PRLL_FUNXX
ID PRLL_FUNXX Reviewed; 495 AA.
AC A0A089FNE5;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 26-NOV-2014, sequence version 1.
DT 25-MAY-2022, entry version 18.
DE RecName: Full=MFS transporter prlL {ECO:0000303|PubMed:25226362};
DE AltName: Full=Pyrrolocin biosynthesis protein L {ECO:0000303|PubMed:25226362};
GN Name=prlL {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; AIP87508.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A089FNE5; -.
DR SMR; A0A089FNE5; -.
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; -; 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; 1.
DR PROSITE; PS50850; MFS; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..495
FT /note="MFS transporter prlL"
FT /id="PRO_0000441313"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..469
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..24
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"
SQ SEQUENCE 495 AA; 54249 MW; ABDF58EF3A98CFC0 CRC64;
MAQSFANEHD PAKRAEERGH VGTIEDVESG TKEPYIAEEP ISAEAARALI WKQDKRIIPL
SAAIYFLCYL DRSNIGNAKI LNAATGNDLL TETHMTNYDY TIALMIFFLA YGLFEVPSNV
LLKKLHPSRW IAILMFSWGA ISMGLAGAHN YATVTVVRFL LGIFEAGLFP GLVYYLTFWY
KTEERSIRVA FILASATLAG AFGGAIAYAV GHMNQAHGIS AWRWLFIIEG APSCVSALFV
LFFLPDYPET VNWLSDEERE LALRRLRVEG SKGLHQSDWW KDAKSTLVEW RLWAHYLIYF
GISTPFSSLS LFTPSITAGL GYDGLQAQLM TVPPYAVAYV VQILVSWSAD RTNSRGLHSA
ASATVGACGF LASAVLPAEA YLHRYGCLIV AAAGAFACIP PLLGWLSSNI FSTASVGLAI
ALNIGLGGAP GQIAGVWIYK ADEAKKGYPT GHWVNAGLLF FVAVACVALR LHYGFRNRKT
VRETGGIEGV RLFKY