LKTB_PASSP
ID LKTB_PASSP Reviewed; 708 AA.
AC P55122;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Leukotoxin translocation ATP-binding protein LktB;
DE EC=7.4.2.5;
GN Name=lktB;
OS Pasteurella haemolytica-like sp. (strain 5943B).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Mannheimia.
OX NCBI_TaxID=53500;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8478098; DOI=10.1128/iai.61.5.2089-2095.1993;
RA Chang Y.-F., Ma D.-P., Shi J., Chengappa M.M.;
RT "Molecular characterization of a leukotoxin gene from a Pasteurella
RT haemolytica-like organism, encoding a new member of the RTX toxin family.";
RL Infect. Immun. 61:2089-2095(1993).
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; L12148; AAA16445.1; -; Genomic_DNA.
DR AlphaFoldDB; P55122; -.
DR SMR; P55122; -.
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_0000092387"
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; 79772 MW; 7326D21411B5090A CRC64;
MEVNHQSNDL GLVALKMLAQ YHNIPLNPEE IKHKFDIEGK GLTLTSWLLA AKSLELKAKH
IKKEISRLHL VNLPALVWQD NGKHFLLVKI DTDKKRYLTY NLEQDAPKIL SQEEFESCYQ
GKIILVTSRA SIVGQLAKFD FTWFIPAVIK YRKIFLETLL VSIFLQIFAL ITPLFFQVVM
DKVLVHRGFS TLNIITVALA IVIIFEIVLS GLRTYIFAHS TSRIDVELGA RLFRHLLALP
ISYFENRRVG DTVARVRELD QIRNFLTGQA LTSVLDLLFS FIFFAVMWYY SPKLTLVILG
SLPCYILWSI FISPILRRRL DDKFARGADN QAFLVESVTA INMIKAMAVS PQMTDTWDKQ
LASYVSSSFR VTVLATIGQQ GVQLIQKTVM VINLWLGAHL VISGDLSIGQ LIAFNMLSGQ
VIAPVIRLAQ LWQDFTQVGI SVTRLGDVLN SPTEQYQGKL SLPEIQGDIA FKNIRFRYKP
DAPTILNNVN LEIKKGEVIG IVGRSGSGKS TLTKLLQRFY IPENGQVLID GHDLALADPN
WLRRQIGVVL QDNVLLNRSI RENIALSEPG MSMERVIYAA KLAGAHDFIS DVREGYNTIV
GEQGAGLSGG QRQRIAIARA LVNNPKILIF DEATSALDYE SEHIIMQNMQ KICQGRTVIL
IAHRLSTVKN ADRIIVMEKG EIVEQGKHNE LLQNNNGLYS YLHQLQLN
