MSBA_PSYCK
ID MSBA_PSYCK Reviewed; 598 AA.
AC Q1QBW0;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=Pcryo_1062;
OS Psychrobacter cryohalolentis (strain ATCC BAA-1226 / DSM 17306 / VKM B-2378
OS / K5).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=335284;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1226 / DSM 17306 / VKM B-2378 / K5;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Sims D.R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Richardson P.;
RT "Complete sequence of chromosome of Psychrobacter cryohalolentis K5.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000323; ABE74843.1; -; Genomic_DNA.
DR RefSeq; WP_011513399.1; NC_007969.1.
DR AlphaFoldDB; Q1QBW0; -.
DR SMR; Q1QBW0; -.
DR STRING; 335284.Pcryo_1062; -.
DR KEGG; pcr:Pcryo_1062; -.
DR eggNOG; COG1132; Bacteria.
DR HOGENOM; CLU_000604_84_3_6; -.
DR OMA; FNTLQMG; -.
DR Proteomes; UP000002425; 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..598
FT /note="ATP-dependent lipid A-core flippase"
FT /id="PRO_0000271645"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT DOMAIN 48..329
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT DOMAIN 360..595
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 393..400
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
SQ SEQUENCE 598 AA; 65885 MW; DCF8B0D410373BE7 CRC64;
MSQAYQPDST KTSAKTPVAP TVATLNPPKR KTLMRLLAYL KPYWWAILLT IIGFAINAAT
EIWIAKLLQY ITDAINQNDQ SKQDLFPFII VMLFFVRGVG SFLGNYYTAL VSRNLVYELR
VEVFNKLLRL PSSFYLANPA GTISSKLIFD VEQVTAASTD SMKTLLRDGL TVVALMGFLL
YSNWRLTLIL FVVLPPILWL IRVASKRYLK LSKGIQETMG DVSHITNEVI NGYQVVKNYG
GQVYESKRFD VTSKKNLRQG MKVVVTNSIN TPAVQLLMAM AMAVVVWLAL RPAVIDDISA
GQFISYIAAA GLLSKPVRSL TDVNQQLQRG LAAGESIFAL LDEPEEADTG VLSPTLAGEI
KLDNVSLVYP DSTVALHDFN LDIRAGETVA LVGRSGAGKS SLVNLLTRTL TTSSGQITLD
GMPIEDIKLE SLRAQIAMVN QQVVLFNTTV FNNIAYGSLA HKTPAEVEQA AKDAFAHDFI
MQMPNGYQSE IGAEGLQLSG GQRQRLSIAR ALLKDAPILI LDEATSALDN ESEYYIQKAL
DNIMKNRTTL VIAHRLTTIE SADRIAVLDG GQIVELGTHT QLMQLHGHYA QMYARDFE
