ID   LKB2B_MANHA             Reviewed;         708 AA.
AC   Q93FG6; Q934E0; Q93FG8;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Leukotoxin translocation ATP-binding protein LktB;
DE            EC=7.4.2.5;
GN   Name=lktB;
OS   Mannheimia haemolytica (Pasteurella haemolytica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Mannheimia.
OX   NCBI_TaxID=75985;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Serotype A2 / PH278, Serotype A2 / PH292, and Serotype A2 / PH494;
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; AF314511; AAL12782.1; -; Genomic_DNA.
DR   EMBL; AF314514; AAL12791.1; -; Genomic_DNA.
DR   EMBL; AF314515; AAL12794.1; -; Genomic_DNA.
DR   RefSeq; WP_020831006.1; NZ_VAIO01000006.1.
DR   RefSeq; WP_032844367.1; NZ_VAIL01000117.1.
DR   AlphaFoldDB; Q93FG6; -.
DR   SMR; Q93FG6; -.
DR   PATRIC; fig|75985.47.peg.432; -.
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_0000092382"
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         46
FT                   /note="S -> A (in strain: Serotype A2 / PH278 and Serotype
FT                   A2 / PH494)"
FT   VARIANT         65
FT                   /note="I -> V (in strain: Serotype A2 / PH494)"
FT   VARIANT         101
FT                   /note="N -> D (in strain: Serotype A2 / PH494)"
FT   VARIANT         104
FT                   /note="Q -> K (in strain: Serotype A2 / PH494)"
FT   VARIANT         322
FT                   /note="D -> E (in strain: Serotype A2 / PH278)"
FT   VARIANT         468
FT                   /note="Y -> D (in strain: Serotype A2 / PH278 and Serotype
FT                   A2 / PH494)"
FT   VARIANT         655
FT                   /note="G -> D (in strain: Serotype A2 / PH278)"
SQ   SEQUENCE   708 AA;  79747 MW;  BDEFB5B81ABD3C23 CRC64;
     MEANHQRNDL GLVALTMLAQ YHNISLNPEE IKHKFDLDGK 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 DDKFARSADN QAFLVESVTA INMIKAMAVA PQMTDTWDKQ
     LASYVSSSFR VTVLATIGQQ GVQLIQKTVM VINLWLGAHL VISGDLSIGQ LIAFNMLSGQ
     VIAPVIRLAQ LWQDFQQVGI SVTRLGDVLN SPTEQYQGKL SLPEIKGYIS FKNIRFRYKP
     DAPTILNNVN LEIRQGEVIG IVGRSGSGKS TLTKLLQRFY IPENGQVLID GHDLALADPN
     WLRRQIGVVL QDNVLLNRSI RENIALSDPG MPMERVIYAA KLAGAHDFIS ELREGYNTIV
     GEQGAGLSGG QRQRIAIARA LVNNPKILIF DEATSALDYE SEHIIMQNMQ KICQGRTVIL
     IAHRLSTVKN ADRIIVMEKG EIVEQGKHHE LLQNSNGLYS YLHQLQLN