RTX3D_ACTPL
ID RTX3D_ACTPL Reviewed; 477 AA.
AC Q08633;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=RTX-III toxin determinant D;
DE AltName: Full=APX-IIID;
DE AltName: Full=Cytolysin IIID;
DE Short=CLY-IIID;
DE AltName: Full=Toxin RTX-III secretion protein D;
GN Name=apxIIID; Synonyms=clyIIID, rtxD;
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).
CC -!- FUNCTION: Involved in the transport of the toxin RTX-III.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}.
CC -!- MISCELLANEOUS: The sequence shown is that of serotype 2.
CC -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1)
CC family. {ECO:0000305}.
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DR EMBL; L12145; AAA21926.1; -; Genomic_DNA.
DR EMBL; X80055; CAA56360.1; -; Genomic_DNA.
DR PIR; S48045; S48045.
DR RefSeq; WP_039709261.1; NZ_JSVZ01000019.1.
DR AlphaFoldDB; Q08633; -.
DR SMR; Q08633; -.
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:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0009306; P:protein secretion; IEA:InterPro.
DR InterPro; IPR039562; MFP_biotin_lipoyl_2.
DR InterPro; IPR006144; Secretion_HlyD_CS.
DR InterPro; IPR010129; T1SS_HlyD.
DR Pfam; PF13533; Biotin_lipoyl_2; 1.
DR TIGRFAMs; TIGR01843; type_I_hlyD; 1.
DR PROSITE; PS00543; HLYD_FAMILY; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Cytolysis; Membrane; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..477
FT /note="RTX-III toxin determinant D"
FT /id="PRO_0000201892"
FT TOPO_DOM 1..59
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..477
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT VARIANT 44
FT /note="R -> A (in strain: 405 / Serotype 8)"
FT VARIANT 132
FT /note="C -> A (in strain: 405 / Serotype 8)"
FT VARIANT 185..186
FT /note="GA -> NT (in strain: 405 / Serotype 8)"
FT VARIANT 376
FT /note="V -> I (in strain: 405 / Serotype 8)"
SQ SEQUENCE 477 AA; 54780 MW; D229F1CAB7D7E90A CRC64;
MKLWILGLGE FFQRYRNIWR EIWKIRKQLD TPARQKDENE FLPRHLELIE TPISKKPRLI
AYLIMLFLFL AIVISIISKV EIVASATGKL VFSGHSKEIK PIENALVKDI FVKDGQFVEK
GQLLLNLTAL GCDADKQKTK VSLGLERLDG YRYKSLLYSI EHNRLPLLDF NQADFDSVQE
EDKTGARHLI TEQFETWQKQ KYQKELAYQR KQAEKQTVLA NIRKYESASR IEKEKLSDLK
KLYDVKSISK HELLAQENRY VEASNELSVY QSHLKEVESD LLKAQEDLKL VTQLFKSDIL
EKLQQNIQRE KQLTLELEKN EQRQLASIIR APVSGTVQQL KTHTKGGVVT TAETLMVIAP
EDDVLEVSAL IQNKDVGFVE IGQEAVIKVE TFPYTRYGYL YGKVKTITLD AIEHPQLGLV
FNSIIEINKK TLTDGDKEIQ LGSGMSVIAE IKTGERSVIS FLLSPLEESI TESLRER
