HST1_ECOLX
ID HST1_ECOLX Reviewed; 72 AA.
AC P01559; Q47653;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Heat-stable enterotoxin ST-IA/ST-P;
DE AltName: Full=STh;
DE AltName: Full=STp;
DE Flags: Precursor;
GN Name=sta1;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TRANSPOSON=Tn1681;
RX PubMed=6254008; DOI=10.1073/pnas.77.7.4011;
RA So M., McCarthy B.J.;
RT "Nucleotide sequence of the bacterial transposon Tn1681 encoding a heat-
RT stable (ST) toxin and its identification in enterotoxigenic Escherichia
RT coli strains.";
RL Proc. Natl. Acad. Sci. U.S.A. 77:4011-4015(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O42:K86:H37 / 18D / ETEC;
RX PubMed=2203756; DOI=10.1128/jb.172.9.5490-5493.1990;
RA Dallas W.S.;
RT "The heat-stable toxin I gene from Escherichia coli 18D.";
RL J. Bacteriol. 172:5490-5493(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2990268;
RA Sekizaki T., Akashi H., Terakado N.;
RT "Nucleotide sequences of the genes for Escherichia coli heat-stable
RT enterotoxin I of bovine, avian, and porcine origins.";
RL Am. J. Vet. Res. 46:909-912(1985).
RN [4]
RP DISULFIDE BONDS.
RX PubMed=3552731; DOI=10.1016/0014-5793(87)80134-5;
RA Shimonishi Y., Hidaka Y., Koizumi M., Hane M., Aimoto S., Takeda T.,
RA Miwatani T., Takeda Y.;
RT "Mode of disulfide bond formation of a heat-stable enterotoxin (STh)
RT produced by a human strain of enterotoxigenic Escherichia coli.";
RL FEBS Lett. 215:165-170(1987).
RN [5]
RP PROTEOLYTIC PROCESSING.
RX PubMed=2203746; DOI=10.1128/jb.172.9.5260-5265.1990;
RA Okamoto K., Takahara M.;
RT "Synthesis of Escherichia coli heat-stable enterotoxin STp as a pre-pro
RT form and role of the pro sequence in secretion.";
RL J. Bacteriol. 172:5260-5265(1990).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (0.89 ANGSTROMS) OF 59-71.
RX PubMed=8038153; DOI=10.1021/bi00195a004;
RA Sato T., Ozaki H., Hata Y., Kitagawa Y., Katsube Y., Shimonishi Y.;
RT "Structural characteristics for biological activity of heat-stable
RT enterotoxin produced by enterotoxigenic Escherichia coli: X-ray
RT crystallography of weakly toxic and nontoxic analogs.";
RL Biochemistry 33:8641-8650(1994).
CC -!- FUNCTION: Toxin which activates the particulate form of guanylate
CC cyclase and increases cyclic GMP levels within the host intestinal
CC epithelial cells.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the heat-stable enterotoxin family.
CC {ECO:0000305}.
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; V00612; CAA23883.1; -; Genomic_DNA.
DR EMBL; M58746; AAA62776.1; -; Genomic_DNA.
DR EMBL; M25607; AAA24653.1; -; Genomic_DNA.
DR PIR; A01822; QHEC1.
DR RefSeq; WP_001353651.1; NZ_WTVB01000054.1.
DR PDB; 1ETL; X-ray; 0.89 A; A=60-71.
DR PDB; 1ETM; X-ray; 0.89 A; A=60-71.
DR PDB; 1ETN; X-ray; 0.89 A; A=60-71.
DR PDBsum; 1ETL; -.
DR PDBsum; 1ETM; -.
DR PDBsum; 1ETN; -.
DR AlphaFoldDB; P01559; -.
DR SMR; P01559; -.
DR Reactome; R-HSA-8942233; Intestinal infectious diseases.
DR EvolutionaryTrace; P01559; -.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR019806; Heat-stable_enterotox_CS.
DR InterPro; IPR001489; Heat-stable_enterotox_STa.
DR Pfam; PF02048; Enterotoxin_ST; 1.
DR PROSITE; PS00273; ENTEROTOXIN_H_STABLE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Enterotoxin; Secreted; Signal; Toxin;
KW Transposable element; Virulence.
FT SIGNAL 1..19
FT PROPEP 20..54
FT /id="PRO_0000035126"
FT PEPTIDE 55..72
FT /note="Heat-stable enterotoxin ST-IA/ST-P"
FT /id="PRO_0000035127"
FT DISULFID 59..64
FT /evidence="ECO:0000269|PubMed:3552731"
FT DISULFID 60..68
FT /evidence="ECO:0000269|PubMed:3552731"
FT DISULFID 63..71
FT /evidence="ECO:0000269|PubMed:3552731"
FT CONFLICT 70
FT /note="G -> P (in Ref. 3; AAA24653)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 72 AA; 8075 MW; 92E8B766B3988264 CRC64;
MKKLMLAIFI SVLSFPSFSQ STESLDSSKE KITLETKKCD VVKNNSEKKS ENMNNTFYCC
ELCCNPACAG CY