MSBA_XANCP
ID MSBA_XANCP Reviewed; 589 AA.
AC Q8P8W4;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=XCC2120;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
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; AE008922; AAM41405.1; -; Genomic_DNA.
DR RefSeq; NP_637481.1; NC_003902.1.
DR RefSeq; WP_011037271.1; NC_003902.1.
DR AlphaFoldDB; Q8P8W4; -.
DR SMR; Q8P8W4; -.
DR STRING; 340.xcc-b100_2060; -.
DR EnsemblBacteria; AAM41405; AAM41405; XCC2120.
DR KEGG; xcc:XCC2120; -.
DR PATRIC; fig|190485.4.peg.2270; -.
DR eggNOG; COG1132; Bacteria.
DR HOGENOM; CLU_000604_84_7_6; -.
DR OMA; WGTYLVK; -.
DR Proteomes; UP000001010; 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; IBA:GO_Central.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
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..589
FT /note="ATP-dependent lipid A-core flippase"
FT /id="PRO_0000092607"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT DOMAIN 32..314
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT DOMAIN 346..582
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT BINDING 380..387
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
SQ SEQUENCE 589 AA; 64255 MW; 738ED5810107E73B CRC64;
MKTINENAPQ VSSWQTYRRL LAFAKPYRLL LVAALIAALI EAAGTTGFLA LMKPITDETF
IYKNAEVSRW LPVQIILLFV IRGAAGYITD MAMGKSARSI ARDLRVKVMS KYLRLPGSRF
DSEPVPSMLI RLGSDSDQVA QAAVDAVKVM IQQSLQVIGA LALMLWHSWQ VTLTILVLAP
VLAWVMDKVA RRYRRISHSI QESGAHLLQA ADQTLSSHQE VKIYGAQQSE MERYSGLADR
NLRLAMKVES TRGISTATVQ MIGAIGLSAL LFVAGAQALA GRLTAGDFVV LMTSMLTIIP
GLKQLTNVQN MVQRGLASAE RLFSVLDSPD EPDQGQVPLT RAKGLIEFRD VTARYPGQAN
PALADVSFVA QPGTVTAIVG RSGSGKSSLI KLIPRFYEAE SGQILLDGHP VQAYALADLR
RQIALVGQQV MLFDGSIAEN VAYGEMRQCD AGQLERAIQG ANAMEFVAQL PEGLQSHVGT
KGGRLSGGQR QRLAIARAML KDAPILILDE ATAALDNESE RLVQDALHKL MPDRTTLVIA
HRLSTIEHAD QVLVMDQGRI VERGTHQELL ALGGLYSHLH GMQFRERQA
