(data stored in ACNUC7421 zone)

SWISSPROT: 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   08-MAY-2019, entry version 106.
DE   RecName: Full=Lipid A export ATP-binding/permease protein MsbA {ECO:0000255|HAMAP-Rule:MF_01703};
DE            EC=7.5.2.6 {ECO:0000255|HAMAP-Rule:MF_01703};
GN   Name=msbA {ECO:0000255|HAMAP-Rule:MF_01703};
GN   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 lipid A export and possibly also in
CC       glycerophospholipid export and for biogenesis of the outer
CC       membrane. Transmembrane domains (TMD) form a pore in the inner
CC       membrane and the ATP-binding domain (NBD) is responsible for
CC       energy generation. {ECO:0000255|HAMAP-Rule:MF_01703}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H(2)O + lipid A-core oligosaccharide(Side 1) = ADP
CC         + phosphate + lipid A-core oligosaccharide(Side 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.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Lipid
CC       exporter (TC 3.A.1.106) family. {ECO:0000255|HAMAP-Rule:MF_01703}.
DR   EMBL; CP000094; ABA72225.1; -; Genomic_DNA.
DR   RefSeq; WP_011332146.1; NC_007492.2.
DR   SMR; Q3KJ31; -.
DR   STRING; 205922.Pfl01_0481; -.
DR   EnsemblBacteria; ABA72225; ABA72225; Pfl01_0481.
DR   KEGG; pfo:Pfl01_0481; -.
DR   eggNOG; ENOG4105BZ1; Bacteria.
DR   eggNOG; COG1132; LUCA.
DR   KO; K11085; -.
DR   OMA; KDHEDAK; -.
DR   BioCyc; PFLU205922:G1G4S-486-MONOMER; -.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0034040; F:lipid-transporting ATPase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.1560.10; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011527; ABC1_TM_dom.
DR   InterPro; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR011917; ABC_transpr_lipidA.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039421; Type_I_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;
DR   PRODOM; Q3KJ31.
DR   SWISS-2DPAGE; Q3KJ31.
KW   ATP-binding; Cell inner membrane; Cell membrane; Complete proteome;
KW   Lipid transport; Membrane; Nucleotide-binding; Translocase;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    600       Lipid A export ATP-binding/permease
FT                                protein MsbA.
FT                                /FTId=PRO_0000271641.
FT   TRANSMEM     27     47       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01703}.
FT   TRANSMEM     83    103       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01703}.
FT   TRANSMEM    174    194       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01703}.
FT   TRANSMEM    267    287       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01703}.
FT   DOMAIN       30    322       ABC transmembrane type-1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01703}.
FT   DOMAIN      354    590       ABC transporter. {ECO:0000255|HAMAP-
FT                                Rule:MF_01703}.
FT   NP_BIND     388    395       ATP. {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
//

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