ID   Y1799_STAAB             Reviewed;         578 AA.
AC   Q2YU20;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Putative multidrug export ATP-binding/permease protein SAB1799c;
DE            EC=7.6.2.-;
GN   OrderedLocusNames=SAB1799c;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
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; AJ938182; CAI81488.1; -; Genomic_DNA.
DR   RefSeq; WP_000597234.1; NC_007622.1.
DR   AlphaFoldDB; Q2YU20; -.
DR   SMR; Q2YU20; -.
DR   KEGG; sab:SAB1799c; -.
DR   HOGENOM; CLU_000604_84_3_9; -.
DR   OMA; TMTERFN; -.
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   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; 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   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 SAB1799c"
FT                   /id="PRO_0000271547"
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..242
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        243..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        263..267
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        268..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;  64934 MW;  9A82BE6CD14D0350 CRC64;
     MIKRYLQFVK PYKYRIFATI IVGIIKFGIP MLIPLLIKYA IDGVINNHAL TTDEKVHHLT
     IAIGIALFIF VIVRPPIEFI RQYLAQWTSN KILYDIRKKL YNHLQALSAR FYANNQVGQV
     ISRVINDVEQ TKDFILTGLM NIWLDCITII IALSIMFFLD VKLTLAALFI FPFYILTVYV
     FFGRLRKLTR ERSQALAEVQ GFLHERVQGI SVVKSFAIED NEAKNFDKKN ANFLTRALKH
     TRWNAYSFAT INTVTDIGPI IVIGVGAYLA ISGSITVGTL AAFVGYLELL FGPLRRLVAS
     FTTLTQSFAS MDRVFQLIDE DYDIKNGVGA QPIEIKQGRI DIYHVNFQYN DNEAPILKDI
     NLSIEKGETV AFVGMSGGGK STLINLIPRF YDVTSGQILI DGHNIKDFLT GSLRNQIGLV
     QQDNILFSDT VKENILLGRP TATDEEVVEV AKVANAHDFI MNLPQGYDTE VGERGVKLSG
     GQKQRLSIAR IFLNNPPILI LDEATSALDL ESESIIQEAL DVLSKDRTTL IVAHRLSTIT
     HADKIVVIEN GHIVETGTHR ELIAKQGAYE HLYSIQNL