LKB1B_MANHA
ID LKB1B_MANHA Reviewed; 708 AA.
AC Q93FH6;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 103.
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 A1 / PH2;
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; AF314503; AAL12767.1; -; Genomic_DNA.
DR RefSeq; WP_006248024.1; NZ_VAJK01000035.1.
DR AlphaFoldDB; Q93FH6; -.
DR SMR; Q93FH6; -.
DR STRING; 75985.WC39_13375; -.
DR GeneID; 67370329; -.
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_0000092380"
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"
SQ SEQUENCE 708 AA; 79697 MW; 2D6FA9AF15A7FFD1 CRC64;
MEANHQRNDL GLVALTMLAQ YHNISLNPEE IKHKFDLDGK GLSLTAWLLA 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 SLPEIKGDIS FKNIRFRYKP
DAPTILNNVN LEIRQGEVIG IVGRSGSGKS TLTKLLQRFY IPENGQVLID GHDLALADPN
WLRRQIGVVL QDNVLLNRSI RENIALSDPG MPMERVIYAA KLAGAHDFIS ELREGYNTIV
GEQGAGLSGG QRQRIAIARA LVNNPKILIF DEATSALDYE SEHIIMQNMQ KICQGRTVIL
IAHRLSTVKN ADRIIVMEKG EIVEQGKHHE LLQNSNGLYS YLHQLQLN
