ID   Q44063_AERHY            Unreviewed;       493 AA.
AC   Q44063;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 79.
DE   SubName: Full=Cytolytic enterotoxin {ECO:0000313|EMBL:AAA72103.1};
OS   Aeromonas hydrophila.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=644 {ECO:0000313|EMBL:AAA72103.1};
RN   [1] {ECO:0000313|EMBL:AAA72103.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=8330262;
RA   Chopra A.K., Houston C.W., Peterson J.W., Jin G.F.;
RT   "Cloning, expression, and sequence analysis of a cytolytic enterotoxin gene
RT   from Aeromonas hydrophila.";
RL   Can. J. Microbiol. 39:513-523(1993).
CC   -!- SUBUNIT: Homodimer in solution; homoheptamer in the host membrane.
CC       After binding to GPI-anchored proteins in target membranes and
CC       proteolytic removal of the C-terminal propeptide, the protein assembles
CC       into a heptameric pre-pore complex. A further conformation change leads
CC       to insertion into the host membrane. {ECO:0000256|ARBA:ARBA00026029}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC       Host cell membrane {ECO:0000256|ARBA:ARBA00004165}. Secreted
CC       {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the aerolysin family.
CC       {ECO:0000256|ARBA:ARBA00009831}.
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DR   EMBL; M84709; AAA72103.1; -; Genomic_DNA.
DR   PIR; A30590; A30590.
DR   PIR; I39541; I39541.
DR   AlphaFoldDB; Q44063; -.
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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   CDD; cd20218; PFM_aerolysin; 1.
DR   Gene3D; 3.10.40.10; Aerolysin/Pertussis toxin (APT), N-terminal domain; 1.
DR   Gene3D; 3.30.412.10; Proaerolysin, chain A, domain 2; 1.
DR   Gene3D; 2.170.15.10; Proaerolysin, chain A, domain 3; 1.
DR   InterPro; IPR005831; Aerolysin/haemolysin_CS.
DR   InterPro; IPR005830; Aerolysn.
DR   InterPro; IPR005138; APT_dom.
DR   InterPro; IPR037015; APT_N_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   Pfam; PF01117; Aerolysin; 1.
DR   Pfam; PF03440; APT; 1.
DR   PRINTS; PR00754; AEROLYSIN.
DR   SMART; SM00999; Aerolysin; 1.
DR   SUPFAM; SSF56973; Aerolisin/ETX pore-forming domain; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   PROSITE; PS00274; AEROLYSIN; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Host cell membrane {ECO:0000256|ARBA:ARBA00022511};
KW   Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Toxin {ECO:0000256|ARBA:ARBA00022656};
KW   Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..493
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004232015"
FT   DOMAIN          24..105
FT                   /note="Aerolysin/Pertussis toxin"
FT                   /evidence="ECO:0000259|Pfam:PF03440"
SQ   SEQUENCE   493 AA;  54488 MW;  ED984E02CA031845 CRC64;
     MQKLKITGLS LIISGLLIAQ AHAAEPVYPD QLRLFSLGQE VCGDKYRPIT REEAQSVKSN
     IVNMMGQWQI SGLANGWVIM GPGYNGEIKP GSASNTWCYP VNPVTGEIPT LSALDIPDGD
     EVDVQWRLVH DSANFIKPTS YLAHYLGYAW VGGNHSQYVG EDMDVTRDGD GWVIRGNNDG
     GCEGYRCGEK TSIKVSNFAY NLDPDSFKHG DVTQSDRQLV KTVVGWAIND SDTPQSGYDV
     TLRYDTATNW SKTNTYGLSE KVTTKNKFKW PLVGETELSI EIAANQSWAS QNGGSTTTSL
     SQSVRPTVPA RSKIPVKIEL YKADISYPYE FKADVSYDLT LSGFLRWGGN AWYTHPDNRP
     NWNHTFVIGP YKDKASSIRY QWDKRYIPGE VKWWDWNWTI QQNGLSTMQN NLARVLRPVR
     AGITGDFSAE SQFAGNIEIG APVPLAADGK APRALSARRG EQGLRLEIPL DAQELSGLGF
     SNVSLSVTPA ANQ
//