MSBA_PSEPF
ID MSBA_PSEPF Reviewed; 600 AA.
AC Q3KJ31;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
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=Pfl01_0481;
OS Pseudomonas fluorescens (strain Pf0-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=205922;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pf0-1;
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(2009).
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; CP000094; ABA72225.1; -; Genomic_DNA.
DR RefSeq; WP_011332146.1; NC_007492.2.
DR AlphaFoldDB; Q3KJ31; -.
DR SMR; Q3KJ31; -.
DR STRING; 205922.Pfl01_0481; -.
DR PRIDE; Q3KJ31; -.
DR EnsemblBacteria; ABA72225; ABA72225; Pfl01_0481.
DR KEGG; pfo:Pfl01_0481; -.
DR eggNOG; COG1132; Bacteria.
DR HOGENOM; CLU_000604_84_3_6; -.
DR OMA; FNTLQMG; -.
DR Proteomes; UP000002704; 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; 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..600
FT /note="ATP-dependent lipid A-core flippase"
FT /id="PRO_0000271641"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT DOMAIN 31..322
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT DOMAIN 354..590
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT BINDING 388..395
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
SQ SEQUENCE 600 AA; 66099 MW; 78F4379022A7A9E0 CRC64;
MTDSSPAASP SSLKIYFRLL GYVRPYISLF LISIVGFLIF ASTQPMLGYI LKYFVDGLSN
PEAVLFPTVP YLRDLQLLQA VPLLIILIAA WQGLGSYLGN YFLAKVSLGL VHDLRVQLFN
NLLVLPNRYF DKHNSGHLIS RITFNVTMVT GAATDAIKVV IREGMTVIFL FASLLFMNWK
LTLVMVAILP LIAVMVRTAS KKFRKQSKKI QLAMGDVTHV ASETIQGYRV VRSFGGEAYE
EKRFLDASQG NTDKQLRMTR TGAIYTPLLQ LVIYSAMAIL MFLVLYLRGD ASAGDMVAYI
TLAGLLPKPI RQLSEVSSTI QKGVAGAESI FEQLDVEPEV DTGTVERDSV SGRLDVRNLS
FTYPGTERQV LDDISFSVEP GQMVALVGRS GSGKSTLANL IPRFYHHDKG EILIDGVEVE
QYKLLNLRRH IAQVTQHVTL FSDTVANNIA YGDLAGAPRE DIEKAARDAY AMDFIAQLPE
GLDTQVGENG VLLSGGQRQR LAIARALLKN APLLILDEAT SALDTESERH IQAALDQVMK
GRTTLVIAHR LSTIEKADLI LVMDQGRIVE RGTHDDLLAQ NGYYARLNAM GLDAPAEDIA
