ID   HLYE_SALPA              Reviewed;         303 AA.
AC   Q93RR6; Q5PHY8;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Hemolysin E;
DE   AltName: Full=Cytotoxin ClyA;
DE   AltName: Full=Silent hemolysin SheA;
GN   Name=hlyE; Synonyms=clyA, sheA; OrderedLocusNames=SPA1306;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SMI S3068/99;
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=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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=AAV77254.1; Type=Erroneous initiation; Evidence={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; AJ313033; CAC38362.1; -; Genomic_DNA.
DR   EMBL; CP000026; AAV77254.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q93RR6; -.
DR   SMR; Q93RR6; -.
DR   EnsemblBacteria; AAV77254; AAV77254; SPA1306.
DR   KEGG; spt:SPA1306; -.
DR   HOGENOM; CLU_080941_0_0_6; -.
DR   Proteomes; UP000008185; 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: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_0000083997"
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;  33744 MW;  041F03F2018CCAE3 CRC64;
     MTGIFAEQTV EVVKSAIETA DGALDFYNKY LDQVIPWKTF DETIKELSRF KQEYSQEASV
     LVGDIKVLLM DSQDKYFEAT QTVYEWCGVV TQLLSAYILL FDEYNEKKAS AQKDILIRIL
     DDGVNKLNEA QKSLLGSSQS FNNASGKLLA LDSQLTNDFS EKSSYFQSQV DRIRKEAYAG
     AAAGIVAGPF GLIISYSIAA GVIEGKLIPE LNDRLKAVQN FFTSLSVTVK QANKDIDAAK
     LKLATEIAAI GEIKTETETT RFYVDYDDLM LSLLKGAAKK MINTCNEYQQ RHGKKTLLEV
     PDI