ID A0A0B0DE81_9MICC Unreviewed; 143 AA.
AC A0A0B0DE81;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=AS25_11855 {ECO:0000313|EMBL:KHE73579.1};
OS Kocuria marina.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=223184 {ECO:0000313|EMBL:KHE73579.1, ECO:0000313|Proteomes:UP000030664};
RN [1] {ECO:0000313|EMBL:KHE73579.1, ECO:0000313|Proteomes:UP000030664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO9-6 {ECO:0000313|EMBL:KHE73579.1,
RC ECO:0000313|Proteomes:UP000030664};
RA Castro D.B., Pereira L.B., Silva M.V., Silva B.P., Zanardi B.R., Carlos C.,
RA Belgini D.R., Limache E.G., Lacerda G.V., Nery M.B., Gomes M.B., Souza S.,
RA Silva T.M., Rodrigues V.D., Paulino L.C., Vicentini R., Ferraz L.F.,
RA Ottoboni L.M.;
RT "High-quality draft genome sequence of Kocuria marina SO9-6, an
RT actinobacterium isolated from a copper mine.";
RL Submitted (SEP-2014) 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:KHE73579.1}.
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DR EMBL; JROM01000055; KHE73579.1; -; Genomic_DNA.
DR RefSeq; WP_035965344.1; NZ_JROM01000055.1.
DR AlphaFoldDB; A0A0B0DE81; -.
DR STRING; 223184.AS25_11855; -.
DR eggNOG; COG0239; Bacteria.
DR Proteomes; UP000030664; 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}; 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 37..57
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT TRANSMEM 69..88
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT TRANSMEM 108..129
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT BINDING 80
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT BINDING 83
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
SQ SEQUENCE 143 AA; 14738 MW; 49F5C50839E5878A CRC64;
MNRTLTDALL VAAGGAAGSL ARWWVSLVLP AGPGWSWATF AVNASGAFLL GLLLEALTRP
GRERRGAHTT RVLFGTGLLG GFTTYSTFAL ELWERVRSEA SAAAFGDAVL MLVAGLAAAA
AGLAVGAWLR GRRRGTPTAG AAR
//
