ID   RTX3B_ACTPL             Reviewed;         711 AA.
AC   Q04473;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Toxin RTX-III translocation ATP-binding protein;
DE   AltName: Full=APX-IIIB;
DE   AltName: Full=Cytolysin IIIB;
DE            Short=CLY-IIIB;
DE   AltName: Full=RTX-III toxin determinant B;
GN   Name=apxIIIB; Synonyms=clyIIIB, rtxB;
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].
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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
RC   STRAIN=405 / 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: Involved in the transport of the toxin RTX-III.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- MISCELLANEOUS: The sequence shown is that of serotype 2.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Protein-1
CC       exporter (TC 3.A.1.109) family. {ECO:0000305}.
CC   -!- CAUTION: Tyr-13 is present instead of the conserved Cys which is
CC       expected to be the active site residue of peptidase C39. Thus they are
CC       presumed to be without peptidase activity. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA48712.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L12145; AAA21925.1; -; Genomic_DNA.
DR   EMBL; X80055; CAA56359.1; -; Genomic_DNA.
DR   EMBL; X68815; CAA48712.1; ALT_INIT; Genomic_DNA.
DR   PIR; S51785; C49219.
DR   AlphaFoldDB; Q04473; -.
DR   SMR; Q04473; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030256; C:type I protein secretion system complex; IEA:InterPro.
DR   GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0030253; P:protein secretion by the type I secretion system; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd02417; Peptidase_C39_likeA; 1.
DR   Gene3D; 1.20.1560.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011527; ABC1_TM_dom.
DR   InterPro; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR010132; ATPase_T1SS_HlyB.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005074; Peptidase_C39.
DR   InterPro; IPR039395; Peptidase_C39-like_A.
DR   InterPro; IPR039421; Type_1_exporter.
DR   PANTHER; PTHR24221; PTHR24221; 1.
DR   Pfam; PF00664; ABC_membrane; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF03412; Peptidase_C39; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF90123; SSF90123; 1.
DR   TIGRFAMs; TIGR01846; type_I_sec_HlyB; 1.
DR   PROSITE; PS50929; ABC_TM1F; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS50990; PEPTIDASE_C39; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Cytolysis; Membrane; Nucleotide-binding;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..711
FT                   /note="Toxin RTX-III translocation ATP-binding protein"
FT                   /id="PRO_0000092391"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        195..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        273..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        299..319
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        392..412
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          1..129
FT                   /note="Peptidase C39"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00362"
FT   DOMAIN          158..440
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          472..707
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00362,
FT                   ECO:0000255|PROSITE-ProRule:PRU00434"
FT   ACT_SITE        87
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00362"
FT   BINDING         506..513
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00362,
FT                   ECO:0000255|PROSITE-ProRule:PRU00434"
FT   VARIANT         61
FT                   /note="M -> A (in serotype 8)"
FT   VARIANT         91
FT                   /note="M -> T (in serotype 8)"
FT   VARIANT         125..126
FT                   /note="GM -> DV (in serotype 8)"
FT   VARIANT         213
FT                   /note="S -> N (in serotype 8)"
FT   VARIANT         416
FT                   /note="T -> A (in serotype 8)"
FT   VARIANT         469
FT                   /note="F -> K (in serotype 8)"
FT   VARIANT         606
FT                   /note="L -> Q (in serotype 8)"
FT   VARIANT         638
FT                   /note="S -> R (in serotype 8)"
SQ   SEQUENCE   711 AA;  80406 MW;  5B8E46B889D12D92 CRC64;
     MESQMPFNEK IDYGLHALVI LAQYHNVAVN PEEVKHKFDL DGKGLDLVAW LLAAKSLELK
     MKRVKKSIER LPFIHLPALI WRDDGQHVIL MKIDTQTNRY LIFDLEERNP KVLSAAEFHE
     IFQGGMILIT SRASIMGQLA KFDFTWFIPA VIKYRKIFVE TIIVSIFLQL FALITPLFFQ
     VVMDKVLVHR GFSTLNVITV ALSVVVIFEI VLSGLRTYIF SHSTSRIDVE LGAKLFRHLL
     ALPISYFENR RVGDTVARVR ELDQIRNFLT GQALTSVLDL LFSFIFFAVM WYYSPKLTIV
     ILLSLPCYIA WSIFISPILR RRLDEKFARN ADNQSFLVES VSAIDTIKAL AVTPQMTNIW
     DKQLASYVSA DFRVTVLATI GQQGVQLIQK TVMIINLWLG AHLVISGDLS IGQLITFNML
     SGQVIAPVVR LAQLWQDFQQ VGISITRLGD VLNSPTENYQ GKLSLPEIFG DIAFKHIRFR
     YKPDAPIILD DVNLSVKQGE VIGIVGRSGS GKSTLTKLLQ RFYIPENGQV LIDGHDLALA
     DPNWLRRQIG VVLQDNVLLN RSIRDNIALT DPSMSMERVI YAAKLAGAHD FISELREGYN
     TIVGELGAGL SGGQRQRIAI ARALVNNPRI LIFDEATSAL DYESEHIIMQ NMQKICHGRT
     VIIIAHRLST VKNADRIIVM EKGHIVEQGK HNQLLENENG LYYYLNQLQS N