MEPA_STAAW
ID MEPA_STAAW Reviewed; 451 AA.
AC Q8NYB0;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Multidrug export protein MepA;
GN Name=mepA; OrderedLocusNames=MW0311;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
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; BA000033; BAB94176.1; -; Genomic_DNA.
DR RefSeq; WP_000651054.1; NC_003923.1.
DR AlphaFoldDB; Q8NYB0; -.
DR SMR; Q8NYB0; -.
DR EnsemblBacteria; BAB94176; BAB94176; BAB94176.
DR KEGG; sam:MW0311; -.
DR HOGENOM; CLU_012893_0_1_9; -.
DR OMA; MDGIWLA; -.
DR Proteomes; UP000000418; Chromosome.
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_0000290232"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
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 397..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 451 AA; 48876 MW; CF65343BB2816704 CRC64;
MKDEQLYYFE KSPVFKAMMH FSLPMMIGTL LSVIYGILNI YFIGFLEDSH MISAISLTLP
VFAILMGLGN LFGVGAGTYI SRLLGAKDYS KSKFVSSFSI YGGIALGLIV ILVTLPFSDQ
IAAILGARGE TLALTSNYLK VMFLSAPFVI LFFILEQFAR AIGAPMISMI GMLASVGLNI
ILDPILIFGF DLNVVGAALG TAISNVAAAL FFIVYFMKNS DVVSVNIKLA KPNKEMLSEI
FKIGIPAFLM SILMGFTGLV LNLFLAHYGN FAIASYGISF RLVQFPELII MGLCEGVVPL
IAYNFMANKG RMKDVIKAVI MSIGVIFVVC MIAVFTIGHH MVGLFTTDQD IVEMATFILK
VTMTSLLLNG IGFLFTGMLQ ATGQGRGATI MAILQGAIII PVLFIMNALF GLTGVIWSLL
IAESLCALAA MLIVYLLRDR LTVDTSELIE G