ID   HLYA_ACTSU              Reviewed;         956 AA.
AC   Q00951;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Hemolysin;
DE   AltName: Full=APPA;
DE   AltName: Full=CLY-IIA;
DE   AltName: Full=CYTC;
DE   AltName: Full=Cytolysin II;
DE   AltName: Full=HLY-IIA;
GN   Name=appA; Synonyms=clyIIA, cytC, hlyIIA;
OS   Actinobacillus suis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=716;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=3714;
RX   PubMed=1587585; DOI=10.1128/iai.60.6.2166-2173.1992;
RA   Burrows L.L., Lo R.Y.;
RT   "Molecular characterization of an RTX toxin determinant from Actinobacillus
RT   suis.";
RL   Infect. Immun. 60:2166-2173(1992).
CC   -!- FUNCTION: Bacterial hemolysins are exotoxins that attack host cell
CC       membranes and cause cell rupture by forming a pore.
CC       {ECO:0000250|UniProtKB:P08715}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P08715}. Host
CC       cell membrane {ECO:0000250|UniProtKB:P08715}; Multi-pass membrane
CC       protein {ECO:0000250|UniProtKB:P08715}.
CC   -!- DOMAIN: The Gly-rich region is probably involved in binding calcium,
CC       which is required for target cell-binding or cytolytic activity.
CC   -!- DOMAIN: The three transmembrane domains are believed to be involved in
CC       pore formation by the cytotoxin. {ECO:0000250|UniProtKB:P08715}.
CC   -!- PTM: Fatty acylated by LktC; the toxin only becomes active when
CC       modified. {ECO:0000250|UniProtKB:P08715}.
CC   -!- SIMILARITY: Belongs to the RTX prokaryotic toxin (TC 1.C.11) family.
CC       {ECO:0000305}.
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DR   EMBL; M90440; AAA21918.1; -; Genomic_DNA.
DR   PIR; A43834; A43834.
DR   AlphaFoldDB; Q00951; -.
DR   SMR; Q00951; -.
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:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   Gene3D; 2.150.10.10; -; 1.
DR   InterPro; IPR001343; Hemolysn_Ca-bd.
DR   InterPro; IPR013550; RTX_C.
DR   InterPro; IPR018504; RTX_N.
DR   InterPro; IPR003995; RTX_toxin_determinant-A.
DR   InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR   Pfam; PF00353; HemolysinCabind; 3.
DR   Pfam; PF02382; RTX; 1.
DR   Pfam; PF08339; RTX_C; 1.
DR   PRINTS; PR01488; RTXTOXINA.
DR   SUPFAM; SSF51120; SSF51120; 1.
DR   PROSITE; PS00330; HEMOLYSIN_CALCIUM; 1.
PE   3: Inferred from homology;
KW   Calcium; Cytolysis; Hemolysis; Host cell membrane; Host membrane;
KW   Lipoprotein; Membrane; Myristate; Repeat; Secreted; Toxin; Transmembrane;
KW   Transmembrane helix; Virulence.
FT   CHAIN           1..956
FT                   /note="Hemolysin"
FT                   /id="PRO_0000196217"
FT   TRANSMEM        238..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        302..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        383..406
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REPEAT          718..735
FT                   /note="Hemolysin-type calcium-binding 1"
FT   REPEAT          736..753
FT                   /note="Hemolysin-type calcium-binding 2"
FT   REPEAT          754..771
FT                   /note="Hemolysin-type calcium-binding 3"
FT   REPEAT          772..789
FT                   /note="Hemolysin-type calcium-binding 4"
FT   REPEAT          792..809
FT                   /note="Hemolysin-type calcium-binding 5"
SQ   SEQUENCE   956 AA;  102453 MW;  3415FF1D7ADD4365 CRC64;
     MSKITLSSLK SSLQQGLKNG KNKLNQAGTT LKNGLTQTGH SLQNGAKKLI LYIPQGYDSG
     QGNGIQDLVK AANDLGIEVW REERSNLDIA KTSFDTTQKI LGFTDRGIVL FAPQLDNLLK
     KNPKIGNTLG SASSISQNIG KANTVLGGIQ SILGSVLSGV NLNELLQNKD PNQLELAKAG
     LELTNELVGN IASSVQTVDA FAEQISKLGS HLQNVKGLGG LSNKLQNLPD LGKASLGLDI
     ISGLLSGASA GLILADKKAS TEKKAAAGVE FANQIIGNVT KAVSSYILAQ RVASGLSSTG
     PVAALIASTV ALAVSPLSFL NVADKFKQAD LIKSYSERFQ KLGYDGDRLL ADFHRETGTI
     DASVTTINTA LAAISGGVGA ASAGSLVGAP VALLVAGVTG LITTILEYSK QAMFEHVANK
     VHDRIVEWEK KHNKNYFEQG YDSRHLADLQ DNMKFLINLN KELQAERVVA ITQQRWDNQI
     GDLAAISRRT DKISSGKAYV DAFEEGNTSP SIHPYSIDNK NGIINISNTN RKTQSVLFRT
     PLLTPGEENR ERIQEGKNSY ITKLHIQRVD SWTVTVGDAS SSVDFTNVVQ RIAVKFDDAG
     NIIESKDTKI IANLGAGNDN VFVGSSTTVI DGGDGHDRVH YSRGEYGALV IDATAETEKG
     SYSVKRYVGD SKALHETIAT HQTNVGNREE KIEYRREDDR FHTGYTVTDS LKSVEEIIGS
     QFNDIFKGSQ FDDVFHGGNG VDTIDGNDGD DHLFGGAGDD VIDGGNGNNF LVGGTGNDII
     SGGKDNDIYV HKTGDGNDSI TDSGGQDKLA FSDVNLKDLT FKKVDSSLEI INQKGEKVRI
     GNWFLEDDLA STVANYKATN DRKIEEIIGK GGERITSEQV DKLIKEGNNQ ISAEALSKVV
     NDYNTSKDRQ NVSNSLAKLI SSVGSFTSSS DFRNNLGTYV PSSIDVSNNI QLARAA