HLYE_ECO57
ID HLYE_ECO57 Reviewed; 303 AA.
AC Q9REB3;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Hemolysin E;
DE AltName: Full=Cytotoxin ClyA;
DE AltName: Full=Silent hemolysin SheA;
GN Name=hlyE; Synonyms=clyA, sheA; OrderedLocusNames=Z1944, ECs1677;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O157:H7 / EHEC;
RX PubMed=10865950; DOI=10.1016/s0923-2508(00)00143-1;
RA del Castillo F.J., Moreno F., del Castillo I.;
RT "Characterization of the genes encoding the SheA haemolysin in Escherichia
RT coli O157:H7 and Shigella flexneri 2a.";
RL Res. Microbiol. 151:229-230(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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=AAG56033.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB35100.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB64962.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ238954; CAB64962.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE005174; AAG56033.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000007; BAB35100.1; ALT_INIT; Genomic_DNA.
DR PIR; E85696; E85696.
DR PIR; E90838; E90838.
DR RefSeq; NP_309704.2; NC_002695.1.
DR RefSeq; WP_001304191.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q9REB3; -.
DR SMR; Q9REB3; -.
DR STRING; 155864.EDL933_1876; -.
DR EnsemblBacteria; AAG56033; AAG56033; Z1944.
DR EnsemblBacteria; BAB35100; BAB35100; ECs_1677.
DR GeneID; 913196; -.
DR KEGG; ece:Z1944; -.
DR KEGG; ecs:ECs_1677; -.
DR PATRIC; fig|386585.9.peg.1774; -.
DR eggNOG; ENOG502ZB9A; Bacteria.
DR HOGENOM; CLU_080941_0_0_6; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; Reference proteome; Secreted; Toxin; Transmembrane;
KW Transmembrane helix; Virulence.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..303
FT /note="Hemolysin E"
FT /id="PRO_0000083995"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DISULFID 87..285
FT /note="In monomeric form"
FT /evidence="ECO:0000250"
SQ SEQUENCE 303 AA; 33716 MW; D4A5707EAB0A9605 CRC64;
MTEIVADKTV EVVKNAIETA DGALDLYNKY LDQVIPWQTF DETIKELSRF KQEYSQAASV
LVGNIKTLLM DSQDKYFEAT QTVYEWCGVA TQLLAAYILL FDEYNEKKAS AQKDILIKVL
DDGITKLNEA QKSLLVSSQS FNNASGKLLA LDSQLTNDFS EKSSYFQSQV DKIRKEAYAG
AAAGVVAGPF GLIISYSIAA GVVEGKLIPE LKNKLKSVQS FFTTLSNTVK QANKDIDAAK
LKLTTEIAAI GEIKTETETT RFYVDYDDLM LSLLKEAANK MINTCNEYQK RHGKKTLFEV
PEV
