PRLG_FUNXX
ID PRLG_FUNXX Reviewed; 473 AA.
AC A0A089FRP6;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 26-NOV-2014, sequence version 1.
DT 25-MAY-2022, entry version 17.
DE RecName: Full=MFS transporter prlG {ECO:0000303|PubMed:25226362};
DE AltName: Full=Pyrrolocin biosynthesis protein G {ECO:0000303|PubMed:25226362};
GN Name=prlG {ECO:0000303|PubMed:25226362};
OS Fungal sp. (strain NRRL 50135).
OC Eukaryota; Fungi.
OX NCBI_TaxID=1547289;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=25226362; DOI=10.1021/sb500296p;
RA Kakule T.B., Jadulco R.C., Koch M., Janso J.E., Barrows L.R., Schmidt E.W.;
RT "Native promoter strategy for high-yielding synthesis and engineering of
RT fungal secondary metabolites.";
RL ACS Synth. Biol. 4:625-633(2015).
CC -!- FUNCTION: Efflux pump that might be required for efficient secretion of
CC pyrrolocin or other secondary metabolies produced by the pyrrolocin
CC gene cluster (PubMed:25226362). {ECO:0000305|PubMed:25226362}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KM107910; AIP87507.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A089FRP6; -.
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 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 3: Inferred from homology;
KW Cell membrane; Membrane; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..473
FT /note="MFS transporter prlG"
FT /id="PRO_0000441312"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 473 AA; 51360 MW; 07C24AFADEF0E228 CRC64;
MSSTDAEAKN EEAVDWEGPD DPENPRNWNQ GAKMTHVLLV SSFTLYSNLA AVMFAPGAQD
LVAEFGITST IVASLTVSIY ILGYVFGPFL LASMSEIYGR LIIYHICNAV YIAFTIGCAL
STDTAMFLVF RFICGCAASA PMAIGGGTIA DLHKPEERGK AMALFGLGPL LGPVIGPVVG
GFVTQFLGWR WTFWLVLILA GVVSLLALVL MRETFEPVLL TRKAAELRKS TGNYRLQART
YNKDLTPAQL LARATIRPTK MLLMSPIVFL LSVYCAFMFG LTYLLFTTFP AVFEETYGFA
ADVSGLAYLG LGVGMIISIG LFAVLSDKLL HQPHGGTIAR PELRLILMIW SSPLVPIGFF
WYGWSAKYEV HWIVPILGTS VIGLGAFLIL MPAQLYLVDA FGTEAAASAL AANTVLRSLF
GAVLPLAGPS LYDSLGLGWG NSLLAFIGLA FAPVPFFFYK YGERLRVRFP VNS