RTX11_ACTPL
ID RTX11_ACTPL Reviewed; 1023 AA.
AC P55128;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=RTX-I toxin determinant A from serotypes 1/9;
DE AltName: Full=APX-IA;
DE AltName: Full=ApxI;
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=ATCC 27088 / DSM 13472 / CCM 5869 / S4074 / Serotype 1;
RX PubMed=1879928; DOI=10.1128/iai.59.9.3026-3032.1991;
RA Frey J., Meier R., Gygi D., Nicolet J.;
RT "Nucleotide sequence of the hemolysin I gene from Actinobacillus
RT pleuropneumoniae.";
RL Infect. Immun. 59:3026-3032(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 27088 / DSM 13472 / CCM 5869 / S4074 / Serotype 1;
RX PubMed=8181764; DOI=10.1016/0378-1119(94)90361-1;
RA Frey J., Haldimann A., Nicolet J., Boffini A., Prentki P.;
RT "Sequence analysis and transcription of the apxI operon (hemolysin I) from
RT Actinobacillus pleuropneumoniae.";
RL Gene 142:97-102(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate CVI 13261 / Serotype 9;
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 27088 / DSM 13472 / CCM 5869 / S4074 / Serotype 1;
RA Chang Y., Wang Y., Chin N.;
RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 604-685, AND CHARACTERIZATION IN VIVO.
RC STRAIN=CM5 / Serotype 1;
RX PubMed=7830567; DOI=10.1111/j.1365-2958.1994.tb01282.x;
RA Tascon R.I., Vazquez-Boland J.A., Gutierrez-Martin C.B.,
RA Rodriguez-Barbosa I., Rodriguez-Ferri E.F.;
RT "The RTX haemolysins ApxI and ApxII are major virulence factors of the
RT swine pathogen Actinobacillus pleuropneumoniae: evidence from mutational
RT analysis.";
RL Mol. Microbiol. 14:207-216(1994).
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 1.
CC -!- MISCELLANEOUS: In strain CM15 (serotype 1), disruption of this gene
CC results in production of only RTX-II toxin, and a weak hemolytic
CC activity in mice and pigs.
CC -!- SIMILARITY: Belongs to the RTX prokaryotic toxin (TC 1.C.11) family.
CC {ECO:0000305}.
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DR EMBL; X52899; CAA37081.1; -; Genomic_DNA.
DR EMBL; X68595; CAA48586.1; -; Genomic_DNA.
DR EMBL; X73117; CAA51548.1; -; Genomic_DNA.
DR EMBL; U05042; AAB05034.1; -; Genomic_DNA.
DR PIR; I39643; I39643.
DR RefSeq; WP_005598583.1; NZ_CP030753.1.
DR AlphaFoldDB; P55128; -.
DR SMR; P55128; -.
DR STRING; 228399.appser1_15240; -.
DR GeneID; 66258126; -.
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 1: Evidence at protein level;
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 1/9"
FT /id="PRO_0000196237"
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. 3 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="R -> A (in Ref. 3 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 562
FT /note="Q -> E (in Ref. 3 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 687..688
FT /note="TC -> R (in Ref. 3 and 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1023 AA; 110194 MW; F99A88CFC9F1A598 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 LSARSAGVGA AATGSLVGAP VAALVSAITG IISGILDASK QAIFERVATK
LANKIDEWEK KHGKNYFENG YDARHSAFLE DTFELLSQYN KEYSVERVVA ITQQRWDVNI
GELAGITRKG SDTKSGKAYV DFFEEGKLLE KEPDRFDKKV FDPLEGKIDL SSINKTTLLK
FVTPVFTAGE EIRERKQTGK YQYMTELFVK GKEKWVVTGV QSHNAIYDYT 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 ISSTGAFTGD HGKVSVGSGG PLVYNNSANN VANSLSYSLA
QAA
