ID   VRTL_PENAE              Reviewed;         503 AA.
AC   D7PHY8;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   25-MAY-2022, entry version 26.
DE   RecName: Full=Efflux pump vrtL {ECO:0000303|PubMed:20534346};
DE   AltName: Full=Viridicatumtoxin synthesis protein L {ECO:0000303|PubMed:20534346};
GN   Name=vrtL {ECO:0000303|PubMed:20534346};
OS   Penicillium aethiopicum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=36650;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=IBT 5753;
RX   PubMed=20534346; DOI=10.1016/j.chembiol.2010.03.015;
RA   Chooi Y.H., Cacho R., Tang Y.;
RT   "Identification of the viridicatumtoxin and griseofulvin gene clusters from
RT   Penicillium aethiopicum.";
RL   Chem. Biol. 17:483-494(2010).
RN   [2]
RP   BIOTECHNOLOGY.
RX   PubMed=19168978; DOI=10.1038/ja.2008.84;
RA   Zheng C.J., Yu H.E., Kim E.H., Kim W.G.;
RT   "Viridicatumtoxin B, a new anti-MRSA agent from Penicillium sp. FR11.";
RL   J. Antibiot. 61:633-637(2008).
RN   [3]
RP   BIOTECHNOLOGY.
RX   PubMed=27049441; DOI=10.1038/ja.2016.35;
RA   Inokoshi J., Nakamura Y., Komada S., Komatsu K., Umeyama H., Tomoda H.;
RT   "Inhibition of bacterial undecaprenyl pyrophosphate synthase by small
RT   fungal molecules.";
RL   J. Antibiot. 69:798-805(2016).
CC   -!- FUNCTION: Efflux pump; part of the gene cluster that mediates the
CC       biosynthesis of viridicatumtoxin, a tetracycline-like fungal
CC       meroterpenoid with a unique, fused spirobicyclic ring system
CC       (PubMed:20534346). {ECO:0000269|PubMed:20534346}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- BIOTECHNOLOGY: Viridicatumtoxin and its derivative, viridicatumtoxin B,
CC       exhibit anti-methicillin-resistant Staphylococcus aureus (anti-MRSA)
CC       activity (PubMed:19168978). Moreover, viridicatumtoxin and a C2 acetyl
CC       analog, spirohexaline, have been demonstrated to inhibit bacterial
CC       undecaprenyl diphosphate synthase, a potential new target for
CC       antibiotic development (PubMed:27049441). {ECO:0000269|PubMed:19168978,
CC       ECO:0000269|PubMed:27049441}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC       {ECO:0000305}.
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DR   EMBL; GU574477; ADI24938.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7PHY8; -.
DR   SMR; D7PHY8; -.
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; -; 1.
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   PROSITE; PS50850; MFS; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Membrane; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..503
FT                   /note="Efflux pump vrtL"
FT                   /id="PRO_0000436819"
FT   TRANSMEM        68..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        101..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        133..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        221..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        295..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        329..349
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        377..397
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        401..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        432..454
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        471..491
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        7
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   503 AA;  55280 MW;  C2C3C15044844D66 CRC64;
     MSKLSDNHSS ASEGEKEAGD LESGPTAISS EPSFDDADRD PNLITWDGPK DPENPKNWPK
     GLRWKNTWTV SLFVFISPVS SSMIAPAMSD LAKSLGMHAE IEIYLSLSIF ILAYSIGPIF
     FGPASELYGR VRLLQISNVW YLAWNLGCGF ATTKGQLFAF RFLAGIGGSA PLAIGGGAIS
     DMWTAEERGK AMGVYTLGPL LGPVVGPIAG GFIAEYSTWR WVFWSTSAAA LAVQVVGFFW
     LQECHPGTLL RKRRDRLAKE TGNENLHTAE KVETLGYKLL HAFERPVKMF TTQPIVFCMA
     IYMAYLFGIS YLMFATFPEI WTVVYHESPG IGGLNYLSIA IGSFIGLFFN LKLVDRIYRS
     LKARNNGVGK PEYRMPSLAV GSVISTIGLF WYGWSIGNTH WIMPNIGALI FAMGTISCLQ
     GMQTYIVDSY QTYAASAMAA CAVLRSLCGF GFPLFAPYMY NSLGYGWGTS LLAFITMVVG
     WGAPFAFWHF GPRLRAMSKY ASG