ID A0A2A4SEI6_9CHLR Unreviewed; 132 AA.
AC A0A2A4SEI6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=COB68_04075 {ECO:0000313|EMBL:PCI19776.1};
OS SAR202 cluster bacterium.
OC Bacteria; Chloroflexota; SAR202 cluster.
OX NCBI_TaxID=2030829 {ECO:0000313|EMBL:PCI19776.1, ECO:0000313|Proteomes:UP000217661};
RN [1] {ECO:0000313|Proteomes:UP000217661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT "A dynamic microbial community with high functional redundancy inhabits the
RT cold, oxic subseafloor aquifer.";
RL Submitted (AUG-2017) 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 -!- 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-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:PCI19776.1}.
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DR EMBL; NVSQ01000009; PCI19776.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A4SEI6; -.
DR Proteomes; UP000217661; 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: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 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 38..59
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT TRANSMEM 71..89
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT TRANSMEM 101..124
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
SQ SEQUENCE 132 AA; 13849 MW; 0CA6848376E6E167 CRC64;
MEGYELKEAG LVMLGGASGA LTRYMLQQLA LRIGLTGQIG LLTVNVSGSF ALGLLLSFWL
TRTSYPTGLQ LLLAVGFISS YTTFATLMWD SFRLAQNGSV LMALLNLFGS LVAGLGAVAL
GFLAGRLIGQ VA
//
