ID   RTX2A_ACTPL             Reviewed;         956 AA.
AC   P15377;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=RTX-II toxin determinant A;
DE   AltName: Full=APX-IIA;
DE   AltName: Full=Cytolysin IIA;
DE            Short=CLY-IIA;
DE   AltName: Full=Hemolysin IIA;
DE            Short=HLY-IIA;
GN   Name=apxIIA; Synonyms=appA, clyIIA, cytC, hlyIIA;
OS   Actinobacillus pleuropneumoniae (Haemophilus pleuropneumoniae).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=715;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Serotype 5;
RX   PubMed=2693022; DOI=10.1089/dna.1.1989.8.635;
RA   Chang Y.-F., Young R., Struck D.K.;
RT   "Cloning and characterization of a hemolysin gene from Actinobacillus
RT   (Haemophilus) pleuropneumoniae.";
RL   DNA 8:635-647(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Isolate CVI 13261 / Serotype 9;
RX   PubMed=1937809; DOI=10.1128/iai.59.12.4497-4504.1991;
RA   Smits M.A., Briaire J., Jansen R., Smith H.E., Kamp E.M., Gielkens A.L.J.;
RT   "Cytolysins of Actinobacillus pleuropneumoniae serotype 9.";
RL   Infect. Immun. 59:4497-4504(1991).
CC   -!- FUNCTION: One of the virulence factors of A.pleuropneumoniae, which
CC       shows a weak hemolytic activity and is moderately cytotoxic for
CC       alveolar macrophages and neutrophils.
CC   -!- SUBCELLULAR LOCATION: Secreted. Host cell membrane {ECO:0000305};
CC       Multi-pass membrane protein {ECO:0000305}.
CC   -!- DOMAIN: The Gly-rich region is probably involved in binding calcium,
CC       which is required for target cell-binding or cytolytic activity.
CC       {ECO:0000250}.
CC   -!- DOMAIN: The three transmembrane domains are believed to be involved in
CC       pore formation by the cytotoxin. {ECO:0000250}.
CC   -!- PTM: Palmitoylated by ApxIIC. The toxin only becomes active when
CC       modified (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RTX prokaryotic toxin (TC 1.C.11) family.
CC       {ECO:0000305}.
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DR   EMBL; M30602; AAA87232.1; -; Genomic_DNA.
DR   EMBL; X61111; CAA43423.1; -; Genomic_DNA.
DR   PIR; B33389; B33389.
DR   RefSeq; WP_005597652.1; NZ_LS483358.1.
DR   AlphaFoldDB; P15377; -.
DR   SMR; P15377; -.
DR   STRING; 228399.appser1_10640; -.
DR   TCDB; 1.C.11.1.2; the pore-forming rtx toxin (rtx-toxin) family.
DR   GeneID; 66259876; -.
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; Palmitate; Repeat; Secreted; Toxin; Transmembrane;
KW   Transmembrane helix; Virulence.
FT   CHAIN           1..956
FT                   /note="RTX-II toxin determinant A"
FT                   /id="PRO_0000196239"
FT   TRANSMEM        233..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        266..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        361..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;  102532 MW;  BDBCABBADF14A641 CRC64;
     MSKITLSSLK SSLQQGLKNG KNKLNQAGTT LKNGLTQTGH SLQNGAKKLI LYIPQGYDSG
     QGNGVQDLVK AANDLGIEVW REERSNLDIA KTSFDTTQKI LGFTDRGIVL FAPQLDNLLK
     KNPKIGNTLG SASSISQNIG KANTVLGGIQ SILGSVLSGV NLNELLQNKD PNQLELAKAG
     LELTNELVGN IASSVQTVDA FAEQISKLGS HLQNVKGLGG LSNKLQNLPD LGKASLGLDI
     ISGLLSGASA GLILADKEAS TEKKAAAGVE FANQIIGNVT KAVSSYILAQ RVASGLSSTG
     PVAALIASTV ALAVSPLSFL NVADKFKQAD LIKSYSERFQ KLGYDGDRLL ADFHRETGTI
     DASVTTINTA LAAISGGVGA ASAGSLVGAP VALLVAGVTG LITTILEYSK QAMFEHVANK
     VHDRIVEWEK KHNKNYFEQG YDSRHLADLQ DNMKFLINLN KELQAERVVA ITQQRWDNQI
     GDLAAISRRT DKISSGKAYV DAFEEGQHQS YDSSVQLDNK NGIINISNTN RKTQSVLFRT
     PLLTPGEENR ERIQEGKNSY ITKLHIQRVD SWTVTDGDAS 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