MSBA_DESPS
ID MSBA_DESPS Reviewed; 572 AA.
AC Q6AJW3;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, 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=DP2634;
OS Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfocapsaceae; Desulfotalea.
OX NCBI_TaxID=177439;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12343 / LSv54;
RX PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT permanently cold Arctic sediments.";
RL Environ. Microbiol. 6:887-902(2004).
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; CR522870; CAG37363.1; -; Genomic_DNA.
DR RefSeq; WP_011189875.1; NC_006138.1.
DR AlphaFoldDB; Q6AJW3; -.
DR SMR; Q6AJW3; -.
DR STRING; 177439.DP2634; -.
DR PRIDE; Q6AJW3; -.
DR EnsemblBacteria; CAG37363; CAG37363; DP2634.
DR KEGG; dps:DP2634; -.
DR eggNOG; COG1132; Bacteria.
DR HOGENOM; CLU_000604_84_3_7; -.
DR OMA; FNTLQMG; -.
DR OrthoDB; 643917at2; -.
DR Proteomes; UP000000602; 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; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..572
FT /note="ATP-dependent lipid A-core flippase"
FT /id="PRO_0000092576"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT DOMAIN 22..304
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT DOMAIN 338..571
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT BINDING 370..377
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
SQ SEQUENCE 572 AA; 63983 MW; 9F506ECB4A252A6B CRC64;
MTNKEIIKRL YHEIIPYKIP LFIAMFAMIV VAALTGAQAY LVKDLLDKIF MEKDVFFLQI
LPLIIIAIFF TKGVLYYTYA IILERVGQSI IRDFRLKIFA HIHRQSLSFF HNTPTGTLIS
RVLSDVALMQ QAVSTVIIQL LRDFFQVIFL LGVIFYMNWK LALICFLIIP LAAIPIVKFG
KIFRKLSTKT QEETAEVSNM LHETISGSRI VKAFCREDYE VERFHRQVET LFTITMKNAK
YRVFQSPLME IIGGFAVAGI IWVGGSEVIN GSATPGTFFA FLTAMITAYD PVKRVSQVNS
TIQQGLASAQ RVFAILDIKP EIEDKPEATS LAPFKESIEF HDVSFSYGTE KILSHINLKV
PAGEALAIVG PSGGGKTTLT NLIPRFIDLQ EGSITIDGTD IRDVTTNSLR NQIAMVTQQT
ILFNDTIRNN IAYGKDSCTE EEIRRAAKAA HALTFIEELP NGFDTALGEG GAKLSGGQRQ
RISIARALLA DAPILILDEA TSALDTESER EVQKALENLM QNRTTFVIAH RLSTIKNASR
IVVVKKGKIV EEGSHEELLK LEGEYQLLYN MQ
