELIX 84..94
FT /evidence="ECO:0007829|PDB:1LTS"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:1LTI"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:1LTS"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:1LTS"
FT HELIX 115..119
FT /evidence="ECO:0007829|PDB:1LTS"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:1LTS"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:1LTS"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:1LTS"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:1LTS"
FT STRAND 142..149
FT /evidence="ECO:0007829|PDB:1LTS"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:1LT3"
FT HELIX 165..170
FT /evidence="ECO:0007829|PDB:1LTS"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:1LTS"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:1LTS"
FT HELIX 190..193
FT /evidence="ECO:0007829|PDB:1LTS"
FT HELIX 197..200
FT /evidence="ECO:0007829|PDB:1LTS"
FT HELIX 215..240
FT /evidence="ECO:0007829|PDB:1LTS"
FT HELIX 241..244
FT /evidence="ECO:0007829|PDB:1LTS"
FT HELIX 250..253
FT /evidence="ECO:0007829|PDB:1LTS"
SQ SEQUENCE 258 AA; 29902 MW; 2F0786442619F81F CRC64;
MKNITFIFFI LLASPLYANG DRLYRADSRP PDEIKRSGGL MPRGHNEYFD RGTQMNINLY
DHARGTQTGF VRYDDGYVST SLSLRSAHLA GQSILSGYST YYIYVIATAP NMFNVNDVLG
VYSPHPYEQE VSALGGIPYS QIYGWYRVNF GVIDERLHRN REYRDRYYRN LNIAPAEDGY
RLAGFPPDHQ AWREEPWIHH APQGCGNSSR TITGDTCNEE TQNLSTIYLR EYQSKVKRQI
FSDYQSEVDI YNRIRDEL
