ID   LKTB_MANGL              Reviewed;         708 AA.
AC   Q933I3; Q93FG2; Q93FG4; Q93FG5;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Leukotoxin translocation ATP-binding protein LktB;
DE            EC=7.4.2.5;
GN   Name=lktB;
OS   Mannheimia glucosida.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Mannheimia.
OX   NCBI_TaxID=85401;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Serotype A11 / PH240, Serotype A11 / PH344, Serotype A11 / PH498,
RC   Serotype UG3 / PH290, Serotype UG3 / PH496, and Serotype UG3 / PH574;
RX   PubMed=11741868; DOI=10.1128/jb.184.1.266-277.2002;
RA   Davies R.L., Campbell S., Whittam T.S.;
RT   "Mosaic structure and molecular evolution of the leukotoxin operon
RT   (lktCABD) in Mannheimia (Pasteurella) haemolytica, Mannheimia glucosida,
RT   and Pasteurella trehalosi.";
RL   J. Bacteriol. 184:266-277(2002).
CC   -!- FUNCTION: Part of the ABC transporter complex LktBD involved in
CC       leukotoxin export. Transmembrane domains (TMD) form a pore in the inner
CC       membrane and the ATP-binding domain (NBD) is responsible for energy
CC       generation (Probable). {ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + proteinSide 1 = ADP + phosphate + proteinSide 2.;
CC         EC=7.4.2.5;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}.
CC   -!- DOMAIN: In LktB the peptidase C39 domain, the ATP-binding domain (NBD)
CC       and the transmembrane domain (TMD) are fused.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Protein-1
CC       exporter (TC 3.A.1.109) family. {ECO:0000305}.
CC   -!- CAUTION: Leu-10 is present instead of the conserved Cys which is
CC       expected to be the active site residue of peptidase C39. Thus this
CC       protein is presumed to be without peptidase activity. {ECO:0000305}.
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DR   EMBL; AF314517; AAL12797.1; -; Genomic_DNA.
DR   EMBL; AF314518; AAL12800.1; -; Genomic_DNA.
DR   EMBL; AF314519; AAL12803.1; -; Genomic_DNA.
DR   EMBL; AF314520; AAL12806.1; -; Genomic_DNA.
DR   EMBL; AF314521; AAL12808.1; -; Genomic_DNA.
DR   EMBL; AF314522; AAL12811.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q933I3; -.
DR   SMR; Q933I3; -.
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: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 inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Translocase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..708
FT                   /note="Leukotoxin translocation ATP-binding protein LktB"
FT                   /id="PRO_0000092378"
FT   TRANSMEM        159..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        192..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        270..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        296..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        389..409
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          1..126
FT                   /note="Peptidase C39"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00362"
FT   DOMAIN          155..437
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          469..704
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00362,
FT                   ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         503..510
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00362,
FT                   ECO:0000255|PROSITE-ProRule:PRU00434"
FT   VARIANT         40
FT                   /note="N -> K (in strain: Serotype A11 / PH240 and Serotype
FT                   UG3 / PH496)"
FT   VARIANT         121
FT                   /note="G -> E (in strain: Serotype UG3 / PH496)"
FT   VARIANT         232
FT                   /note="L -> F (in strain: Serotype A11 / PH498)"
SQ   SEQUENCE   708 AA;  79659 MW;  844485AFD0AA11DC CRC64;
     MEANHQRNDL GLVALTMLAQ YHNISLNPEE IKHKFDLDGN GLSLTSWLLA AKSLALKAKH
     IKKEISRLHL VNLPALVWQD NGKHFLLVKV DTDNNRYLTY NLEQDAPQIL SQDEFEACYQ
     GQLILVTSRA SVVGQLAKFD FTWFIPAVIK YRKIFLETLI VSIFLQIFAL ITPLFFQVVM
     DKVLVHRGFS TLNIITVALA IVIIFEIVLS GLRTYVFSHS TSRIDVELGA KLFRHLLSLP
     ISYFENRRVG DTVARVRELD QIRNFLTGQA LTSVLDLLFS FIFFAVMWYY SPKLTLVILG
     SLPCYILWSI FISPILRRRL DEKFARSADN QAFLVESVTA INMIKAMAVA PQMTDTWDKQ
     LASYVSSSFR VTVLATIGQQ GVQLIQKTVM VINLWLGAHL VISGDLSIGQ LIAFNMLSGQ
     VIAPVIRLAQ LWQDFQQVGI SVTRLGDVLN SPTEQYQGKL SLPEIQGDIA FKNIRFRYKP
     DAPTILNNVN LEIKKGEVIG IVGRSGSGKS TLTKLLQRFY IPENGQVLID GHDLALADPN
     WLRRQIGVVL QDNVLLNRSI RENIALSEPG MSMERVIYAA KLAGAHDFIS ELREGYNTIV
     GEQGAGLSGG QRQRIAIARA LVNNPKILIF DEATSALDYE SEHIIMQNMQ KICQGRTVIL
     IAHRLSTVKN ADRIIVMEKG EIVEQGKHHE LLQNSNGLYS YLHQLQLN