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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}.
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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
 
 
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