MSBA_BLOFL
ID MSBA_BLOFL Reviewed; 583 AA.
AC Q7VR44;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=Bfl379;
OS Blochmannia floridanus.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX NCBI_TaxID=203907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12886019; DOI=10.1073/pnas.1533499100;
RA Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F.,
RA Latorre A., Rausell C., Kamerbeek J., Gadau J., Hoelldobler B.,
RA van Ham R.C.H.J., Gross R., Moya A.;
RT "The genome sequence of Blochmannia floridanus: comparative analysis of
RT reduced genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003).
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; BX248583; CAD83445.1; -; Genomic_DNA.
DR RefSeq; WP_011126653.1; NC_005061.1.
DR AlphaFoldDB; Q7VR44; -.
DR SMR; Q7VR44; -.
DR STRING; 203907.Bfl379; -.
DR EnsemblBacteria; CAD83445; CAD83445; Bfl379.
DR KEGG; bfl:Bfl379; -.
DR eggNOG; COG1132; Bacteria.
DR HOGENOM; CLU_000604_84_3_6; -.
DR OMA; WGTYLVK; -.
DR OrthoDB; 643917at2; -.
DR Proteomes; UP000002192; Chromosome.
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; 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; 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; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..583
FT /note="ATP-dependent lipid A-core flippase"
FT /id="PRO_0000092573"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 105..127
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT DOMAIN 30..312
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT DOMAIN 344..580
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT BINDING 378..385
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
SQ SEQUENCE 583 AA; 65499 MW; D4B5B840829342D5 CRC64;
MHYCNNGNIS NWKVFRRLWP IINPFKIGLI IASITLIINA VSDSLMLALL KPLLDEGFGK
ANRSIFMWMP LVLMGLMIMR GMSGFASTYC ISWVSGKVVM HIRRLLFNHI MNMPVSFFIE
QSTATLMSRI TYDADQVASS SSGALITIIR EGASVVGLCI MMFYYSWQLS LVLILIMPII
SIIIKLVSNK FKDIGKKIQN SMSQLVNSVE QMLKGHKEVL IFGGQHLEQN RFNYLSNRMR
QYTMKMVQTS SVFEPLIQFV ASLALACVLY IASIPSVIEM LSAGTITVIF SSMIALMKPL
KSLTNVSAQF QRGMVACQTL FTILDLKTEK NIGKFSVKRV KGHIIFDNVT FFYPETNTPS
LCNINFNIES GKTIALVGRS GSGKSTIVNL LTRFYDVYQG RILLDGLNLN DYTLTSLREQ
VSVVTQNVYL FNDTIANNIA YARTRFYSRA SIEEAAKMAY AMGFISKMKN GFDTIVGENG
ILLSNGQRQR IAIARALLRN CPILILDEAT SSLDTESECI IYKSINILKK NRTSLIIAHR
LSTIENADEI LVVERGSIVE RGIHVDLLNH KGVYSQLYKF QFS
