ID E5WFM3_9BACI Unreviewed; 136 AA.
AC E5WFM3;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 47.
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=HMPREF1013_01248 {ECO:0000313|EMBL:EFV78382.1};
OS Bacillus sp. 2_A_57_CT2.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=665959 {ECO:0000313|EMBL:EFV78382.1, ECO:0000313|Proteomes:UP000003283};
RN [1] {ECO:0000313|EMBL:EFV78382.1, ECO:0000313|Proteomes:UP000003283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2_A_57_CT2 {ECO:0000313|EMBL:EFV78382.1,
RC ECO:0000313|Proteomes:UP000003283};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacillus sp. strain 2_A_57_CT2.";
RL Submitted (DEC-2010) 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:EFV78382.1}.
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DR EMBL; ACWD01000020; EFV78382.1; -; Genomic_DNA.
DR AlphaFoldDB; E5WFM3; -.
DR eggNOG; COG0239; Bacteria.
DR HOGENOM; CLU_114342_1_2_9; -.
DR Proteomes; UP000003283; 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 Reference proteome {ECO:0000313|Proteomes:UP000003283};
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 12..36
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT TRANSMEM 42..66
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT TRANSMEM 78..101
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT BINDING 84
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
FT BINDING 87
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00454"
SQ SEQUENCE 136 AA; 14531 MW; FB95F6B4ECF5384B CRC64;
MDKLRKKGGI GVVYLLVGAA GFLGASLRYS IGIFLFHESA VFPFATLTVN LLGSFLLAWL
MTGLLVRFSL PAHLKTALGT GFVGSFTTFS TLSVETVTLF LDGKTALAVL YVAASIFGGL
WMSRLGFRVT KGEEAE
//
