ID   RTX32_ACTPL             Reviewed;        1052 AA.
AC   P55131;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=RTX-III toxin determinant A from serotype 8;
DE   AltName: Full=APX-IIIA;
DE   AltName: Full=Cytolysin IIIA;
DE            Short=CLY-IIIA;
GN   Name=apxIIIA; Synonyms=clyIIIA, ptxA, rtxA;
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=405 / Serotype 8;
RX   PubMed=7927703; DOI=10.1128/iai.62.10.4411-4418.1994;
RA   Jansen R., Briaire J., van Geel A.B.M., Kamp E.M., Gielkens A.L.J.,
RA   Smits M.A.;
RT   "Genetic map of the Actinobacillus pleuropneumoniae RTX-toxin (Apx)
RT   operons: characterization of the ApxIII operons.";
RL   Infect. Immun. 62:4411-4418(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Serotype 8;
RX   PubMed=8432615; DOI=10.1128/iai.61.3.947-954.1993;
RA   Jansen R., Briaire J., Kamp E.M., Gielkens A.L.J., Smits M.A.;
RT   "Cloning and characterization of the Actinobacillus pleuropneumoniae-RTX-
RT   toxin III (ApxIII) gene.";
RL   Infect. Immun. 61:947-954(1993).
CC   -!- FUNCTION: Does not have hemolytic activity but shows a strong
CC       cytotoxicity towards 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 ApxIIIC. 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; X80055; CAA56358.1; -; Genomic_DNA.
DR   EMBL; X68815; CAA48711.1; -; Genomic_DNA.
DR   PIR; B49219; B49219.
DR   RefSeq; WP_005620396.1; NZ_UIFY01000002.1.
DR   AlphaFoldDB; P55131; -.
DR   SMR; P55131; -.
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:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.150.10.10; -; 2.
DR   InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
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; 3.
PE   3: Inferred from homology;
KW   Calcium; Cytolysis; Host cell membrane; Host membrane; Lipoprotein;
KW   Membrane; Palmitate; Repeat; Secreted; Toxin; Transmembrane;
KW   Transmembrane helix; Virulence.
FT   CHAIN           1..1052
FT                   /note="RTX-III toxin determinant A from serotype 8"
FT                   /id="PRO_0000196241"
FT   TRANSMEM        248..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        275..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        372..418
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REPEAT          744..761
FT                   /note="Hemolysin-type calcium-binding 1"
FT   REPEAT          762..779
FT                   /note="Hemolysin-type calcium-binding 2"
FT   REPEAT          780..797
FT                   /note="Hemolysin-type calcium-binding 3"
FT   REPEAT          798..815
FT                   /note="Hemolysin-type calcium-binding 4"
FT   REPEAT          826..843
FT                   /note="Hemolysin-type calcium-binding 5"
FT   REPEAT          844..861
FT                   /note="Hemolysin-type calcium-binding 6"
SQ   SEQUENCE   1052 AA;  112810 MW;  F83AFE25A6FD8758 CRC64;
     MSTWSSMLAD LKKRAEEAKR QAKKGYDVTK NGLQYGVSQA KLQALAAGKA VQKYGNKLVL
     VIPKEYDGSV GNGFFDLVKA AEELGIQVKY VNRNELEVAH KSLGTADQFL GLTERGLTLF
     APQLDQFLQK HSKISNVVGS STGDAVSKLA KSQTIISGIQ SVLGTVLAGI NLNEAIISGG
     SELELAEAGV SLASELVSNI AKGTTTIDAF TTQIQNFGKL VENAKGLGGV GRQLQNISGS
     ALSKTGLGLD IISSLLSGVT ASFALANKNA STSTKVAAGF ELSNQVIGGI TKAVSSYILA
     QRLAAGLSTT GPAAALIASS ISLAISPLAF LRVADNFNRS KEIGEFAERF KKLGYDGDKL
     LSEFYHEAGT IDASITTIST ALSAIAAGTA AASAGALVGA PITLLVTGIT GLISGILEFS
     KQPMLDHVAS KIGNKIDEWE KKYGKNYFEN GYDARHKAFL EDSFSLLSSF NKQYETERAV
     LITQQRWDEY IGELAGITGK GDKLSSGKAY VDYFQEGKLL EKKPDDFSKV VFDPTKGEID
     ISNSQTSTLL KFVTPLLTPG TESRERTQTG KYEYITKLVV KGKDKWVVNG VKDKGAVYDY
     TNLIQHAHIS SSVARGEEYR EVRLVSHLGN GNDKVFLAAG SAEIHAGEGH DVVYYDKTDT
     GLLVIDGTKA TEQGRYSVTR ELSGATKILR EVIKNQKSAV GKREETLEYR DYELTQSGNS
     NLKAHDELHS VEEIIGSNQR DEFKGSKFRD IFHGADGDDL LNGNDGDDIL YGDKGNDELR
     GDNGNDQLYG GEGNDKLLGG NGNNYLSGGD GNDELQVLGN GFNVLRGGKG DDKLYGSSGS
     DLLDGGEGND YLEGGDGSDF YVYRSTSGNH TIYDQGKSSD LDKLYLSDFS FDRLLVEKVD
     DNLVLRSNES SHNNGVLTIK DWFKEGNKYN HKIEQIVDKN GRKLTAENLG TYFKNAPKAD
     NLLNYATKED QNESNLSSLK TELSKIITNA GNFGVAKQGN TGINTAALNN EVNKIISSAN
     TFATSQLGGS GMGTLPSTNV NSMMLGNLAR AA