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Database: UniProt
Entry: Q4FS42
LinkDB: Q4FS42
Original site: Q4FS42 
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-OCT-2014, entry version 74.
DE   RecName: Full=Lipid A export ATP-binding/permease protein MsbA {ECO:0000255|HAMAP-Rule:MF_01703};
DE            EC=3.6.3.- {ECO:0000255|HAMAP-Rule:MF_01703};
GN   Name=msbA {ECO:0000255|HAMAP-Rule:MF_01703};
GN   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. {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.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Lipid
CC       exporter (TC 3.A.1.106) family. {ECO:0000255|HAMAP-Rule:MF_01703}.
CC   -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain.
CC       {ECO:0000255|HAMAP-Rule:MF_01703}.
CC   -!- SIMILARITY: Contains 1 ABC transporter domain. {ECO:0000255|HAMAP-
CC       Rule:MF_01703}.
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DR   EMBL; CP000082; AAZ19166.1; -; Genomic_DNA.
DR   RefSeq; YP_264600.1; NC_007204.1.
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; NALEMEH; -.
DR   OrthoDB; EOG6T7N3V; -.
DR   BioCyc; PARC259536:GI3A-1348-MONOMER; -.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0034040; F:lipid-transporting ATPase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011527; ABC1_TM_dom.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR011917; ABC_transpr_lipidA.
DR   InterPro; IPR001140; ABC_transptr_TM_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
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; Complete proteome;
KW   Hydrolase; Lipid transport; Membrane; Nucleotide-binding;
KW   Reference proteome; 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. {ECO:0000255|HAMAP-
FT                                Rule:MF_01703}.
FT   TRANSMEM     81    101       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01703}.
FT   TRANSMEM    178    200       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01703}.
FT   TRANSMEM    266    286       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01703}.
FT   DOMAIN       44    326       ABC transmembrane type-1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01703}.
FT   DOMAIN      357    592       ABC transporter. {ECO:0000255|HAMAP-
FT                                Rule:MF_01703}.
FT   NP_BIND     390    397       ATP. {ECO:0000255|HAMAP-Rule:MF_01703}.
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
//
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