ID A0A2A3Y7P6_9MICC Unreviewed; 136 AA.
AC A0A2A3Y7P6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Fluoride-specific ion channel {ECO:0000256|RuleBase:RU004340};
GN ORFNames=CIK74_11740 {ECO:0000313|EMBL:PCC33845.1};
OS Glutamicibacter sp. BW77.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Glutamicibacter.
OX NCBI_TaxID=2024402 {ECO:0000313|EMBL:PCC33845.1, ECO:0000313|Proteomes:UP000218926};
RN [1] {ECO:0000313|EMBL:PCC33845.1, ECO:0000313|Proteomes:UP000218926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BW77 {ECO:0000313|EMBL:PCC33845.1,
RC ECO:0000313|Proteomes:UP000218926};
RX PubMed=28644126;
RA Bonham K.S., Wolfe B.E., Dutton R.J.;
RT "Extensive horizontal gene transfer in cheese-associated bacteria.";
RL Elife 6:e22144-e22144(2017).
CC -!- FUNCTION: Important for reducing fluoride concentration in the cell,
CC thus reducing its toxicity. {ECO:0000256|RuleBase:RU004340}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=fluoride(in) = fluoride(out); Xref=Rhea:RHEA:76159,
CC ChEBI:CHEBI:17051; Evidence={ECO:0000256|ARBA:ARBA00035585};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76160;
CC Evidence={ECO:0000256|ARBA:ARBA00035585};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the fluoride channel Fluc/FEX (TC 1.A.43)
CC family. {ECO:0000256|ARBA:ARBA00035120, ECO:0000256|RuleBase:RU004340}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PCC33845.1}.
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DR EMBL; NRGT01000069; PCC33845.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3Y7P6; -.
DR OrthoDB; 5148600at2; -.
DR Proteomes; UP000218926; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:1903425; F:fluoride transmembrane transporter activity; IEA:UniProt.
DR InterPro; IPR003691; FluC.
DR Pfam; PF02537; CRCB; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU004340};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023303};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU004340};
KW Reference proteome {ECO:0000313|Proteomes:UP000218926};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU004340};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU004340}; Transport {ECO:0000256|ARBA:ARBA00023303}.
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004340"
FT TRANSMEM 81..102
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004340"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004340"
SQ SEQUENCE 136 AA; 14627 MW; AE1C64C8444E8493 CRC64;
MIWLLLLAGA IGAMIRYLLD RSLPATHDLA QGLFAGWPRG ILLANILGSF ALGVVLGYAR
SHQLDLTHEN FVHTIPAADR LWLLASGVCG SLTTASTLFV GFRLIYEVNK ARAIVYLCST
FVIAGGAGAL GWLMTR
//
