MSBA_SALPA
ID MSBA_SALPA Reviewed; 582 AA.
AC Q5PGH0;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=SPA1814;
OS Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=295319;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9150 / SARB42;
RX PubMed=15531882; DOI=10.1038/ng1470;
RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA Warren W., Florea L., Spieth J., Wilson R.K.;
RT "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT restricted serovars of Salmonella enterica that cause typhoid.";
RL Nat. Genet. 36:1268-1274(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; CP000026; AAV77730.1; -; Genomic_DNA.
DR RefSeq; WP_000551245.1; NC_006511.1.
DR AlphaFoldDB; Q5PGH0; -.
DR SMR; Q5PGH0; -.
DR EnsemblBacteria; AAV77730; AAV77730; SPA1814.
DR KEGG; spt:SPA1814; -.
DR HOGENOM; CLU_000604_84_3_6; -.
DR OMA; WGTYLVK; -.
DR Proteomes; UP000008185; 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; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..582
FT /note="ATP-dependent lipid A-core flippase"
FT /id="PRO_0000271651"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
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; 64372 MW; B8906F9CD650D538 CRC64;
MHNDKDLSTW QTFRRLWPTI APFKAGLIVA GIALILNAAS DTFMLSLLKP LLDDGFGKTD
RSVLLWMPLV VIGLMILRGI TSYISSYCIS WVSGKVVMTM RRRLFGHMMG MPVAFFDKQS
TGTLLSRITY DSEQVASSSS GALITVVREG ASIIGLFIMM FYYSWQLSII LVVLAPIVSI
AIRVVSKRFR SISKNMQNTM GQVTTSAEQM LKGHKEVLIF GGQEVETKRF DKVSNKMRLQ
GMKMVSASSI SDPIIQLIAS LALAFVLYAA SFPSVMDSLT AGTITVVFSS MIALMRPLKS
LTNVNAQFQR GMAACQTLFA ILDSEQEKDE GKRVIDRATG DLEFRNVTFT YPGREVPALR
NINLKIPAGK TVALVGRSGS GKSTIASLIT RFYDIDEGHI LMDGHDLREY TLASLRNQVA
LVSQNVHLFN DTVANNIAYA RTEEYSREQI EEAARMAYAM DFINKMDNGL DTIIGENGVL
LSGGQRQRIA IARALLRDSP ILILDEATSA LDTESERAIQ AALDELQKNR TSLMIAHRLS
TIEQADEIVV VEDGIIVERG THSELLAQHG VYAQLHKMQF GQ
