ID Q47262_ECOLX Unreviewed; 998 AA.
AC Q47262;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 24-JAN-2024, entry version 87.
DE SubName: Full=Hemolysin {ECO:0000313|EMBL:CAA56234.1};
GN Name=EHEC-hlyA {ECO:0000313|EMBL:CAA56234.1};
OS Escherichia coli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:CAA56234.1};
RN [1] {ECO:0000313|EMBL:CAA56234.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=7868227;
RA Schmidt H., Beutin L., Karch H.;
RT "Molecular analysis of the plasmid-encoded hemolysin of Escherichia coli
RT O157:H7 strain EDL 933.";
RL Infect. Immun. 63:1055-1061(1995).
RN [2] {ECO:0000313|EMBL:CAA56234.1}
RP NUCLEOTIDE SEQUENCE.
RA Schmidt H.;
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the RTX prokaryotic toxin (TC 1.C.11) family.
CC {ECO:0000256|ARBA:ARBA00005918}.
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DR EMBL; X79839; CAA56234.1; -; Genomic_DNA.
DR PIR; I41078; I41078.
DR AlphaFoldDB; Q47262; -.
DR SMR; Q47262; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0015267; F:channel activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 3.
DR InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR InterPro; IPR001343; Hemolysn_Ca-bd.
DR InterPro; IPR013550; RTX_C.
DR InterPro; IPR018504; RTX_pore_form.
DR InterPro; IPR003995; RTX_toxin_determinant-A.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR NCBIfam; NF033203; entero_EhxA; 1.
DR NCBIfam; NF033943; RTX_toxin; 1.
DR PANTHER; PTHR38340; S-LAYER PROTEIN; 1.
DR PANTHER; PTHR38340:SF1; S-LAYER PROTEIN; 1.
DR Pfam; PF00353; HemolysinCabind; 2.
DR Pfam; PF02382; RTX; 1.
DR Pfam; PF08339; RTX_C; 1.
DR PRINTS; PR00313; CABNDNGRPT.
DR PRINTS; PR01488; RTXTOXINA.
DR SUPFAM; SSF51120; beta-Roll; 1.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 4.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cytolysis {ECO:0000256|ARBA:ARBA00022852};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Toxin {ECO:0000256|ARBA:ARBA00022656};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT DOMAIN 278..584
FT /note="RTX pore-forming"
FT /evidence="ECO:0000259|Pfam:PF02382"
FT DOMAIN 854..998
FT /note="RTX C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08339"
SQ SEQUENCE 998 AA; 107059 MW; 0D3BE108C309B8B3 CRC64;
MTVNKIKNIF NNATLTTKSA FNTASSSVRS AGKKLILLIP DNYEAQGVGI NELVKAADEL
GIEIHRTERD DTAIANQFFG AAEKVVGLTE RGVAIFAPQL DKLLQKYQKV GSKIGGTAEN
VGNNLGKAGT VLSALQNFTG IALSGMALDE LLRKQREGED ISQNDIAKSS IELINQLVDT
VSSINSTVDS FSEQLNQLGS FLSSKPRLSS VGGKLQNLPD LGPLGDGLDV VSGILSAVSA
SFILGNSDAH TGTKAAAGIE LTTQVLGNVG KAVSQYILAQ RMAQGLSTTA ASAGLITSAV
MLAISPLSFL AAADKFERAK QLESYSERFK KLNYEGDALL AGFHKETGAI DAGLTTINTV
LSSVSAGVSA ASSASLIGAP ISMLVSALTG TISGILEASK QAMFEHVAEK FAARINEWEK
EHGKNYFENG YDARHAAFLE DSLSLLADFS RQHAVERAVA ITHQHWDEKI GELAGITRNA
DRSQSGKPYI NYLENGGLLE AQPKEFTQQV FDPQKGTIDL STGNVSSVLT FITPTFTPGE
EVRERKQSGK YEYMTSLIVN GKDTWSVKGI KNHKGVYDYS KLIQFVEKNT KHYQARIISE
LGDKDDVVYS GAGSSEVFAG EGYDPVSYNK TDVGKLTIDA TGAPKPGEYI VPKNMYGDVE
VLQEVVKEQE VSVGKRTEKI QYRDFEFRTG GIPYDVIDNL HSVEELIGGK HDDEFKGGKF
NDIFHGADGN DYIEGNYGND RLYGDDGDDY ISGGQGDDQL FGGSGNDKLS GGDGNNYLTG
GSGNDELQAH GAYNILSGGT GDDKLYGGGG IDLLDGGEGN DYLNGGFGND IYVYGQNYGH
HTIADEGGKG DRLHLSDISF DDIAFKRVGN DLIMNKAING VLSFNESNDV NGITFKNWFA
KDASGADNHL VEVITDKDGR EIKVDKIPHN NNERSGYIKA SNIASEKNMV NITSVANDIN
KIISSVSGFD SGDERLASLY NLSLHQNNTH STTLTTTV
//
