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 27-MAR-2024, entry version 118.
DE RecName: Full=Putative multidrug export ATP-binding/permease protein SAR1956;
DE EC=7.6.2.-;
GN OrderedLocusNames=SAR1956;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC 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., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT 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 domains
CC (TMD) form a pore in the cell membrane and the ATP-binding domain (NBD)
CC is responsible for energy generation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- DOMAIN: The ATP-binding domain (NBD) and the transmembrane domain (TMD)
CC are fused.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; BX571856; CAG40943.1; -; Genomic_DNA.
DR RefSeq; WP_000597238.1; NC_002952.2.
DR AlphaFoldDB; Q6GFJ1; -.
DR SMR; Q6GFJ1; -.
DR KEGG; sar:SAR1956; -.
DR HOGENOM; CLU_000604_84_3_9; -.
DR Proteomes; UP000000596; Chromosome.
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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd18554; ABC_6TM_Sav1866_like; 1.
DR CDD; cd03251; ABCC_MsbA; 1.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221:SF658; ABC TRANSPORTER B FAMILY MEMBER 29, CHLOROPLASTIC; 1.
DR PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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; Membrane; Nucleotide-binding; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..578
FT /note="Putative multidrug export ATP-binding/permease
FT protein SAR1956"
FT /id="PRO_0000271551"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 37..59
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 81..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 160..162
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 184..244
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..263
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 264..269
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..287
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 288..578
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 16..306
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 340..575
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 374..381
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
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
//
