MSBA_FRAT1
ID MSBA_FRAT1 Reviewed; 609 AA.
AC Q14JW6;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=FTF0109;
OS Francisella tularensis subsp. tularensis (strain FSC 198).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=393115;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSC 198;
RX PubMed=17406676; DOI=10.1371/journal.pone.0000352;
RA Chaudhuri R.R., Ren C.-P., Desmond L., Vincent G.A., Silman N.J.,
RA Brehm J.K., Elmore M.J., Hudson M.J., Forsman M., Isherwood K.E.,
RA Gurycova D., Minton N.P., Titball R.W., Pallen M.J., Vipond R.;
RT "Genome sequencing shows that European isolates of Francisella tularensis
RT subspecies tularensis are almost identical to US laboratory strain Schu
RT S4.";
RL PLoS ONE 2:E352-E352(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. {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; AM286280; CAL08125.1; -; Genomic_DNA.
DR RefSeq; WP_003019850.1; NC_008245.1.
DR PDB; 5DGX; X-ray; 1.73 A; A=357-609.
DR PDBsum; 5DGX; -.
DR AlphaFoldDB; Q14JW6; -.
DR SMR; Q14JW6; -.
DR KEGG; ftf:FTF0109; -.
DR HOGENOM; CLU_000604_84_3_6; -.
DR OMA; FNTLQMG; -.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane;
KW Lipid transport; Membrane; Nucleotide-binding; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..609
FT /note="ATP-dependent lipid A-core flippase"
FT /id="PRO_0000271628"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT DOMAIN 47..340
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT DOMAIN 372..606
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT BINDING 404..411
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT STRAND 372..381
FT /evidence="ECO:0007829|PDB:5DGX"
FT STRAND 384..394
FT /evidence="ECO:0007829|PDB:5DGX"
FT STRAND 399..403
FT /evidence="ECO:0007829|PDB:5DGX"
FT HELIX 410..417
FT /evidence="ECO:0007829|PDB:5DGX"
FT STRAND 424..430
FT /evidence="ECO:0007829|PDB:5DGX"
FT HELIX 435..437
FT /evidence="ECO:0007829|PDB:5DGX"
FT HELIX 440..445
FT /evidence="ECO:0007829|PDB:5DGX"
FT STRAND 447..452
FT /evidence="ECO:0007829|PDB:5DGX"
FT STRAND 458..460
FT /evidence="ECO:0007829|PDB:5DGX"
FT HELIX 461..466
FT /evidence="ECO:0007829|PDB:5DGX"
FT HELIX 475..484
FT /evidence="ECO:0007829|PDB:5DGX"
FT HELIX 488..492
FT /evidence="ECO:0007829|PDB:5DGX"
FT HELIX 497..499
FT /evidence="ECO:0007829|PDB:5DGX"
FT HELIX 504..506
FT /evidence="ECO:0007829|PDB:5DGX"
FT HELIX 511..525
FT /evidence="ECO:0007829|PDB:5DGX"
FT STRAND 528..533
FT /evidence="ECO:0007829|PDB:5DGX"
FT HELIX 552..556
FT /evidence="ECO:0007829|PDB:5DGX"
FT STRAND 558..563
FT /evidence="ECO:0007829|PDB:5DGX"
FT HELIX 567..572
FT /evidence="ECO:0007829|PDB:5DGX"
FT STRAND 574..580
FT /evidence="ECO:0007829|PDB:5DGX"
FT STRAND 583..588
FT /evidence="ECO:0007829|PDB:5DGX"
FT HELIX 590..595
FT /evidence="ECO:0007829|PDB:5DGX"
FT HELIX 599..605
FT /evidence="ECO:0007829|PDB:5DGX"
SQ SEQUENCE 609 AA; 66772 MW; 996449AD1EAC7166 CRC64;
MANMIDKIDL KSQGSSNLSG EMTNHQKVGT LYKRLLLQVK HLWHFLLLAA IGSIFFSAAD
ASMIYLINPI LNYGFGPGGG ITKQSATILM LMGVGMVGLL ALRSVGSFVS QYFIGSLGQK
VVYKFRKDIY KRLMDLPASF FDKHSTGQII SRLLYNVDQV IEATSTAIIT VVQDGTFVIG
LIVVMFVSSW QLSLFLIVVG PFLGLFISII NKKFRNLSRN TQSSMGNVTH TAEETIRNYK
EIRIFGAQQK QQNKFFKNLD YTYSQQIRTI ALDALTSPVI QIIASLVLAF SLFTIAIFGT
NEGDGSSWLT AGSFASFFAA AAAILKPIKN LTKVNVVIQK AVAATEDIFY ILDYPAEKET
GSKELAKVDG NVTIKDLSFA FGEHKVLSGV SVDIKAGQTV AFVGKSGSGK TTLTSIISRF
YTQHEGEILL DGVDTRELTL ENLRSHLSIV SQNVHLFDDT VYNNIAFGLS REVSEEEVID
ALKRANAYEF VQELSDGINT NIGNNGSKLS GGQRQRISIA RALLKNAPVL IFDEATSALD
NESERVVQQA LESLTKSCTT IVIAHRLSTV ENADKIVVMD GGRVVESGKH QELLEQGGLY
TRLYQSGLQ
