ID   MEFA_ENTFL              Reviewed;         323 AA.
AC   P86889;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   25-MAY-2022, entry version 26.
DE   RecName: Full=Macrolide efflux protein A {ECO:0000303|Ref.1};
DE   Flags: Fragment;
GN   Name=mefA;
OS   Enterococcus faecalis (Streptococcus faecalis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1351;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RC   STRAIN=Clinical isolate;
RA   Chouchani C., Marrakchi R., Aboulkacem N., Ferchichi L., Karray A.,
RA   El Salabi A.;
RT   "Involvement of TEM-1 type beta-lactamase and efflux pumps in the defense
RT   mechanisms of Enterococcus faecalis.";
RL   Submitted (JAN-2011) to UniProtKB.
CC   -!- FUNCTION: Confers resistance to 14-membered macrolides including
CC       erythromycin and to 15-membered macrolides but not to 16-membered
CC       macrolides, lincosamides or analogs of streptogramin B. May function as
CC       an efflux pump to regulate intracellular macrolide levels (By
CC       similarity). {ECO:0000250|UniProtKB:P95827}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Drug:H(+)
CC       antiporter-3 (DHA3) (TC 2.A.1.21) family. {ECO:0000305}.
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DR   AlphaFoldDB; P86889; -.
DR   SMR; P86889; -.
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:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   InterPro; IPR004751; Drug_antiport.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   TIGRFAMs; TIGR00900; 2A0121; 1.
DR   PROSITE; PS50850; MFS; 2.
PE   1: Evidence at protein level;
KW   Antibiotic resistance; Cell membrane; Direct protein sequencing; Membrane;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           <1..>323
FT                   /note="Macrolide efflux protein A"
FT                   /id="PRO_0000408962"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        51..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        128..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        182..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        219..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        245..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        270..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        303..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
FT                   /evidence="ECO:0000305"
FT   NON_TER         323
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   323 AA;  34947 MW;  5EF4120A219AA1DE CRC64;
     MGSAMVLSMS LLGFLPYAVF GPAIGVLVDR HDRKKIMIGA DLIIAAAGSV LTIVAFYMEL
     PVWMVMIVLF IRSIGTAFHT PALNAVTPLL VPEEQLTKCA GYSQSLQSIS YIVSPAVAAL
     LYSVWELNAI IAIDVLGAVI ASITVLIVRI PKLGDRVQSL DPNFIREMQE GMAVLRQNKG
     LFALLLVGTL YMFVYMPINA LFPLISMDYF NGTPVHISIT EISFASGMLI GGLLLGLFGN
     YQKRILLITA SIFMMGISLT ISGLLPQSGF FIFVVCSAIM GLSVPFYSGV QTALFQEKIK
     PEYLGRVFSL TGSIMSLAMP IGL