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MSBA_LEGPA
ID   MSBA_LEGPA              Reviewed;         588 AA.
AC   Q5X498;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=ATP-dependent lipid A-core flippase {ECO:0000255|HAMAP-Rule:MF_01703};
DE            EC=7.5.2.6 {ECO:0000255|HAMAP-Rule:MF_01703};
DE   AltName: Full=Lipid A export ATP-binding/permease protein MsbA {ECO:0000255|HAMAP-Rule:MF_01703};
GN   Name=msbA {ECO:0000255|HAMAP-Rule:MF_01703}; OrderedLocusNames=lpp1782;
OS   Legionella pneumophila (strain Paris).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Paris;
RX   PubMed=15467720; DOI=10.1038/ng1447;
RA   Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA   Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA   Glaser P., Buchrieser C.;
RT   "Evidence in the Legionella pneumophila genome for exploitation of host
RT   cell functions and high genome plasticity.";
RL   Nat. Genet. 36:1165-1173(2004).
CC   -!- FUNCTION: Involved in lipopolysaccharide (LPS) biosynthesis.
CC       Translocates lipid A-core from the inner to the outer leaflet of the
CC       inner membrane. Transmembrane domains (TMD) form a pore in the inner
CC       membrane and the ATP-binding domain (NBD) is responsible for energy
CC       generation. {ECO:0000255|HAMAP-Rule:MF_01703}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + lipid A-core oligosaccharideSide 1 = ADP +
CC         phosphate + lipid A-core oligosaccharideSide 2.; EC=7.5.2.6;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01703};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01703}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01703}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01703}.
CC   -!- DOMAIN: In MsbA the ATP-binding domain (NBD) and the transmembrane
CC       domain (TMD) are fused. {ECO:0000255|HAMAP-Rule:MF_01703}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Lipid exporter
CC       (TC 3.A.1.106) family. {ECO:0000255|HAMAP-Rule:MF_01703}.
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DR   EMBL; CR628336; CAH12934.1; -; Genomic_DNA.
DR   RefSeq; WP_011214077.1; NC_006368.1.
DR   AlphaFoldDB; Q5X498; -.
DR   SMR; Q5X498; -.
DR   KEGG; lpp:lpp1782; -.
DR   LegioList; lpp1782; -.
DR   HOGENOM; CLU_000604_84_3_6; -.
DR   OMA; WGTYLVK; -.
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:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0034040; F:ATPase-coupled lipid transmembrane transporter activity; IEA:InterPro.
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; IPR011917; ABC_transpr_lipidA.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039421; Type_1_exporter.
DR   PANTHER; PTHR24221; PTHR24221; 1.
DR   Pfam; PF00664; ABC_membrane; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF90123; SSF90123; 1.
DR   TIGRFAMs; TIGR02203; MsbA_lipidA; 1.
DR   PROSITE; PS50929; ABC_TM1F; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS51239; MSBA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Lipid transport; Membrane;
KW   Nucleotide-binding; Translocase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..588
FT                   /note="ATP-dependent lipid A-core flippase"
FT                   /id="PRO_0000092584"
FT   TRANSMEM        23..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT   TRANSMEM        257..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT   TRANSMEM        278..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT   DOMAIN          28..310
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT   DOMAIN          342..576
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT   BINDING         375..382
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
SQ   SEQUENCE   588 AA;  65476 MW;  1EF7B7BBFD7252D3 CRC64;
     MKNNLPIKSR LLYKRLLSYV KPFWPVLLLG VLANILYSGI DAGFTYMTKL FLDKSFITID
     LDFVKQIPLI VLIGITLRGL VSSLGSYCMT WVARSVVKVL RQTVFSHIIH LPADYYDEAT
     SGQLLSKILY DVEQVAQVSA DALTDFIQNI CLVIGLLTVM MVICWQLSLM FLLTIPFVGI
     IVNYTNKRVR RISHKVQKTM GEVTEIASEA IEGYRVVRIF GGERYEITKF NKATEYSRKN
     DMKVAISKAI NVSGVQLVIA IGIAMIIMAA IHLSTVITIS AGSFLAIIAA MLQLIKPMKT
     LTTLNATIQR GLAGAESVFN LLDLPLERNN GLILKEKVRG EIEFKHVYHA YRQSQNILHD
     VNFVIEAGTS VALVGHSGSG KTTIASLLPR FYELSQGMIT LDGMPIQQLS LESLRKQISL
     VSQNVTLFND TLANNIAYGR FDASREQIIT AAKLAYADEF IKQLPDGYDT RVGENGVLLS
     GGQRQRIAIA RAILKDAPIL ILDEATSALD SESEHYIQAA LEQVMKGRTT LIIAHRLSTI
     KHAHKIIVLQ HGRIVEQGSH QELLDMDGHY AQLYKVQQFG RINEEVVV
 
 
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