ELBP_ECOLX
ID ELBP_ECOLX Reviewed; 124 AA.
AC P32890; P01557; P13768;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Heat-labile enterotoxin B chain;
DE AltName: Full=LT-B, porcine;
DE AltName: Full=LTP-B;
DE Flags: Precursor;
GN Name=eltB; Synonyms=ltpB;
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;
RX PubMed=7003397; DOI=10.1038/288499a0;
RA Dallas W.S., Falkow S.;
RT "Amino acid sequence homology between cholera toxin and Escherichia coli
RT heat-labile toxin.";
RL Nature 288:499-501(1980).
RN [2]
RP SEQUENCE REVISION TO 28 AND 64.
RC STRAIN=Isolate P307 / ETEC;
RX PubMed=3884513; DOI=10.1128/iai.48.1.73-77.1985;
RA Leong J., Vinal A.C., Dallas W.S.;
RT "Nucleotide sequence comparison between heat-labile toxin B-subunit
RT cistrons from Escherichia coli of human and porcine origin.";
RL Infect. Immun. 48:73-77(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
RX PubMed=3301830; DOI=10.1016/s0021-9258(18)61096-8;
RA Ibrahimi I., Gentz R.;
RT "A functional interaction between the signal peptide and the translation
RT apparatus is detected by the use of a single point mutation which blocks
RT translocation across mammalian endoplasmic reticulum.";
RL J. Biol. Chem. 262:10189-10194(1987).
RN [5]
RP PROTEIN SEQUENCE OF 22-124.
RC STRAIN=240-3 / ETEC;
RX PubMed=3333803; DOI=10.1016/0882-4010(87)90079-9;
RA Tsuji T., Iida T., Honda T., Miwatani T., Nagahama M., Sakurai J., Wada K.,
RA Matsubara H.;
RT "A unique amino acid sequence of the B subunit of a heat-labile enterotoxin
RT isolated from a human enterotoxigenic Escherichia coli.";
RL Microb. Pathog. 2:381-390(1987).
RN [6]
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 [7]
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 [8]
RP X-RAY CRYSTALLOGRAPHY (2.14 ANGSTROMS).
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 [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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M17873; AAA98065.1; -; Genomic_DNA.
DR EMBL; M15363; AAA24792.1; -; Genomic_DNA.
DR EMBL; M17101; AAA23973.1; -; Genomic_DNA.
DR PIR; A01820; QLECB.
DR RefSeq; WP_015675362.1; NZ_UGAN01000003.1.
DR PDB; 1DJR; X-ray; 1.30 A; D/E/F/G/H=22-124.
DR PDB; 1EEF; X-ray; 1.80 A; D/E/F/G/H/L/M/N/O/P=22-124.
DR PDB; 1EFI; X-ray; 1.60 A; D/E/F/G/H=22-124.
DR PDB; 1FD7; X-ray; 1.80 A; D/E/F/G/H/L/M/N/O/P=22-124.
DR PDB; 1HTL; X-ray; 2.50 A; D/E/F/G/H=22-124.
DR PDB; 1JQY; X-ray; 2.14 A; D/E/F/G/H/L/M/N/O/P/V/W/X/Y/Z=22-124.
DR PDB; 1LT3; X-ray; 2.00 A; D/E/F/G/H=22-124.
DR PDB; 1LT4; X-ray; 2.00 A; D/E/F/G/H=22-124.
DR PDB; 1LT5; X-ray; 1.70 A; D/E/F/G/H=22-124.
DR PDB; 1LT6; X-ray; 2.20 A; D/E/F/G/H/L/M/N/O/P=22-124.
DR PDB; 1LTA; X-ray; 2.20 A; D/E/F/G/H=22-124.
DR PDB; 1LTB; X-ray; 2.60 A; D/E/F/G/H=22-124.
DR PDB; 1LTG; X-ray; 2.40 A; D/E/F/G/H=22-124.
