ID F0I6Z6_STRSA Unreviewed; 108 AA. AC F0I6Z6; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 24-JUL-2024, entry version 41. DE RecName: Full=Fluoride-specific ion channel FluC {ECO:0000256|HAMAP-Rule:MF_00454}; GN Name=crcB1 {ECO:0000313|EMBL:EGD31626.1}; GN Synonyms=crcB {ECO:0000256|HAMAP-Rule:MF_00454}, fluC GN {ECO:0000256|HAMAP-Rule:MF_00454}; GN ORFNames=HMPREF9382_0579 {ECO:0000313|EMBL:EGD31626.1}; OS Streptococcus sanguinis SK115. OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=888810 {ECO:0000313|EMBL:EGD31626.1, ECO:0000313|Proteomes:UP000003351}; RN [1] {ECO:0000313|EMBL:EGD31626.1, ECO:0000313|Proteomes:UP000003351} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SK115 {ECO:0000313|EMBL:EGD31626.1, RC ECO:0000313|Proteomes:UP000003351}; 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:EGD31626.1}. 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; AEXW01000005; EGD31626.1; -; Genomic_DNA. DR RefSeq; WP_002906450.1; NZ_GL872408.1. DR AlphaFoldDB; F0I6Z6; -. DR PATRIC; fig|888810.3.peg.561; -. DR HOGENOM; CLU_114342_2_3_9; -. DR Proteomes; UP000003351; 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; 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}; 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 30..48 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454" FT TRANSMEM 55..75 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454" FT TRANSMEM 87..107 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454" FT BINDING 65 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_note="structural" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454" FT BINDING 68 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_note="structural" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454" SQ SEQUENCE 108 AA; 11967 MW; 3CA2DE9B0C0790E3 CRC64; MMWAILICCG AGSLVRYVFS KVNSRAYLPI GTLLANLLGA FLIGYFYNHI EDKQLYVILA TGFCGGLTTF STLNAELAAL FPERKKFLLY LALTYILGFL AILLGIFI //