ID Q07MP6_RHOP5 Unreviewed; 145 AA. AC Q07MP6; DT 31-OCT-2006, integrated into UniProtKB/TrEMBL. DT 31-OCT-2006, sequence version 1. DT 29-MAY-2024, entry version 97. DE RecName: Full=Fluoride-specific ion channel FluC {ECO:0000256|HAMAP-Rule:MF_00454}; GN Name=fluC {ECO:0000256|HAMAP-Rule:MF_00454}; GN Synonyms=crcB {ECO:0000256|HAMAP-Rule:MF_00454}; GN OrderedLocusNames=RPE_2851 {ECO:0000313|EMBL:ABJ06788.1}; OS Rhodopseudomonas palustris (strain BisA53). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Nitrobacteraceae; Rhodopseudomonas. OX NCBI_TaxID=316055 {ECO:0000313|EMBL:ABJ06788.1}; RN [1] {ECO:0000313|EMBL:ABJ06788.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BisA53 {ECO:0000313|EMBL:ABJ06788.1}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Pelletier D.A., Kyrpides N., Kim E., Harwood C.S., Oda Y., RA Richardson P.; RT "Complete sequence of Rhodopseudomonas palustris BisA53."; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Fluoride-specific ion channel. Important for reducing CC fluoride concentration in the cell, thus reducing its toxicity. CC {ECO:0000256|HAMAP-Rule:MF_00454}. 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 -!- ACTIVITY REGULATION: Na(+) is not transported, but it plays an CC essential structural role and its presence is essential for fluoride CC channel function. {ECO:0000256|HAMAP-Rule:MF_00454}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00454}; CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00454}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {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|HAMAP- CC Rule:MF_00454}. 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; CP000463; ABJ06788.1; -; Genomic_DNA. DR AlphaFoldDB; Q07MP6; -. DR STRING; 316055.RPE_2851; -. DR KEGG; rpe:RPE_2851; -. DR eggNOG; COG0239; Bacteria. DR HOGENOM; CLU_114342_3_0_5; -. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0062054; F:fluoride channel activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0140114; P:cellular detoxification of fluoride; IEA:UniProtKB-UniRule. DR HAMAP; MF_00454; FluC; 1. DR InterPro; IPR003691; FluC. DR PANTHER; PTHR28259; FLUORIDE EXPORT PROTEIN 1-RELATED; 1. DR PANTHER; PTHR28259:SF1; FLUORIDE EXPORT PROTEIN 1-RELATED; 1. DR Pfam; PF02537; CRCB; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP- KW Rule:MF_00454}; KW Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|HAMAP- KW Rule:MF_00454}; Ion transport {ECO:0000256|HAMAP-Rule:MF_00454}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00454}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00454}; KW Sodium {ECO:0000256|HAMAP-Rule:MF_00454}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP- KW Rule:MF_00454}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_00454}; Transport {ECO:0000256|HAMAP-Rule:MF_00454}. FT TRANSMEM 12..32 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454" FT TRANSMEM 44..67 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454" FT TRANSMEM 83..100 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454" FT TRANSMEM 112..136 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454" FT BINDING 90 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_note="structural" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454" FT BINDING 93 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_note="structural" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454" SQ SEQUENCE 145 AA; 15655 MW; 0BDFDC6C5AA01BF2 CRC64; MSGARSELRD RAVLYGYIAA GSVIGGWARY LVSVVQTAWL GPGLGFPWAT LFVNVTGSFV IGFYATLTAP DGRVFASSRQ RQLVMTGICG GYTTFSGFSF ETFELLRTDH ALAALINLGI SPVTWLLAVW IGHFAATRLN RLKGS //