ID   FTRA_EPIFE              Reviewed;         362 AA.
AC   K7ND00;
DT   20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2013, sequence version 1.
DT   25-MAY-2022, entry version 17.
DE   RecName: Full=High affinity iron permease ftrA {ECO:0000303|PubMed:23658520};
GN   Name=ftrA {ECO:0000303|PubMed:23658520};
OS   Epichloe festucae (strain E2368).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Epichloe.
OX   NCBI_TaxID=696363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC   STRAIN=E2368;
RX   PubMed=23658520; DOI=10.1371/journal.ppat.1003332;
RA   Johnson L.J., Koulman A., Christensen M., Lane G.A., Fraser K.,
RA   Forester N., Johnson R.D., Bryan G.T., Rasmussen S.;
RT   "An extracellular siderophore is required to maintain the mutualistic
RT   interaction of Epichloe festucae with Lolium perenne.";
RL   PLoS Pathog. 9:E1003332-E1003332(2013).
CC   -!- FUNCTION: High affinity iron permease; part of the reductive iron
CC       assimilatory system (RIA), a siderophore-independent high affinity iron
CC       uptake mechanism (PubMed:23658520). {ECO:0000305|PubMed:23658520}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Expression is repressed by iron starvation and up-regulated
CC       in the absence of the sidN siderophore synthetase (PubMed:23658520).
CC       {ECO:0000269|PubMed:23658520}.
CC   -!- SIMILARITY: Belongs to the oxidase-dependent Fe transporter (OFeT) (TC
CC       9.A.10.1) family. {ECO:0000305}.
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DR   EMBL; JN132405; AET13877.1; -; Genomic_DNA.
DR   AlphaFoldDB; K7ND00; -.
DR   PhylomeDB; K7ND00; -.
DR   GO; GO:0033573; C:high-affinity iron permease complex; IEA:InterPro.
DR   GO; GO:0005381; F:iron ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR   InterPro; IPR004923; FTR1/Fip1/EfeU.
DR   PANTHER; PTHR31632; PTHR31632; 1.
DR   Pfam; PF03239; FTR1; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Ion transport; Iron; Iron transport; Membrane;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..362
FT                   /note="High affinity iron permease ftrA"
FT                   /id="PRO_0000444442"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        207..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        293..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          326..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..348
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   362 AA;  38841 MW;  B53412AEE6AAFB07 CRC64;
     MAKDVFSVPV FLVVFRETLE TVIIVSVLLA FLKQTLDDGS ERHVKTYKTL RRQVWLGVAA
     GLLVCMIVAA SLIGVFYTVG SNSWENSENY YEGAFCLLAA VIITAMGAAL LRIGKMQAKW
     RVKLARAIES PIKAGTRGCF AHWLEKYAMF VLPFITVLRE GIEAVVFVAG VTFSAPARAV
     PLPVCVGLVV GGLIGWILYK GGSTAKLQMF LVASTCLLYL VAAGLFSRGV WSLEAQKWNI
     AIGGDAAETG SGPGSYDIDN SIWHVNCCSP TAADNGGWGV FNAILGWQNS ATYGSVISYN
     VYWIFVMVGF CTMRFKETKG HYPFAKPKTA DPSVNSRSSS SSQQGVDVGK TAGVEIAGAP
     GA