MSBA_VIBCH
ID MSBA_VIBCH Reviewed; 582 AA.
AC Q9KQW9;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
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=VC_1878;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2]
RP RETRACTED PAPER.
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=12823979; DOI=10.1016/s0022-2836(03)00587-4;
RA Chang G.;
RT "Structure of MsbA from Vibrio cholera: a multidrug resistance ABC
RT transporter homolog in a closed conformation.";
RL J. Mol. Biol. 330:419-430(2003).
RN [3]
RP RETRACTION NOTICE OF PUBMED:12823979.
RX PubMed=17580380; DOI=10.1016/j.jmb.2003.05.001;
RA Chang G.;
RL J. Mol. Biol. 369:596-596(2007).
RN [4] {ECO:0007744|PDB:3B5X}
RP X-RAY CRYSTALLOGRAPHY (5.50 ANGSTROMS), ATPASE ACTIVITY, SUBUNIT, AND
RP DOMAIN.
RX PubMed=18024585; DOI=10.1073/pnas.0709388104;
RA Ward A., Reyes C.L., Yu J., Roth C.B., Chang G.;
RT "Flexibility in the ABC transporter MsbA: Alternating access with a
RT twist.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:19005-19010(2007).
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 (By similarity). Shows ATPase activity (PubMed:18024585).
CC {ECO:0000255|HAMAP-Rule:MF_01703, ECO:0000269|PubMed:18024585}.
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 ECO:0000269|PubMed:18024585}.
CC -!- INTERACTION:
CC Q9KQW9; Q9KQW9: msbA; NbExp=2; IntAct=EBI-15671160, EBI-15671160;
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 ECO:0000269|PubMed:18024585}.
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; AE003852; AAF95026.1; -; Genomic_DNA.
DR PIR; D82146; D82146.
DR RefSeq; NP_231512.1; NC_002505.1.
DR RefSeq; WP_000052153.1; NZ_LT906614.1.
DR PDB; 3B5X; X-ray; 5.50 A; A/B=1-582.
DR PDBsum; 3B5X; -.
DR AlphaFoldDB; Q9KQW9; -.
DR SMR; Q9KQW9; -.
DR DIP; DIP-46176N; -.
DR STRING; 243277.VC_1878; -.
DR DNASU; 2613632; -.
DR EnsemblBacteria; AAF95026; AAF95026; VC_1878.
DR GeneID; 57740513; -.
DR KEGG; vch:VC_1878; -.
DR PATRIC; fig|243277.26.peg.1794; -.
DR eggNOG; COG1132; Bacteria.
DR HOGENOM; CLU_000604_84_3_6; -.
DR OMA; WGTYLVK; -.
DR BioCyc; VCHO:VC1878-MON; -.
DR BRENDA; 7.5.2.5; 6626.
DR EvolutionaryTrace; Q9KQW9; -.
DR Proteomes; UP000000584; Chromosome 1.
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:0042802; F:identical protein binding; IPI:IntAct.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane;
KW Lipid transport; Membrane; Nucleotide-binding; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..582
FT /note="ATP-dependent lipid A-core flippase"
FT /id="PRO_0000092601"
FT TRANSMEM 27..48
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:18024585"
FT TRANSMEM 63..85
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:18024585"
FT TRANSMEM 144..168
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:18024585"
FT TRANSMEM 170..188
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:18024585"
FT TRANSMEM 244..266
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:18024585"
FT TRANSMEM 283..302
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:18024585"
FT DOMAIN 28..310
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT DOMAIN 342..578
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT BINDING 376..383
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
SQ SEQUENCE 582 AA; 64554 MW; D82C931DD6210945 CRC64;
MSLHSDESNW QTFKRLWTYI RLYKAGLVVS TIALVINAAA DTYMISLLKP LLDEGFGNAE
SNFLRILPFM ILGLMFVRGL SGFASSYCLS WVSGNVVMQM RRRLFNHFMH MPVRFFDQES
TGGLLSRITY DSEQVAGATS RALVSIVREG ASIIGLLTLM FWNSWQLSLV LIVVAPVVAF
AISFVSKRFR KISRNMQTAM GHVTSSAEQM LKGHKVVLSY GGQEVERKRF DKVSNSMRQQ
TMKLVSAQSI ADPVIQMIAS LALFAVLFLA SVDSIRAELT PGTFTVVFSA MFGLMRPLKA
LTSVTSEFQR GMAACQTLFG LMDLETERDN GKYEAERVNG EVDVKDVTFT YQGKEKPALS
HVSFSIPQGK TVALVGRSGS GKSTIANLFT RFYDVDSGSI CLDGHDVRDY KLTNLRRHFA
LVSQNVHLFN DTIANNIAYA AEGEYTREQI EQAARQAHAM EFIENMPQGL DTVIGENGTS
LSGGQRQRVA IARALLRDAP VLILDEATSA LDTESERAIQ AALDELQKNK TVLVIAHRLS
TIEQADEILV VDEGEIIERG RHADLLAQDG AYAQLHRIQF GE
