MSBA_PSEAE
ID MSBA_PSEAE Reviewed; 603 AA.
AC Q9HUG8;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
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=PA4997;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; AE004091; AAG08382.1; -; Genomic_DNA.
DR PIR; B83022; B83022.
DR RefSeq; NP_253684.1; NC_002516.2.
DR RefSeq; WP_003114544.1; NZ_QZGE01000002.1.
DR AlphaFoldDB; Q9HUG8; -.
DR SMR; Q9HUG8; -.
DR STRING; 287.DR97_2352; -.
DR PaxDb; Q9HUG8; -.
DR PRIDE; Q9HUG8; -.
DR EnsemblBacteria; AAG08382; AAG08382; PA4997.
DR GeneID; 881672; -.
DR KEGG; pae:PA4997; -.
DR PATRIC; fig|208964.12.peg.5237; -.
DR PseudoCAP; PA4997; -.
DR HOGENOM; CLU_000604_84_3_6; -.
DR InParanoid; Q9HUG8; -.
DR OMA; FNTLQMG; -.
DR PhylomeDB; Q9HUG8; -.
DR BioCyc; PAER208964:G1FZ6-5113-MON; -.
DR BRENDA; 7.5.2.6; 5087.
DR Proteomes; UP000002438; 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:0016887; F:ATP hydrolysis activity; IDA:PseudoCAP.
DR GO; GO:0005347; F:ATP transmembrane transporter activity; IDA:PseudoCAP.
DR GO; GO:0034040; F:ATPase-coupled lipid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0009245; P:lipid A biosynthetic process; IMP:PseudoCAP.
DR GO; GO:0015920; P:lipopolysaccharide transport; IMP:PseudoCAP.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
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; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..603
FT /note="ATP-dependent lipid A-core flippase"
FT /id="PRO_0000092593"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT DOMAIN 31..324
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT DOMAIN 356..592
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT BINDING 390..397
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
SQ SEQUENCE 603 AA; 66432 MW; 4A91DA2845BCF5C9 CRC64;
MSDSPQNPGP SSLKIYFRLL GYVKPYIGMF LLSIVGFLIF ASTQPMLAGI LKYFVDGLSN
PDAALFPNVQ WPWLRDLHLV YAVPLLIILI AAWQGLGSFL GNFFLAKVSL GLVHDLRVAL
FNKLLVLPNR YFDTHSSGHL ISRITFNVTM VTGAATDAIK VVIREGLTVV FLFLYLLWMN
WKLTLVMLAI LPVIAVMVTT ASRKFRKQSK KIQVAMGDVT HVASETIQGY RVVRSFGGEA
YEEKRFLDAS QSNTDKQLRM TKTGAVYTPM LQLVIYVAMA ILMFLVLWLR GDASAGDLVA
YITAAGLLPK PIRQLSEVSS TVQRGVAGAE SIFEQLDEAA EEDQGTVEKE RVSGRLEVRN
LSFRYPGTDK QVLDDISFIA EPGQMIALVG RSGSGKSTLA NLVPRFYQHN DGKILLDGVE
VEDYRLRNLR RHIALVTQQV TLFNDSVANN IAYGDLAGAP REEIERAAKA ANAKEFIDNL
PQGFDTEVGE NGVLLSGGQR QRLAIARALL KDAPLLILDE ATSALDTESE RHIQAALDEV
MKGRTTLVIA HRLSTIEKAD LILVMDQGQI VERGSHAELL AQNGHYARLH AMGLDEQAPA
PVG
