ID Y1956_STAAR Reviewed; 578 AA.
AC Q6GFJ1;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 29-MAY-2013, entry version 72.
DE RecName: Full=Putative multidrug export ATP-binding/permease protein SAR1956;
DE EC=3.6.3.-;
GN OrderedLocusNames=SAR1956;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T.,
RA Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L.,
RA Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K.,
RA James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K.,
RA Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M.,
RA Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G.,
RA Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains:
RT evidence for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC -!- FUNCTION: May be involved in multidrug export. Transmembrane
CC domains (TMD) form a pore in the cell membrane and the ATP-binding
CC domain (NBD) is responsible for energy generation (By similarity).
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC (By similarity).
CC -!- DOMAIN: The ATP-binding domain (NBD) and the transmembrane domain
CC (TMD) are fused.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily.
CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain.
CC -!- SIMILARITY: Contains 1 ABC transporter domain.
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DR EMBL; BX571856; CAG40943.1; -; Genomic_DNA.
DR RefSeq; YP_041331.1; NC_002952.2.
DR ProteinModelPortal; Q6GFJ1; -.
DR SMR; Q6GFJ1; 1-578.
DR STRING; 282458.SAR1956; -.
DR EnsemblBacteria; CAG40943; CAG40943; SAR1956.
DR GeneID; 2861198; -.
DR KEGG; sar:SAR1956; -.
DR PATRIC; 19547547; VBIStaAur71814_1963.
DR eggNOG; COG1132; -.
DR KO; K11085; -.
DR OMA; FFFGRLR; -.
DR ProtClustDB; CLSK872876; -.
DR BioCyc; SAUR282458:GJA5-1990-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:0042626; F:ATPase activity, coupled to transmembrane movement of substances; 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; IPR001140; ABC_transptr_TM_dom.
DR InterPro; IPR011527; ABC_transptrTM_dom_typ1.
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; SSF90123; ABC_TM_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Complete proteome; Hydrolase; Membrane;
KW Nucleotide-binding; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1 578 Putative multidrug export ATP-
FT binding/permease protein SAR1956.
FT /FTId=PRO_0000271551.
FT TOPO_DOM 1 15 Cytoplasmic (Potential).
FT TRANSMEM 16 36 Helical; (Potential).
FT TOPO_DOM 37 59 Extracellular (Potential).
FT TRANSMEM 60 80 Helical; (Potential).
FT TOPO_DOM 81 138 Cytoplasmic (Potential).
FT TRANSMEM 139 159 Helical; (Potential).
FT TOPO_DOM 160 162 Extracellular (Potential).
FT TRANSMEM 163 183 Helical; (Potential).
FT TOPO_DOM 184 244 Cytoplasmic (Potential).
FT TRANSMEM 245 263 Helical; (Potential).
FT TOPO_DOM 264 269 Extracellular (Potential).
FT TRANSMEM 270 287 Helical; (Potential).
FT TOPO_DOM 288 578 Cytoplasmic (Potential).
FT DOMAIN 16 306 ABC transmembrane type-1.
FT DOMAIN 340 575 ABC transporter.
FT NP_BIND 374 381 ATP (Potential).
SQ SEQUENCE 578 AA; 64863 MW; 0DA5945AE8F1799C CRC64;
MIKRYLQFVK PYKYRIFATI IVGIIKFGIP MLIPLLIKYA IDGVINNHAL TTDEKVHHLT
IAIGIALFIF VIVRPPIEFI RQYLAQWTSN KILYDIRKKL YNHLQALSAR FYANNQVGQV
ISRVINDVEQ TKDFILTGLM NIWLDCITII IALSIMFFLD VKLTLAALFI FPFYILTVYV
FFGRLRKLTR ERSQALAEVQ GFLHERVQGI SVVKSFAIED NEAKNFDKKN TNFLTRALKH
TRWNAYSFAA INTVTDIGPI IVIGVGAYLA ISGSITVGTL AAFVGYLELL FGPLRRLVAS
FTTLTQSFAS MDRVFQLIDE DYDIKNGVGA QPIEIKQGRI DIDHVSFQYN DNEAPILKDI
NLSIEKGETV AFVGMSGGGK STLINLIPRF YDVTSGQILI DGHNIKDFLT GSLRNQIGLV
QQDNILFSDT VKENILLGRP TATDEEVVEA AKMANAHDFI MNLPQGYDTE VGERGVKLSG
GQKQRLSIAR IFLNNPPILI LDEATSALDL ESESIIQEAL DVLSKDRTTL IVAHRLSTIT
HADKIVVIEN GHIVETGTHR ELIAKQGAYE HLYSIQNL
//
