MSBA_NITOC
ID MSBA_NITOC Reviewed; 597 AA.
AC Q3J7R8;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=Noc_2675;
OS Nitrosococcus oceani (strain ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB
OS 11848 / C-107).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Nitrosococcus.
OX NCBI_TaxID=323261;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB 11848 / C-107;
RX PubMed=16957257; DOI=10.1128/aem.00463-06;
RA Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J.,
RA Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M., Poret-Peterson A.T.,
RA Vergez L.M., Ward B.B.;
RT "Complete genome sequence of the marine, chemolithoautotrophic, ammonia-
RT oxidizing bacterium Nitrosococcus oceani ATCC 19707.";
RL Appl. Environ. Microbiol. 72:6299-6315(2006).
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; CP000127; ABA59128.1; -; Genomic_DNA.
DR RefSeq; WP_011331031.1; NC_007484.1.
DR AlphaFoldDB; Q3J7R8; -.
DR SMR; Q3J7R8; -.
DR STRING; 323261.Noc_2675; -.
DR EnsemblBacteria; ABA59128; ABA59128; Noc_2675.
DR KEGG; noc:Noc_2675; -.
DR eggNOG; COG1132; Bacteria.
DR HOGENOM; CLU_000604_84_3_6; -.
DR OMA; FNTLQMG; -.
DR OrthoDB; 643917at2; -.
DR Proteomes; UP000006838; 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; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..597
FT /note="ATP-dependent lipid A-core flippase"
FT /id="PRO_0000271635"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT DOMAIN 29..311
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT DOMAIN 343..579
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
FT BINDING 377..384
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01703"
SQ SEQUENCE 597 AA; 66459 MW; C2F6440E39DCE632 CRC64;
MTFTPSLNSG LAVYRRLLSY TRPYRWIFAA SIITMAIYAA TETGLAALMK PLMDGSFIER
DPATIQIIPL LLIGLFVIRG GANFITQYGL KWVARRVVRD LREQMFCHLL ALPARYYDQK
ASGQLLAKLI YDVEQVSNAA TDAILTIIRD SLTILGLLAW MAYLNGLLTL IILVTAPLIA
LIIWWVSHRF RRISRKIQNS MGDVSQVAQE TIEGHREVKI FGGQTYEAER FDQVNEQNRR
QTMKMAATDA ISQPVVQLIA VLGLAGVIHL ATRESMLAQI SVGTFISFIT AMMLLLGPVK
RLTKINGTLQ RGIAAAQSIF GLLAETPEAD RGQQSLRRAR GAIRFEHLSF CYEPAKGPVL
ENIDLEIKPY QTIALVGHSG SGKSTLVSLL ARFYETTSGR ILIDEMDIQT LRLTELRRQI
ALVSQQIILF NDTIAHNIAY GSYQQTSKQD IIRAAEAAHA MEFINRLPDG LDTVIGEKGV
LLSGGQRQRL AIARALLKDA PILILDEATA SLDTEAERHI QAALETLMRQ RTTLVIAHRL
STVENADQII VLHQGQIIER GTHSQLLARE SHYAGLYRLQ FRHSHEHVSP LSANVGL
