ID   AERA_AERSO              Reviewed;         488 AA.
AC   Q06304;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Aerolysin;
DE   AltName: Full=Hemolysin;
DE   Flags: Precursor;
GN   Name=asa1;
OS   Aeromonas sobria.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=646;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=33;
RX   PubMed=1302284; DOI=10.1016/0882-4010(92)90011-c;
RA   Hirono I., Aoki T., Asao T., Kozaki S.;
RT   "Nucleotide sequences and characterization of haemolysin genes from
RT   Aeromonas hydrophila and Aeromonas sobria.";
RL   Microb. Pathog. 13:433-446(1992).
CC   -!- FUNCTION: Secreted, cytolytic toxin that forms pores in host membranes
CC       after proteolytic removal of a C-terminal propeptide, leading to
CC       destruction of the membrane permeability barrier and cell death. The
CC       pores are formed by transmembrane beta-strands and are approximately 3
CC       nm in diameter. {ECO:0000269|PubMed:1302284}.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1302284}. Host cell
CC       membrane {ECO:0000269|PubMed:1302284}. Note=Secreted as a soluble
CC       precursor.
CC   -!- DOMAIN: The C-terminal propeptide is required for normal protein
CC       folding and secretion; it maintains the aerolysin precursor in its
CC       soluble form and prevents premature heptamerization and pore formation.
CC       {ECO:0000250}.
CC   -!- PTM: Proteolytic cleavage and subsequent release of the propeptide
CC       trigger a major conformation change, leading to the formation of a
CC       heptameric pre-pore that then inserts into the host membrane.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the aerolysin family. {ECO:0000305}.
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DR   EMBL; X65046; CAA46182.1; -; Genomic_DNA.
DR   PIR; I39682; S26576.
DR   AlphaFoldDB; Q06304; -.
DR   SMR; Q06304; -.
DR   STRING; 646.BJD16_10710; -.
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:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.40.10; -; 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; SSF56436; SSF56436; 1.
DR   PROSITE; PS00274; AEROLYSIN; 1.
PE   3: Inferred from homology;
KW   Cytolysis; Disulfide bond; Hemolysis; Host cell membrane; Host membrane;
KW   Membrane; Secreted; Signal; Toxin; Transmembrane;
KW   Transmembrane beta strand; Virulence.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..443
FT                   /note="Aerolysin"
FT                   /id="PRO_0000035630"
FT   PROPEP          444..488
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000035631"
FT   REGION          69..85
FT                   /note="Interaction with host N-linked glycan"
FT                   /evidence="ECO:0000250"
FT   REGION          256..288
FT                   /note="Part of the transmembrane beta-barrel after
FT                   proteolytic activation of the toxin and insertion into the
FT                   host membrane"
FT                   /evidence="ECO:0000250"
FT   REGION          346..355
FT                   /note="Interaction with glycans from host GPI-anchor"
FT                   /evidence="ECO:0000250"
FT   SITE            156
FT                   /note="Important for oligomerization"
FT                   /evidence="ECO:0000250"
FT   SITE            390
FT                   /note="Important for heptamerization"
FT                   /evidence="ECO:0000250"
FT   DISULFID        43..99
FT                   /evidence="ECO:0000250"
FT   DISULFID        183..188
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   488 AA;  53921 MW;  F4C4821F86F9BF82 CRC64;
     MMNRIITANL AFLASSLMLA QVQAAEPVYP DQVKWAGLGT GVCASGYRPL TRDEAMSIKG
     NLVSRMGQWQ ITGLADRWVI MGPGYNGEIK QGTAGETWCY PNSPVSGEIP TLSDWNIPAG
     DEVDVQWRLV HDNDYFIKPV SYLAHYLGYA WVGGNHSPYV GEDMDVTRVG DGWLIKGNND
     GGCSGYRCGE KSSIKVSNFS YTLEPDSFSH GQVTESGKQL VKTITANATN YTDLPQQVVV
     TLKYDKATNW SKTDTYSLSE KVTTKNKFQW PLVGETELAI EIAASQSWAS QKGGSTTETV
     SVEARPTVPP HSSLPVRVAL YKSNISYPYE FKAEVNYDLT MKGFLRWGGN AWYTHPDNRP
     TWEHTLLLGP FRGQGEQHPL PVDKRYIPGE VKWWDWNWTI SEYGLSTMQN NLGRVLRPIR
     SAVTGDFYAE SQFAGDIEIG QPQTRSAKAA QLRSASAEEV ALTSVDLDSE ALANEGFGNV
     SLTIVPVQ