MSBA_FRANO
ID MSBA_FRANO Reviewed; 593 AA.
AC Q47908;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 106.
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}; Synonyms=valA;
OS Francisella novicida.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=264;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=U112;
RX PubMed=7881549; DOI=10.1099/13500872-140-12-3309;
RA Mdluli K.E., Anthony L.S., Baron G.S., McDonald M.K., Myltseva S.V.,
RA Nano F.E.;
RT "Serum-sensitive mutation of Francisella novicida: association with an ABC
RT transporter gene.";
RL Microbiology 140:3309-3318(1994).
RN [2]
RP FUNCTION.
RX PubMed=9401020; DOI=10.1128/jb.179.24.7638-7643.1997;
RA McDonald M.K., Cowley S.C., Nano F.E.;
RT "Temperature-sensitive lesions in the Francisella novicida valA gene cloned
RT into an Escherichia coli msbA lpxK mutant affecting deoxycholate resistance
RT and lipopolysaccharide assembly at the restrictive temperature.";
RL J. Bacteriol. 179:7638-7643(1997).
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 ECO:0000269|PubMed:9401020}.
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 membrane {ECO:0000255|HAMAP-Rule:MF_01703};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD15237.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L17003; AAD15237.1; ALT_FRAME; Genomic_DNA.
DR AlphaFoldDB; Q47908; -.
DR SMR; Q47908; -.
DR STRING; 676032.FN3523_1670; -.
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 membrane; Lipid transport; Membrane; Nucleotide-binding;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..593
FT /note="ATP-dependent lipid A-core flippase"
FT /id="PRO_0000092581"
FT TRANSMEM 33..55
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT DOMAIN 38..319
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT DOMAIN 351..585
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT BINDING 383..390
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
SQ SEQUENCE 593 AA; 65130 MW; 004E90B90EC9D311 CRC64;
MTNHQKVGTL YKRLLLQVKH LMAFSAFGCY RKYIFLSADA SMIYLINPIL NYGFGPGGGI
TKQSATILML MGVGMVGFIA LRSVGSFVSQ YFIGSLGQKV VYKFRKDIYK RLMDLPASFF
DKHSTGQIIS RLLYNVDQVT EATSTAIITV VQDGTFVIGL IVVMFVSSWQ LSLFLIVVGP
FLGLFISIIN KKFRNLSRNT QSSMGNVTHT AEETIRNYKE IRIFGAQQKQ QNKFFKNLDY
TYSQQIRTIA LDALTSPVIQ IIASLVLAFS LFTIAIFGTN DGGGSSWLTA GSFASFFAAA
AAILKPIKNL TKVNVVIQKA VAATEDIFYI LDYPAEKETG SKELAKVDGN VTIKDLSFAF
GEHKVLSGVS VDIKAGQTVA FVGKSGSGKT TLTSIISRFY TQHKGEILLD GVDTRELTLE
NLRSHLSIVS QNVHLFDDTV YNNIAFGLSR EVSEDEVIDA LKRANAYEFV QELSDGIHTN
IGNNGSKLSG GQRQRISIAR ALLKNAPVLI FDEATSALDN ESERVVQQAL ESLTESCTTI
VIAHRLSTVE NADKIVVMDG GKVVESGKHQ ELLEQGGLYT GSINRDFNST YAR
