MSBA_SALTY
ID MSBA_SALTY Reviewed; 582 AA.
AC P63359; Q8XFG5;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-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=STM0984;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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 -!- INTERACTION:
CC P63359; P63359: msbA; NbExp=2; IntAct=EBI-15671217, EBI-15671217;
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; AE006468; AAL19918.1; -; Genomic_DNA.
DR RefSeq; NP_459959.1; NC_003197.2.
DR RefSeq; WP_000551246.1; NC_003197.2.
DR PDB; 3B5Y; X-ray; 4.50 A; A/B/C/D=1-582.
DR PDB; 3B5Z; X-ray; 4.20 A; A/B/C/D=1-582.
DR PDB; 3B60; X-ray; 3.70 A; A/B/C/D=1-582.
DR PDB; 6BL6; X-ray; 2.80 A; A/B=7-582.
DR PDB; 6O30; X-ray; 4.47 A; A/B=7-582.
DR PDBsum; 3B5Y; -.
DR PDBsum; 3B5Z; -.
DR PDBsum; 3B60; -.
DR PDBsum; 6BL6; -.
DR PDBsum; 6O30; -.
DR AlphaFoldDB; P63359; -.
DR SMR; P63359; -.
DR DIP; DIP-46177N; -.
DR STRING; 99287.STM0984; -.
DR TCDB; 3.A.1.106.20; the atp-binding cassette (abc) superfamily.
DR PaxDb; P63359; -.
DR EnsemblBacteria; AAL19918; AAL19918; STM0984.
DR GeneID; 1252502; -.
DR KEGG; stm:STM0984; -.
DR PATRIC; fig|99287.12.peg.1037; -.
DR HOGENOM; CLU_000604_84_3_6; -.
DR OMA; WGTYLVK; -.
DR PhylomeDB; P63359; -.
DR BioCyc; SENT99287:STM0984-MON; -.
DR BRENDA; 7.5.2.6; 5542.
DR EvolutionaryTrace; P63359; -.
DR Proteomes; UP000001014; 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: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_0000092598"
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"
FT HELIX 9..20
FT /evidence="ECO:0007829|PDB:6BL6"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:6BL6"
FT HELIX 25..46
FT /evidence="ECO:0007829|PDB:6BL6"
FT HELIX 48..52
FT /evidence="ECO:0007829|PDB:6BL6"
FT TURN 53..59
FT /evidence="ECO:0007829|PDB:6BL6"
FT HELIX 63..108
FT /evidence="ECO:0007829|PDB:6BL6"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:6BL6"
FT HELIX 121..209
FT /evidence="ECO:0007829|PDB:6BL6"
FT HELIX 214..220
FT /evidence="ECO:0007829|PDB:6BL6"
FT HELIX 223..271
FT /evidence="ECO:0007829|PDB:6BL6"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:6BL6"
FT HELIX 281..293
FT /evidence="ECO:0007829|PDB:6BL6"
FT HELIX 295..301
FT /evidence="ECO:0007829|PDB:6BL6"
FT HELIX 304..323
FT /evidence="ECO:0007829|PDB:6BL6"
FT STRAND 342..349
FT /evidence="ECO:0007829|PDB:6BL6"
FT STRAND 358..366
FT /evidence="ECO:0007829|PDB:6BL6"
FT STRAND 371..376
FT /evidence="ECO:0007829|PDB:6BL6"
FT STRAND 378..381
FT /evidence="ECO:0007829|PDB:6BL6"
FT HELIX 382..389
FT /evidence="ECO:0007829|PDB:6BL6"
FT STRAND 396..402
FT /evidence="ECO:0007829|PDB:6BL6"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:6BL6"
FT HELIX 412..418
FT /evidence="ECO:0007829|PDB:6BL6"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:6BL6"
FT HELIX 433..437
FT /evidence="ECO:0007829|PDB:6BL6"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:6BL6"
FT STRAND 442..445
FT /evidence="ECO:0007829|PDB:6BL6"
FT HELIX 447..456
FT /evidence="ECO:0007829|PDB:6BL6"
FT HELIX 460..463
FT /evidence="ECO:0007829|PDB:6BL6"
FT STRAND 464..466
FT /evidence="ECO:0007829|PDB:6BL6"
FT HELIX 469..471
FT /evidence="ECO:0007829|PDB:6BL6"
FT HELIX 483..496
FT /evidence="ECO:0007829|PDB:6BL6"
FT STRAND 500..505
FT /evidence="ECO:0007829|PDB:6BL6"
FT STRAND 507..509
FT /evidence="ECO:0007829|PDB:6BL6"
FT HELIX 516..527
FT /evidence="ECO:0007829|PDB:6BL6"
FT STRAND 530..535
FT /evidence="ECO:0007829|PDB:6BL6"
FT HELIX 539..543
FT /evidence="ECO:0007829|PDB:6BL6"
FT STRAND 546..552
FT /evidence="ECO:0007829|PDB:6BL6"
FT STRAND 555..560
FT /evidence="ECO:0007829|PDB:6BL6"
FT HELIX 562..566
FT /evidence="ECO:0007829|PDB:6BL6"
FT TURN 567..569
FT /evidence="ECO:0007829|PDB:6BL6"
FT HELIX 571..578
FT /evidence="ECO:0007829|PDB:6BL6"
SQ SEQUENCE 582 AA; 64340 MW; A8806F8CC650D538 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 TSLVIAHRLS
TIEQADEIVV VEDGIIVERG THSELLAQHG VYAQLHKMQF GQ
