ID   MEPA_STAAB              Reviewed;         451 AA.
AC   Q2YVH4;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Multidrug export protein MepA;
GN   Name=mepA; OrderedLocusNames=SAB0284;
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: Multidrug resistance efflux protein. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC
CC       2.A.66.1) family. MepA subfamily. {ECO:0000305}.
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DR   EMBL; AJ938182; CAI79972.1; -; Genomic_DNA.
DR   RefSeq; WP_000651036.1; NC_007622.1.
DR   AlphaFoldDB; Q2YVH4; -.
DR   SMR; Q2YVH4; -.
DR   KEGG; sab:SAB0284; -.
DR   HOGENOM; CLU_012893_0_1_9; -.
DR   OMA; MDGIWLA; -.
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:0015297; F:antiporter activity; IEA:InterPro.
DR   GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   CDD; cd13143; MATE_MepA_like; 1.
DR   InterPro; IPR002528; MATE_fam.
DR   InterPro; IPR045070; MATE_MepA-like.
DR   Pfam; PF01554; MatE; 2.
DR   PIRSF; PIRSF006603; DinF; 1.
DR   TIGRFAMs; TIGR00797; matE; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Cell membrane; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..451
FT                   /note="Multidrug export protein MepA"
FT                   /id="PRO_0000290227"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        245..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        282..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        318..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        355..375
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        390..410
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        417..437
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   451 AA;  48952 MW;  0EF2991D994EA080 CRC64;
     MKDEQLYYFE KSPVFKAMMH FSLPMMIGTL LSVIYGILNI YFIGFLEDSH MISAISLTLP
     VFAILMGLGN LFDVGAGTYI SRLLGAKDYS KSKFVSSFSI YGGIALGLIV ILVALPFSDQ
     IAAILGARGE TLALTSNYLK VMFLSAPFVI LFFILEQFAR AIGAPMISMI GMLASVSLNI
     ILDPILIFGF DLNVVGAALG TAISNVAAAL FFIIYFMKNS DVVSVNIKLA KPNKEMLSEI
     FKIGIPAFLM SILMGFTGLV LNLFLAHYGN FAIASYGISF RLVQFPELII MGLCEGVVPL
     IAYNFMSNKG RMKDVIKAVI MSIGVIFVVC MIAVFTIGHH MVGLFTTDQA IVEMATFILK
     VTMTSLLLNG IGFLFTGMLQ ATGQGRGATI MAILQGVVII PVLFIMNALF GLTGVMWSLL
     IAESLCALAA MLIVYLLRDR LTVDTSELIE G