ID   MSBA_XANOM              Reviewed;         589 AA.
AC   Q2P3E7;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=XOO2175;
OS   Xanthomonas oryzae pv. oryzae (strain MAFF 311018).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=342109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 311018;
RA   Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.;
RT   "Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of
RT   large numbers of effector genes and insertion sequences to its race
RT   diversity.";
RL   Jpn. Agric. Res. Q. 39:275-287(2005).
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; AP008229; BAE68930.1; -; Genomic_DNA.
DR   RefSeq; WP_011258974.1; NC_007705.1.
DR   AlphaFoldDB; Q2P3E7; -.
DR   SMR; Q2P3E7; -.
DR   KEGG; xom:XOO2175; -.
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..589
FT                   /note="ATP-dependent lipid A-core flippase"
FT                   /id="PRO_0000271667"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT   TRANSMEM        70..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT   TRANSMEM        157..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT   TRANSMEM        261..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT   TRANSMEM        283..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT   DOMAIN          32..314
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT   DOMAIN          346..582
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT   BINDING         380..387
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
SQ   SEQUENCE   589 AA;  64108 MW;  BB9C5B7B37DD1130 CRC64;
     MTNSTDRPVS VSSWRTYRRL VAFAKPYRLL LVAALIAALI EAAGTTGFLA LMKPITDETF
     IYKNAEVSRW LPVQIILLFV VRGIAGYITD MAMGKSARSI ARDLRIKVMA KYLRLPGSRF
     DSEPVPSMLI RLGSDSDQVA QAAVDAIKVM IQQSLQVIGA LALMLWHSWQ VTLTILVLAP
     VLAWVMDKVA RRYRRISHSI QESGAHLLQA ADQTLSSHQE VKIYGAQQTE MERYGALADR
     NLRLAMKVES TRGISTATVQ MIGAIGLSAL LFVAGAQALA GRLTAGDFVV LMTSMLTIIP
     GLKQLTNVQN MVQRGLASAE RLFSVLDSPD EPDQGAVALT RAKGLIEFRD VTARYPGQVN
     PALADVSFIA QPGTVTAIVG RSGSGKSSLI KLIPRFYDAE AGQILLDGQP VQAYALADLR
     RQIALVGQQV MLFDGSIAEN VAFGEMRSAD ASQLERAILG ANAMEFVAQL PEGLQSHVGA
     KGGRLSGGQR QRLAIARAML KDAPILILDE ATAALDNESE RLVQDALHKL MPDRTTLVIA
     HRLSTIEHAD QVLVMDQGRI VERGTHHELL AQGGLYSHLH GMQFRERQA