RTX31_ACTPL
ID RTX31_ACTPL Reviewed; 1049 AA.
AC P55130;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=RTX-III toxin determinant A from serotype 2;
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=Serotype 2;
RX PubMed=8494611; DOI=10.1089/dna.1993.12.351;
RA Chang Y.-F., Shi J., Ma D.-P., Shin S.J., Lein D.H.;
RT "Molecular analysis of the Actinobacillus pleuropneumoniae RTX toxin-III
RT gene cluster.";
RL DNA Cell Biol. 12:351-362(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 828-1049.
RC STRAIN=1536 / Serotype 2;
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).
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; L12145; AAA21924.1; -; Genomic_DNA.
DR EMBL; X80056; CAB37652.1; ALT_SEQ; Genomic_DNA.
DR PIR; S51784; S51784.
DR AlphaFoldDB; P55130; -.
DR SMR; P55130; -.
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..1049
FT /note="RTX-III toxin determinant A from serotype 2"
FT /id="PRO_0000196240"
FT TRANSMEM 154..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 397..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 743..760
FT /note="Hemolysin-type calcium-binding 1"
FT REPEAT 761..778
FT /note="Hemolysin-type calcium-binding 2"
FT REPEAT 779..796
FT /note="Hemolysin-type calcium-binding 3"
FT REPEAT 797..814
FT /note="Hemolysin-type calcium-binding 4"
FT REPEAT 825..842
FT /note="Hemolysin-type calcium-binding 5"
FT REPEAT 843..860
FT /note="Hemolysin-type calcium-binding 6"
SQ SEQUENCE 1049 AA; 112491 MW; F99846BFD4E5CE72 CRC64;
MSTWSSMLAD LKKRAEEAKR QVKKGYDVTK NGLQYGVSQA KLQALAAGKA VQKYGNKLVL
VIPKEYDGSV GNGFFDLVKA AEELGIQVKY VNRNELEVAH KSLGTADQFL GLTERGLTLF
APQLDQFLQK HSKISNVVGS STGDAVSKLA KSQTIISGIQ SVLGTVLAGI NLNEAIISGG
SELELAEAGV SLASELVSNI AKGTTTIDAF TTQIQNFGKL AENAKGLGGV GRQLQNISGS
ALSKTGLGLD IISSLLSGVT RSFALRNKNA STSTKVAAGF ELSNQVIGGI TKAVSSYILA
QRLRAGLSTT 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 EVIKNQKYAV GKREETLEYR DYELTQSGNS
NLKAHDELHS VEEIGSNQRD EFKGSKFRDI FHGADGDDLL NGNDGDDILY GDKGNDELRG
DNGNDQLYGG EGDDKLLGGN GNNYLSGGDG NDELQVLGNG FNVLRGGKGD DKLYGSSGSD
LLDGGEGNDY LEGGDGSDFY VYRSTSGNHT IYDQGKASDS DKLYLSDLSF DNILVKRVND
NLEFRSNNNS NSGVLTIKDW FKGGNSYNHK IEQIVDKNGR KLTAGNLGNN FHDTQQASSL
LKNVTQEQNE SNLSSLKTEL GKIITNAGNF GVAKQGNTGI NTAALNNEVN KIISSANTFA
TSQLGGSGMG TLPSTNVNSM MLGNLARAA
