ID B1YHY0_EXIS2 Unreviewed; 133 AA.
AC B1YHY0;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 99.
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 OrderedLocusNames=Exig_0278 {ECO:0000313|EMBL:ACB59764.1};
OS Exiguobacterium sibiricum (strain DSM 17290 / CIP 109462 / JCM 13490 /
OS 255-15).
OC Bacteria; Bacillota; Bacilli; Bacillales;
OC Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX NCBI_TaxID=262543 {ECO:0000313|EMBL:ACB59764.1, ECO:0000313|Proteomes:UP000001681};
RN [1] {ECO:0000313|EMBL:ACB59764.1, ECO:0000313|Proteomes:UP000001681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17290 / CIP 109462 / JCM 13490 / 255-15
RC {ECO:0000313|Proteomes:UP000001681};
RX PubMed=16489412; DOI=10.1007/s00792-005-0497-5;
RA Rodrigues D.F., Goris J., Vishnivetskaya T., Gilichinsky D.,
RA Thomashow M.F., Tiedje J.M.;
RT "Characterization of Exiguobacterium isolates from the Siberian permafrost.
RT Description of Exiguobacterium sibiricum sp. nov.";
RL Extremophiles 10:285-294(2006).
RN [2] {ECO:0000313|EMBL:ACB59764.1, ECO:0000313|Proteomes:UP000001681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17290 / CIP 109462 / JCM 13490 / 255-15
RC {ECO:0000313|Proteomes:UP000001681};
RX PubMed=19019206; DOI=10.1186/1471-2164-9-547;
RA Rodrigues D.F., Ivanova N., He Z., Huebner M., Zhou J., Tiedje J.M.;
RT "Architecture of thermal adaptation in an Exiguobacterium sibiricum strain
RT isolated from 3 million year old permafrost: a genome and transcriptome
RT approach.";
RL BMC Genomics 9:547-547(2008).
RN [3] {ECO:0000313|Proteomes:UP000001681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17290 / CIP 109462 / JCM 13490 / 255-15
RC {ECO:0000313|Proteomes:UP000001681};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C.,
RA Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T.,
RA Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Exiguobacterium sibiricum 255-15.";
RL Submitted (APR-2008) 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 ---------------------------------------------------------------------------
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; CP001022; ACB59764.1; -; Genomic_DNA.
DR RefSeq; WP_012369189.1; NC_010556.1.
DR AlphaFoldDB; B1YHY0; -.
DR STRING; 262543.Exig_0278; -.
DR KEGG; esi:Exig_0278; -.
DR eggNOG; COG0239; Bacteria.
DR HOGENOM; CLU_114342_1_2_9; -.
DR OrthoDB; 9799631at2; -.
DR Proteomes; UP000001681; Chromosome.
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 NCBIfam; TIGR00494; crcB; 1.
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}; 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 Reference proteome {ECO:0000313|Proteomes:UP000001681};
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 32..51
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT TRANSMEM 63..82
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT TRANSMEM 94..119
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT BINDING 74
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT BINDING 77
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
SQ SEQUENCE 133 AA; 14473 MW; 251E2E3F9829D7AE CRC64;
MLYLLVGLAG ILGASARYGL GLLIGNVVVG AFPWTTLTIN LIGCFVLGYA THFLFKTTLL
HQYAMTALGT GFVGSFTTFS TFSVESVELL RAGVYSYAFA YISLSLFGGL LLSYVGYLLG
TRRLRRFQKE EVS
//
