ID MSBA_PSYA2 Reviewed; 595 AA.
AC Q4FS42;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 01-MAY-2013, entry version 66.
DE RecName: Full=Lipid A export ATP-binding/permease protein MsbA;
DE EC=3.6.3.-;
GN Name=msbA; OrderedLocusNames=Psyc_1316;
OS Psychrobacter arcticus (strain DSM 17307 / 273-4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Moraxellaceae; Psychrobacter.
OX NCBI_TaxID=259536;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17307 / 273-4;
RX PubMed=20154119; DOI=10.1128/AEM.02101-09;
RA Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A.,
RA Ivanova N., Bergholz P.W., Di Bartolo G., Hauser L., Land M.,
RA Bakermans C., Rodrigues D., Klappenbach J., Zarka D., Larimer F.,
RA Richardson P., Murray A., Thomashow M., Tiedje J.M.;
RT "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive
RT Siberian permafrost bacterium, reveals mechanisms for adaptation to
RT low-temperature growth.";
RL Appl. Environ. Microbiol. 76:2304-2312(2010).
CC -!- FUNCTION: Involved in lipid A export and possibly also in
CC glycerophospholipid export and for biogenesis of the outer
CC membrane. Transmembrane domains (TMD) form a pore in the inner
CC membrane and the ATP-binding domain (NBD) is responsible for
CC energy generation (By similarity).
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC protein (Potential).
CC -!- DOMAIN: In MsbA the ATP-binding domain (NBD) and the transmembrane
CC domain (TMD) are fused.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Lipid
CC exporter (TC 3.A.1.106) family.
CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain.
CC -!- SIMILARITY: Contains 1 ABC transporter domain.
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DR EMBL; CP000082; AAZ19166.1; -; Genomic_DNA.
DR RefSeq; YP_264600.1; NC_007204.1.
DR HSSP; Q7RBT4; 2GHI.
DR ProteinModelPortal; Q4FS42; -.
DR STRING; 259536.Psyc_1316; -.
DR EnsemblBacteria; AAZ19166; AAZ19166; Psyc_1316.
DR GeneID; 3515273; -.
DR KEGG; par:Psyc_1316; -.
DR PATRIC; 23057263; VBIPsyArc98534_1548.
DR eggNOG; COG1132; -.
DR KO; K11085; -.
DR OMA; TEIWIAK; -.
DR ProtClustDB; CLSK830658; -.
DR BioCyc; PARC259536:GI3A-1383-MONOMER; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0034040; F:lipid-transporting ATPase activity; IEA:InterPro.
DR GO; GO:0006200; P:ATP catabolic process; IEA:GOC.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like.
DR InterPro; IPR017871; ABC_transporter_CS.
DR InterPro; IPR017940; ABC_transporter_type1.
DR InterPro; IPR011917; ABC_transpr_lipidA.
DR InterPro; IPR001140; ABC_transptr_TM_dom.
DR InterPro; IPR011527; ABC_transptrTM_dom_typ1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF90123; ABC_TM_1; 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; Complete proteome;
KW Hydrolase; Lipid transport; Membrane; Nucleotide-binding;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1 595 Lipid A export ATP-binding/permease
FT protein MsbA.
FT /FTId=PRO_0000271644.
FT TRANSMEM 41 61 Helical; (Potential).
FT TRANSMEM 81 101 Helical; (Potential).
FT TRANSMEM 178 200 Helical; (Potential).
FT TRANSMEM 266 286 Helical; (Potential).
FT DOMAIN 44 326 ABC transmembrane type-1.
FT DOMAIN 357 592 ABC transporter.
FT NP_BIND 390 397 ATP (Potential).
SQ SEQUENCE 595 AA; 65482 MW; FAE053A4611B084A CRC64;
MSQAYQPDST KTSAKKSSAV TLNPPKRKTL MRLLAYLKPY WWAILLTITG FAINAGTEIW
IAKLLQYITD AINQNDQSKQ GLFPFIIVML FFVRGVGSFL GNYYTALVSR NLVYELRVEV
FNKLLRLPSS FYLANPAGTI SSKLIFDVEQ VTAASTDSLK TLLRDGLTVI ALMGFLLYSN
WRLTLILFVV LPPILWIIRV ASKRYLKLSK GIQATMGGVS HITNEVINGY QVVKNYGGQA
YESKRFDEVS KKNLRQGMKI VVTNSINTPA VQLLMAVAMA VVVWLALRPA VIDDISAGQF
ISYIAAAGLL SKPVRSLTDV NQQLQRGIAA GESIFALLDE PEEEDTGVLS PALVGEIKLD
NISLVYPDST VALHDFNLDI RAGETVALVG RSGAGKSSLV NLLTRTLSTS SGQITLDGMP
IEDIKLESLR AQIAMVNQQV VLFNTTVFNN IAYGSLAHKT PAEVEQAAKD AFAHDFIMQM
PNGYQSEIGA EGLQLSGGQR QRLSIARALL KDAPILILDE ATSALDNESE YYIQKALDNI
MRNRTTLVIA HRLTTIESAD RIAVLDGGRI VELGTHAELM QLHGHYAQMY ARDFE
//