DR PDB; 1LTI; X-ray; 2.13 A; D/E/F/G/H=22-124.
DR PDB; 1LTS; X-ray; 1.95 A; D/E/F/G/H=22-124.
DR PDB; 1LTT; X-ray; 2.30 A; D/E/F/G/H=22-124.
DR PDB; 1PZI; X-ray; 1.99 A; D/E/F/G/H=22-124.
DR PDB; 1TET; X-ray; 2.30 A; P=71-85.
DR PDB; 2XRQ; X-ray; 2.40 A; D/E/F/G/H=22-124.
DR PDB; 2XRS; X-ray; 1.81 A; D/E/F/G/H/L/M/N/O/P=22-124.
DR PDB; 5LZI; X-ray; 1.60 A; A/B/C/D/E=22-124.
DR PDB; 6IAL; X-ray; 1.45 A; A/B/C/D/E/F/G/H/I/J=22-124.
DR PDBsum; 1DJR; -.
DR PDBsum; 1EEF; -.
DR PDBsum; 1EFI; -.
DR PDBsum; 1FD7; -.
DR PDBsum; 1HTL; -.
DR PDBsum; 1JQY; -.
DR PDBsum; 1LT3; -.
DR PDBsum; 1LT4; -.
DR PDBsum; 1LT5; -.
DR PDBsum; 1LT6; -.
DR PDBsum; 1LTA; -.
DR PDBsum; 1LTB; -.
DR PDBsum; 1LTG; -.
DR PDBsum; 1LTI; -.
DR PDBsum; 1LTS; -.
DR PDBsum; 1LTT; -.
DR PDBsum; 1PZI; -.
DR PDBsum; 1TET; -.
DR PDBsum; 2XRQ; -.
DR PDBsum; 2XRS; -.
DR PDBsum; 5LZI; -.
DR PDBsum; 6IAL; -.
DR AlphaFoldDB; P32890; -.
DR SMR; P32890; -.
DR DIP; DIP-36815N; -.
DR IntAct; P32890; 2.
DR DrugBank; DB03421; 2-Phenethyl-2,3-Dihydro-Phthalazine-1,4-Dione.
DR DrugBank; DB02213; Metanitrophenyl-Alpha-D-Galactoside.
DR DrugBank; DB04040; N-[1,3-Di(4-morpholinyl)-2-propanyl]-3-(Alpha-D-galactopyranosyloxy)-5-nitrobenzamide.
DR DrugBank; DB03446; N-Benzyl-3-(alpha-D-galactopyranosyloxy)benzamide.
DR DrugBank; DB03242; P-Aminophenyl-Alpha-D-Galactopyranoside.
DR DrugBank; DB04396; Thiodigalactoside.
DR UniLectin; P32890; -.
DR ABCD; P32890; 1 sequenced antibody.
DR EvolutionaryTrace; P32890; -.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; 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 Signal; Toxin; Virulence.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:3333803"
FT CHAIN 22..124
FT /note="Heat-labile enterotoxin B chain"
FT /id="PRO_0000019355"
FT DISULFID 30..107
FT VARIANT 96
FT /note="T -> A (in strain: 240-3 / ETEC)"
FT HELIX 26..30
FT /evidence="ECO:0007829|PDB:1DJR"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:1DJR"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:1DJR"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:1DJR"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:1DJR"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:1HTL"
FT HELIX 82..98
FT /evidence="ECO:0007829|PDB:1DJR"
FT STRAND 103..123
FT /evidence="ECO:0007829|PDB:1DJR"
SQ SEQUENCE 124 AA; 14133 MW; 6DB7DE58395EA70D CRC64;
MNKVKCYVLF TALLSSLYAH GAPQTITELC SEYRNTQIYT INDKILSYTE SMAGKREMVI
ITFKSGETFQ VEVPGSQHID SQKKAIERMK DTLRITYLTE TKIDKLCVWN NKTPNSIAAI
SMKN
