ID F2CCR8_STRSA Unreviewed; 124 AA. AC F2CCR8; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 08-NOV-2023, entry version 41. DE RecName: Full=Fluoride-specific ion channel FluC {ECO:0000256|HAMAP-Rule:MF_00454}; GN Name=crcB2 {ECO:0000313|EMBL:EGF19828.1}; GN Synonyms=crcB {ECO:0000256|HAMAP-Rule:MF_00454}, fluC GN {ECO:0000256|HAMAP-Rule:MF_00454}; GN ORFNames=HMPREF9391_0548 {ECO:0000313|EMBL:EGF19828.1}; OS Streptococcus sanguinis SK408. OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=888818 {ECO:0000313|EMBL:EGF19828.1, ECO:0000313|Proteomes:UP000004826}; RN [1] {ECO:0000313|EMBL:EGF19828.1, ECO:0000313|Proteomes:UP000004826} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SK408 {ECO:0000313|EMBL:EGF19828.1, RC ECO:0000313|Proteomes:UP000004826}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V., RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G., RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A., RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (FEB-2011) 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 -!- 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:EGF19828.1}. 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; AFBE01000002; EGF19828.1; -; Genomic_DNA. DR RefSeq; WP_002917150.1; NZ_GL878559.1. DR AlphaFoldDB; F2CCR8; -. DR EnsemblBacteria; EGF19828; EGF19828; HMPREF9391_0548. DR PATRIC; fig|888818.3.peg.532; -. DR HOGENOM; CLU_114342_3_3_9; -. DR Proteomes; UP000004826; Unassembled WGS sequence. 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; CrcB; 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}; KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP- KW 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}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00454}. FT TRANSMEM 7..30 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454" FT TRANSMEM 36..54 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454" FT TRANSMEM 66..85 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454" FT TRANSMEM 100..119 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454" FT BINDING 76 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_note="structural" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454" FT BINDING 79 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_note="structural" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454" SQ SEQUENCE 124 AA; 13260 MW; 4D53253598957D72 CRC64; MKEVQNSIAV ALSAMVGGWL RYQIALLLVV ADSFPLGTLL VNYLGTFLLV YIIKGYLSSK VKSQRLILAL STGFCGGLTT FSGLLLDSIK LADSGRYMEL LIYLVLSVGG GLAIALWAGK QVKS //