RTX12_ACTPL
ID RTX12_ACTPL Reviewed; 1023 AA.
AC P55129;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=RTX-I toxin determinant A from serotypes 5/10;
DE AltName: Full=APX-IA;
DE AltName: Full=Cytolysin IA;
DE Short=CLY-IA;
DE AltName: Full=Hemolysin IA;
DE Short=HLY-IA;
GN Name=apxIA; Synonyms=clyIA, hlyIA;
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=13039 / Serotype 10;
RX PubMed=8007819; DOI=10.1006/mpat.1993.1096;
RA Nagai S., Yagihashi T., Ishihama A.;
RT "DNA sequence analysis of an allelic variant of the Actinobacillus
RT pleuropneumoniae-RTX-toxin I (ApxIA) from serotype 10.";
RL Microb. Pathog. 15:485-495(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K17 / Serotype 5;
RX PubMed=8807793; DOI=10.1111/j.1574-6968.1996.tb08452.x;
RA Chin N., Frey J., Chang C.F., Chang Y.F.;
RT "Identification of a locus involved in the utilization of iron by
RT Actinobacillus pleuropneumoniae.";
RL FEMS Microbiol. Lett. 143:1-6(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 886-1023.
RC STRAIN=K17 / Serotype 5;
RX PubMed=8359891; DOI=10.1128/iai.61.9.3688-3695.1993;
RA Jansen R., Briaire J., Kamp E.M., Gielkens A.L.J., Smits M.A.;
RT "Structural analysis of the Actinobacillus pleuropneumoniae-RTX-toxin I
RT (ApxI) operon.";
RL Infect. Immun. 61:3688-3695(1993).
CC -!- FUNCTION: One of the virulence factors of A.pleuropneumoniae, which has
CC a strong hemolytic activity and is cytotoxic for alveolar macrophages
CC 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 -!- DOMAIN: The three transmembrane domains are believed to be involved in
CC pore formation by the cytotoxin. {ECO:0000250}.
CC -!- PTM: Palmitoylated by ApxIC. The toxin only becomes active when
CC modified (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: ApxIA is partially deleted in serotypes 2, 4, 6, 7, 8,
CC 12, and totally deleted in serotype 3.
CC -!- MISCELLANEOUS: The sequence shown is that of serotype 10.
CC -!- SIMILARITY: Belongs to the RTX prokaryotic toxin (TC 1.C.11) family.
CC {ECO:0000305}.
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DR EMBL; D16582; BAA04014.1; -; Genomic_DNA.
DR EMBL; U04954; AAB17220.1; -; Genomic_DNA.
DR EMBL; X73116; CAA51546.1; -; Genomic_DNA.
DR PIR; I39641; I39641.
DR AlphaFoldDB; P55129; -.
DR SMR; P55129; -.
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; -; 3.
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; 4.
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; 2.
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..1023
FT /note="RTX-I toxin determinant A from serotypes 5/10"
FT /id="PRO_0000196238"
FT TRANSMEM 226..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 730..747
FT /note="Hemolysin-type calcium-binding 1"
FT REPEAT 748..765
FT /note="Hemolysin-type calcium-binding 2"
FT REPEAT 766..783
FT /note="Hemolysin-type calcium-binding 3"
FT REPEAT 784..801
FT /note="Hemolysin-type calcium-binding 4"
FT REPEAT 812..829
FT /note="Hemolysin-type calcium-binding 5"
FT REPEAT 830..847
FT /note="Hemolysin-type calcium-binding 6"
FT CONFLICT 210..217
FT /note="AMPYLTLA -> GNALSNTR (in Ref. 2; AAB17220)"
FT /evidence="ECO:0000305"
FT CONFLICT 581
FT /note="E -> Q (in Ref. 2; AAB17220)"
FT /evidence="ECO:0000305"
FT CONFLICT 687..688
FT /note="TC -> R (in Ref. 2; AAB17220)"
FT /evidence="ECO:0000305"
FT CONFLICT 1015
FT /note="F -> L (in Ref. 2; AAB17220)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1023 AA; 110130 MW; 183C7C15EE57DB55 CRC64;
MANSQLDRVK GLIDSLNQHT KSAAKSGAGA LKNGLGQVKQ AGQKLILYIP KDYQASTGSS
LNDLVKAAEA LGIEVHRSEK NGTALAKELF GTTEKLLGFS ERGIALFAPQ FDKLLNKNQK
LSKSLGGSSE ALGQRLNKTQ TALSALQSFL GTAIAGMDLD SLLRRRRNGE DVSGSELAKA
GVDLAAQLVD NIASATGTVD AFAEQLGKLA MPYLTLALSG LASKLNNLPD LSLAGPGFDA
VSGILSVVSA SFILSNKDAD AGTKAAAGIE ISTKILGNIG KAVSQYIIAQ RVAAGLSTTA
ATGGLIGSVV ALAISPLSFL NVADKFERAK QLEQYSERFK KFGYEGDSLL ASFYRETGAI
EAALTTINSV LSAASAGVGA AATGSLVGAP VAALVSAITG IISGILDASK QAIFERVATK
LANKIDEWEK KHGKNYFENG YDARHSAFLE DTFELLSQYN KEYSVERVVA ITQQRWDVNI
GELAGITRKG ADAKSGKAYV DFFEEGKLLE KDPDRFDKKV FDPLEGKIDL SSINKTTLLK
FITPVFTAGE EIRERKQTGK YEYMTELFVK GKEKWVVTGV ESHNAIYDYT NLIQLAIDKK
GEKRQVTIES HLGEKNDRIY LSSGSSIVYA GNGHDVAYYD KTDTGYLTFD GQSAQKAGEY
IVTKELKADV KVLKEVVKTQ DISVGKTCSE KLEYRDYELS PFELGNGIRA KDELHSVEEI
IGSNRKDKFF GSRFTDIFHG AKGDDEIYGN DGHDILYGDD GNDVIHGGDG NDHLVGGNGN
DRLIGGKGNN FLNGGDGDDE LQVFEGQYNV LLGGAGNDIL YGSDGTNLFD GGVGNDKIYG
GLGKDIYRYS KEYGRHIIIE KGGDDDTLLL SDLSFKDVGF IRIGDDLLVN KRIGGTLYYH
EDYNGNALTI KDWFKEGKEG QNNKIEKIVD KDGAYVLSQY LTELTAPGRG INYFNGLEEK
LYYGEGYNAL PQLRKDIEQI ISSTGALTGE HGQVLVGAGG PLAYSNSPNS IPNAFSNYLT
QSA
