ID A0A1X3PBA6_9MICC Unreviewed; 127 AA.
AC A0A1X3PBA6;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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 ORFNames=BCY76_002540 {ECO:0000313|EMBL:OSM44448.1};
OS Nesterenkonia sp. PF2B19.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Nesterenkonia.
OX NCBI_TaxID=1881858 {ECO:0000313|EMBL:OSM44448.1, ECO:0000313|Proteomes:UP000175621};
RN [1] {ECO:0000313|EMBL:OSM44448.1, ECO:0000313|Proteomes:UP000175621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF2B19 {ECO:0000313|EMBL:OSM44448.1,
RC ECO:0000313|Proteomes:UP000175621};
RX PubMed=28408669;
RA Singh P., Kapse N., Roy U., Singh S.M., Dhakephalkar P.K.;
RT "Draft Genome Sequence of Permafrost Bacterium Nesterenkonia sp. Strain
RT PF2B19, Revealing a Cold Adaptation Strategy and Diverse Biotechnological
RT Potential.";
RL Genome Announc. 5:e00133-17(2017).
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:OSM44448.1}.
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DR EMBL; MDSS02000005; OSM44448.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X3PBA6; -.
DR STRING; 1881858.BCY76_002540; -.
DR Proteomes; UP000175621; 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 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 24..45
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT TRANSMEM 66..89
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT TRANSMEM 101..125
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 127 AA; 13114 MW; D68D0A562FB9C7C5 CRC64;
MTVVLGVALG GAAGAVLRLL LDRYARFGIL VANTLGCLLL GFLYGEFSAL TSADAVPDNG
LFSPGVVTVI SYGLIGALST FATVSLRAAQ RWVDGHRMQA AWIWLVNVVC GFVAAGIGMG
LSGLVEL
//
