HLYE_SALTI
ID HLYE_SALTI Reviewed; 303 AA.
AC Q8Z727; Q934C4;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Hemolysin E;
DE AltName: Full=Cytotoxin ClyA;
DE AltName: Full=Silent hemolysin SheA;
GN Name=hlyE; Synonyms=clyA, sheA; OrderedLocusNames=STY1498, t1477;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SMI S2369/96, and Ty21a;
RX PubMed=12228306; DOI=10.1128/iai.70.10.5759-5769.2002;
RA Oscarsson J., Westermark M., Loefdahl S., Olsen B., Palmgren H.,
RA Mizunoe Y., Wai S.N., Uhlin B.E.;
RT "Characterization of a pore-forming cytotoxin expressed by Salmonella
RT enterica serovars typhi and paratyphi A.";
RL Infect. Immun. 70:5759-5769(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
CC -!- FUNCTION: Toxin, which has some hemolytic activity towards mammalian
CC cells. Acts by forming a pore-like structure upon contact with
CC mammalian cells (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer and oligomer. In periplasm, it is present as a
CC monomer, while in outer membrane vesicles, it oligomerizes to form a
CC pore structure that is active. The pore is formed by a dodecamer (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Periplasm {ECO:0000250}.
CC Host cell membrane {ECO:0000305}; Single-pass membrane protein
CC {ECO:0000305}. Note=Exported from the cell by outer membrane vesicles.
CC Also found in the periplasmic space (By similarity). {ECO:0000250}.
CC -!- PTM: In periplasm, it forms a disulfide bond, which prevents the
CC oligomerization. In outer membrane vesicles, the redox status prevents
CC formation of the disulfide bond, leading to oligomerization and pore
CC formation (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the hemolysin E family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO69115.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAD01758.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ313032; CAC38360.1; -; Genomic_DNA.
DR EMBL; AJ313034; CAC38363.1; -; Genomic_DNA.
DR EMBL; AL513382; CAD01758.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE014613; AAO69115.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_455928.1; NC_003198.1.
DR RefSeq; WP_001681583.1; NZ_WSUR01000006.1.
DR AlphaFoldDB; Q8Z727; -.
DR SMR; Q8Z727; -.
DR STRING; 220341.16502606; -.
DR EnsemblBacteria; AAO69115; AAO69115; t1477.
DR KEGG; stt:t1477; -.
DR KEGG; sty:STY1498; -.
DR PATRIC; fig|220341.7.peg.1508; -.
DR eggNOG; ENOG502ZB9A; Bacteria.
DR HOGENOM; CLU_080941_0_0_6; -.
DR OMA; LTICHAD; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0019836; P:hemolysis by symbiont of host erythrocytes; IMP:CACAO.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR InterPro; IPR027018; Hemolysin_E.
DR Pfam; PF06109; HlyE; 1.
PE 3: Inferred from homology;
KW Cytolysis; Disulfide bond; Hemolysis; Host cell membrane; Host membrane;
KW Membrane; Periplasm; Secreted; Toxin; Transmembrane; Transmembrane helix;
KW Virulence.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..303
FT /note="Hemolysin E"
FT /id="PRO_0000083998"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DISULFID 87..285
FT /note="In monomeric form"
FT /evidence="ECO:0000250"
SQ SEQUENCE 303 AA; 33790 MW; 0D1B4AD566AB972C CRC64;
MTGIFAEQTV EVVKSAIETA DGALDLYNKY LDQVIPWKTF DETIKELSRF KQEYSQEASV
LVGDIKVLLM DSQDKYFEAT QTVYEWCGVV TQLLSAYILL FDEYNEKKAS AQKDILIRIL
DDGVKKLNEA QKSLLTSSQS FNNASGKLLA LDSQLTNDFS EKSSYFQSQV DRIRKEAYAG
AAAGIVAGPF GLIISYSIAA GVIEGKLIPE LNNRLKTVQN FFTSLSATVK QANKDIDAAK
LKLATEIAAI GEIKTETETT RFYVDYDDLM LSLLKGAAKK MINTCNEYQQ RHGKKTLFEV
PDV
