LTXB_AGGAC
ID LTXB_AGGAC Reviewed; 707 AA.
AC P23702;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Leukotoxin export ATP-binding protein LtxB;
DE EC=7.4.2.5 {ECO:0000250};
GN Name=ltxB {ECO:0000303|PubMed:8300209};
GN Synonyms=AaLtb {ECO:0000303|PubMed:1961107},
GN lktB {ECO:0000303|PubMed:2402457};
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].
RX PubMed=2402457; DOI=10.1093/nar/18.17.5291;
RA Guthmiller J.M., Kolodrubetz D., Cagle M.P., Kraig E.;
RT "Sequence of the lktB gene from Actinobacillus actinomycetemcomitans.";
RL Nucleic Acids Res. 18:5291-5291(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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + proteinSide 1 = ADP + phosphate + proteinSide 2.;
CC EC=7.4.2.5; Evidence={ECO:0000250};
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}; Multi-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 ABC transporter superfamily. Protein-1
CC exporter (TC 3.A.1.109) family. {ECO:0000305}.
CC -!- CAUTION: Leu-9 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X53955; CAA37906.1; -; Genomic_DNA.
DR PIR; A61378; A61378.
DR RefSeq; WP_025298517.1; NZ_CP065604.1.
DR AlphaFoldDB; P23702; -.
DR SMR; P23702; -.
DR STRING; 714.ACT75_09610; -.
DR TCDB; 3.A.1.109.8; the atp-binding cassette (abc) superfamily.
DR eggNOG; COG2274; 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:0030256; C:type I protein secretion system complex; IEA:InterPro.
DR GO; GO:0015440; F:ABC-type peptide transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0015462; F:ABC-type protein transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IEA:InterPro.
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 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..707
FT /note="Leukotoxin export ATP-binding protein LtxB"
FT /id="PRO_0000092377"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 4..125
FT /note="Peptidase C39"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00362"
FT DOMAIN 158..436
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 468..703
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT ACT_SITE 83
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00362"
FT BINDING 502..509
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 707 AA; 79579 MW; CA564EACF46DF4FB CRC64;
MDSQKNTNLA LQALEVLAQY HNISINPEEI KHKFDIDGHG LNQTKWLLAA KSLGLKVRTA
NKTVDRLPFL HLPALAWRDD GEHFILLKID QETDRYLIFD LIQKNPIVLD KNEFEERYQS
KVILIASRAS IVGNLAKFDF TWFIPAVIKY RKIFIETLIV SIFLQIFALI TPLFFQVVMD
KVLVHRGFST LNVITVALAI VVLFEIILGG LRTYVFAHST SRIDVELGAR LFRHLLALPI
SYFEARRVGD TVARVRELDQ IRNFLTGQAL TSILDLLFSF IFFAVMWYYS PKLTLVVLGS
LPCYVIWSVF ISPILRRRLD DKFARNADNQ SFLVESVTAI NTIKAMAISP QMTNIWDKQL
ASYVAVSFKV TVLATIGQQG IQLIQKAVMV INLWLGAHLV ISGDLSIGQL IAFNMLAGQI
ISPVIRLAQI WQDFQQVGIS VTRLGDVLNS PTENNTASVS LPEIQGEISF RNIKFRYKPD
SPMILNNINL DISQGEVIGI VGRSGSGKST LTKLIQRFYI PEQGQVLIDG HDLALADPNW
LRRQVGVVLQ DNVLLNRSIR ENIALTNPGM PMEKVIAAAK LAGAHDFISE LREGYNTVVG
EQGAGLSGGQ RQRIAIARAL VNNPRILIFD EATSALDYES ENIIMHNMHK ICQNRTVLII
AHRLSTVKNA DRIIVMDKGE IIEQGKHQEL LKDEKGLYSY LHQLQVN
