ID   LTXD_AGGAC              Reviewed;         477 AA.
AC   P18790;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Leukotoxin export protein LtxD;
GN   Name=ltxD {ECO:0000303|PubMed:8300209};
GN   Synonyms=AaLtd {ECO:0000303|PubMed:1961107},
GN   lktD {ECO:0000303|PubMed:2402458};
OS   Aggregatibacter actinomycetemcomitans (Actinobacillus
OS   actinomycetemcomitans) (Haemophilus actinomycetemcomitans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Aggregatibacter.
OX   NCBI_TaxID=714;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=JP2;
RX   PubMed=2402458; DOI=10.1093/nar/18.17.5292;
RA   Guthmiller J.M., Kraig E., Cagle M.P., Kolodrubetz D.;
RT   "Sequence of the lktD gene from Actinobacillus actinomycetemcomitans.";
RL   Nucleic Acids Res. 18:5292-5292(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1961107; DOI=10.1016/0882-4010(91)90004-t;
RA   Lally E.T., Golub E.E., Kieba I.R., Taichman N.S., Decker S., Berthold P.,
RA   Gibson C.W., Demuth D.R., Rosenbloom J.;
RT   "Structure and function of the B and D genes of the Actinobacillus
RT   actinomycetemcomitans leukotoxin complex.";
RL   Microb. Pathog. 11:111-121(1991).
RN   [3]
RP   INDUCTION, AND GENE NAME.
RC   STRAIN=652, and JP2;
RX   PubMed=8300209; DOI=10.1128/iai.62.2.501-508.1994;
RA   Brogan J.M., Lally E.T., Poulsen K., Kilian M., Demuth D.R.;
RT   "Regulation of Actinobacillus actinomycetemcomitans leukotoxin expression:
RT   analysis of the promoter regions of leukotoxic and minimally leukotoxic
RT   strains.";
RL   Infect. Immun. 62:501-508(1994).
RN   [4]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=7476096; DOI=10.1006/mpat.1995.0028;
RA   Guthmiller J.M., Kolodrubetz D., Kraig E.;
RT   "Mutational analysis of the putative leukotoxin transport genes in
RT   Actinobacillus actinomycetemcomitans.";
RL   Microb. Pathog. 18:307-321(1995).
RN   [5]
RP   SUBUNIT.
RC   STRAIN=IDH781;
RX   PubMed=17116373; DOI=10.1016/j.gene.2006.10.004;
RA   Crosby J.A., Kachlany S.C.;
RT   "TdeA, a TolC-like protein required for toxin and drug export in
RT   Aggregatibacter (Actinobacillus) actinomycetemcomitans.";
RL   Gene 388:83-92(2007).
CC   -!- FUNCTION: Involved in the export of the LtxA leukotoxin.
CC       {ECO:0000303|PubMed:7476096}.
CC   -!- SUBUNIT: Probably part of a complex composed of LtxB, LtxD and TdeA,
CC       which forms a single transport channel across the two membranes.
CC       {ECO:0000303|PubMed:17116373}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Single-pass
CC       membrane protein {ECO:0000255}.
CC   -!- INDUCTION: Levels of toxin expression vary greatly among strains.
CC       Highly leukotoxic strains (JP2-type strains) produce more LtxA protein
CC       and ltx mRNA than minimally leukotoxic strains (652-type strains).
CC       Variations are probably due to different types of promoters.
CC       {ECO:0000269|PubMed:8300209}.
CC   -!- DISRUPTION PHENOTYPE: Mutation has no effect on the levels of
CC       leukotoxin mRNA, but mutants have significantly less total leukotoxin
CC       than the parent strain. {ECO:0000269|PubMed:7476096}.
CC   -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1)
CC       family. {ECO:0000305}.
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DR   EMBL; X53956; CAA37907.1; -; Genomic_DNA.
DR   PIR; B61378; B61378.
DR   RefSeq; WP_025298516.1; NZ_CP065604.1.
DR   AlphaFoldDB; P18790; -.
DR   SMR; P18790; -.
DR   STRING; 714.ACT75_09615; -.
DR   TCDB; 8.A.1.3.4; the membrane fusion protein (mfp) family.
DR   eggNOG; COG0845; Bacteria.
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:0009306; P:protein secretion; IEA:InterPro.
DR   InterPro; IPR006144; Secretion_HlyD_CS.
DR   InterPro; IPR010129; T1SS_HlyD.
DR   TIGRFAMs; TIGR01843; type_I_hlyD; 1.
DR   PROSITE; PS00543; HLYD_FAMILY; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Coiled coil; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..477
FT                   /note="Leukotoxin export protein LtxD"
FT                   /id="PRO_0000201875"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   COILED          206..287
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   477 AA;  54651 MW;  54F20128CADE6260 CRC64;
     MKTWLLALYD VLSRYKNVWN ETWKIRKQLD SPVREKDENE FLPAHLELIE TPVSNAPRFV
     SYSIMLFLTL AIIVSIFSNV EIIATASGKF ALSGRSKEIK PIENSLVKHI FVKEGEYVKK
     GELLLKLTAL GAEADTLKTK TSLSQAKLEE FRYKSLLEAV EKDQLPILDF SKIDLPFMTE
     NDQKRVTLLI EEQFSTWQKQ RHQKTLNLNK KEAEKLSYLA RIKKYEGLIN TEQVRLDDFR
     ALYKEHAIAK HTVLDEENKY QDAINELEVY KASLMQVENE VLLAKEEQEL VTQLFKNDIL
     DKLKQATDNV NLLTFELDKN NQRQQVSEIR APVSGTVQQL KVHTIDGVVT TAETLMVVVP
     EEDSLEVTAL IQNKDIGFVK EGQEVVIKVE AFPYTRYGYL TGKVKNITLD AIEHPKLGLV
     FNTIIELDKK TLSTEEKEIP LSAGMEITAE IKTGMRSVIS YLLSPLEESI DKSLRER