ID FLUC4_BRUAB Reviewed; 133 AA. AC Q578U0; DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2005, sequence version 1. DT 27-MAR-2024, entry version 94. DE RecName: Full=Fluoride-specific ion channel FluC 4 {ECO:0000255|HAMAP-Rule:MF_00454}; GN Name=fluC4 {ECO:0000255|HAMAP-Rule:MF_00454}; GN Synonyms=crcB4 {ECO:0000255|HAMAP-Rule:MF_00454}; GN OrderedLocusNames=BruAb2_0415; OS Brucella abortus biovar 1 (strain 9-941). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Brucellaceae; Brucella/Ochrobactrum group; Brucella. OX NCBI_TaxID=262698; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=9-941; RX PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005; RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., RA Li L.-L., Kapur V., Alt D.P., Olsen S.C.; RT "Completion of the genome sequence of Brucella abortus and comparison to RT the highly similar genomes of Brucella melitensis and Brucella suis."; RL J. Bacteriol. 187:2715-2726(2005). CC -!- FUNCTION: Fluoride-specific ion channel. Important for reducing CC fluoride concentration in the cell, thus reducing its toxicity. CC {ECO:0000255|HAMAP-Rule:MF_00454}. CC -!- CATALYTIC ACTIVITY: CC Reaction=fluoride(in) = fluoride(out); Xref=Rhea:RHEA:76159, CC ChEBI:CHEBI:17051; Evidence={ECO:0000255|HAMAP-Rule:MF_00454}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76160; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00454}; 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:0000255|HAMAP-Rule:MF_00454}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00454}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00454}. CC -!- SIMILARITY: Belongs to the fluoride channel Fluc/FEX (TC 1.A.43) CC family. {ECO:0000255|HAMAP-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; AE017224; AAX75844.1; -; Genomic_DNA. DR RefSeq; WP_002965823.1; NC_006933.1. DR AlphaFoldDB; Q578U0; -. DR SMR; Q578U0; -. DR EnsemblBacteria; AAX75844; AAX75844; BruAb2_0415. DR GeneID; 58777343; -. DR KEGG; bmb:BruAb2_0415; -. DR HOGENOM; CLU_114342_3_0_5; -. DR Proteomes; UP000000540; Chromosome II. 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 Pfam; PF02537; CRCB; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Ion channel; Ion transport; Membrane; KW Metal-binding; Sodium; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..133 FT /note="Fluoride-specific ion channel FluC 4" FT /id="PRO_0000110070" FT TRANSMEM 7..27 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00454" FT TRANSMEM 37..57 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00454" FT TRANSMEM 60..80 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00454" FT TRANSMEM 107..127 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00454" FT BINDING 79 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_note="structural" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00454" FT BINDING 82 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_note="structural" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00454" SQ SEQUENCE 133 AA; 14010 MW; D157200B458C63A0 CRC64; MSVEASILVL VGGFIGGVMR FFLSGYVGRR IGETFPWGTF VVNVSGAFVI GTAAGLGARL GGIFSTTIFH EFIMVGLLGG YTTVSSFCLQ SVNLMLDGEQ RQALFNIVAS ALLCVLAVAA GYGGIMWIME WPG //