ID   MLCE_PENCI              Reviewed;         553 AA.
AC   Q8J0F3;
DT   11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Efflux pump mlcE {ECO:0000303|PubMed:12172803};
DE   AltName: Full=Compactin biosynthesis protein E {ECO:0000303|PubMed:12172803};
GN   Name=mlcE {ECO:0000303|PubMed:12172803};
OS   Penicillium citrinum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=5077;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND FUNCTION.
RX   PubMed=12172803; DOI=10.1007/s00438-002-0697-y;
RA   Abe Y., Suzuki T., Ono C., Iwamoto K., Hosobuchi M., Yoshikawa H.;
RT   "Molecular cloning and characterization of an ML-236B (compactin)
RT   biosynthetic gene cluster in Penicillium citrinum.";
RL   Mol. Genet. Genomics 267:636-646(2002).
RN   [2]
RP   FUNCTION.
RX   PubMed=12242508; DOI=10.1007/s00438-002-0736-8;
RA   Abe Y., Suzuki T., Mizuno T., Ono C., Iwamoto K., Hosobuchi M.,
RA   Yoshikawa H.;
RT   "Effect of increased dosage of the ML-236B (compactin) biosynthetic gene
RT   cluster on ML-236B production in Penicillium citrinum.";
RL   Mol. Genet. Genomics 268:130-137(2002).
RN   [3]
RP   BIOTECHNOLOGY.
RX   PubMed=1010803; DOI=10.7164/antibiotics.29.1346;
RA   Endo A., Kuroda M., Tsujita Y.;
RT   "ML-236A, ML-236B, and ML-236C, new inhibitors of cholesterogenesis
RT   produced by Penicillium citrinium.";
RL   J. Antibiot. 29:1346-1348(1976).
CC   -!- FUNCTION: Efflux pump; part of the gene cluster that mediates the
CC       biosynthesis of compactin, also known as mevastatin or ML-236B, and
CC       which acts as a potent competitive inhibitor of HMG-CoA reductase
CC       (PubMed:12172803, PubMed:12242508). {ECO:0000269|PubMed:12172803,
CC       ECO:0000269|PubMed:12242508}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- BIOTECHNOLOGY: Compactin (also known as mevastatin or ML-236B) and the
CC       intermediary metabolites Ml-236C and ML-236A are inhibitors of HMG-CoA
CC       reductase involved in cholesterogenesis (PubMed:1010803). Their
CC       hypocholesterolemic activity might be useful for lowering cholesterol
CC       levels in the blood and reduce artherosclerosis and coronary heart
CC       disease (PubMed:1010803). {ECO:0000269|PubMed:1010803}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet
CC       family. {ECO:0000305}.
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DR   EMBL; AB072893; BAC20568.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8J0F3; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   Gene3D; 1.20.1250.20; -; 2.
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; 2.
DR   PROSITE; PS50850; MFS; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..553
FT                   /note="Efflux pump mlcE"
FT                   /id="PRO_0000436294"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        77..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        101..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        196..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        245..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        273..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        319..339
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        352..372
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        376..396
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        440..460
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        516..536
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        21
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        543
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   553 AA;  58691 MW;  D3F7C9DD4417748D CRC64;
     MSEPLPPKEG EPRPQKEESQ NDTLEATESK SQHITGLKLG LVVASVTFVA FLMLLDMSII
     VTAIPHITSE FHSLNDVGWY GSAYLLANCA LQPLAGKLYT LLGLKYTFFA FLCIFELGSV
     LCGAARSSTM LIVGRAVAGM GGSGLVNGAL TILSTAAPKH KQPVLIGVMM GLSQIAIVCG
     PLLGGAFTQH ATWRWCFYIN LPIGAVAAFL LLVITIPDRI SSTDSELSTD KPMANIKSTL
     RKLDLVGFVV FAAFATMISL ALEWGGSTYT WRSSVIIGLF CGGGFALIAF VLWERHVGDA
     VAMIPGSVAG KRQVWCSCLF MGFFSGSLLV FSYYLPIYFQ AVKDVSPTLS GVYMLPGILG
     QVIMAMVSGF AIGKTGYYLP WALGSAVLVA IGAGLVSTFQ PHTSTVKWVM YQFIAGFGRG
     CGMQTPIIAI QSTLSPEQGA LGISLAVFGQ TFGGSLFLDF ANLVFGSGLR TGLSKYAPTV
     DTQAVTAAGA TGFRDVVSKN NLPGVVKAYS LAVDHTFYLA VGATACTFVF AFGMGWRKIA
     TKNDTRAVPE TDA