(data stored in ACNUC7421 zone)
SWISSPROT: D6XXI5_BACIE
ID D6XXI5_BACIE Unreviewed; 135 AA.
AC D6XXI5;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 08-MAY-2019, entry version 57.
DE RecName: Full=Putative fluoride ion transporter CrcB {ECO:0000256|HAMAP-Rule:MF_00454};
GN Name=crcB {ECO:0000256|HAMAP-Rule:MF_00454};
GN OrderedLocusNames=Bsel_0506 {ECO:0000313|EMBL:ADH98042.1};
OS Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC unclassified Sporolactobacillaceae.
OX NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH98042.1, ECO:0000313|Proteomes:UP000000271};
RN [1] {ECO:0000313|EMBL:ADH98042.1, ECO:0000313|Proteomes:UP000000271}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC {ECO:0000313|Proteomes:UP000000271};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ovchinnikova G., Stolz J.;
RT "Complete sequence of Bacillus selenitireducens MLS10.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Important for reducing fluoride concentration in the
CC cell, thus reducing its toxicity. {ECO:0000256|HAMAP-
CC Rule:MF_00454, ECO:0000256|SAAS:SAAS00388086}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC Rule:MF_00454}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_00454}.
CC -!- SIMILARITY: Belongs to the CrcB (TC 9.B.71) family.
CC {ECO:0000256|HAMAP-Rule:MF_00454, ECO:0000256|SAAS:SAAS00573618}.
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DR EMBL; CP001791; ADH98042.1; -; Genomic_DNA.
DR STRING; 439292.Bsel_0506; -.
DR EnsemblBacteria; ADH98042; ADH98042; Bsel_0506.
DR KEGG; bse:Bsel_0506; -.
DR eggNOG; COG0239; LUCA.
DR HOGENOM; HOG000052573; -.
DR KO; K06199; -.
DR OMA; CGGFTTM; -.
DR BioCyc; BSEL439292:G1GLR-535-MONOMER; -.
DR Proteomes; UP000000271; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0015103; F:inorganic anion transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00454; CrcB; 1.
DR InterPro; IPR003691; CrcB.
DR PANTHER; PTHR28259; PTHR28259; 1.
DR Pfam; PF02537; CRCB; 1.
PE 3: Inferred from homology;
DR PRODOM; D6XXI5.
DR SWISS-2DPAGE; D6XXI5.
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00454,
KW ECO:0000256|SAAS:SAAS00702610};
KW Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_00454,
KW ECO:0000256|SAAS:SAAS00702614};
KW Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00454,
KW ECO:0000256|SAAS:SAAS00702612};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00454,
KW ECO:0000256|SAAS:SAAS00702611};
KW Transport {ECO:0000256|HAMAP-Rule:MF_00454,
KW ECO:0000256|SAAS:SAAS00702613}.
FT TRANSMEM 7 26 Helical. {ECO:0000256|HAMAP-Rule:
FT MF_00454}.
FT TRANSMEM 32 58 Helical. {ECO:0000256|HAMAP-Rule:
FT MF_00454}.
FT TRANSMEM 70 92 Helical. {ECO:0000256|HAMAP-Rule:
FT MF_00454}.
FT TRANSMEM 104 123 Helical. {ECO:0000256|HAMAP-Rule:
FT MF_00454}.
SQ SEQUENCE 135 AA; 14132 MW; F969F74ACC0B5167 CRC64;
MEKQMFYITI AVFVGGAAGT LLRFFINEWS SMALFPLGTV IENISGSLLL GLLTGWAAYR
YMNPFFKEGL GAGFCGGFTT MSTLMADVTL LATAGGEAVL MTGLYVFVSL AGGLIAAFTG
IVLGERFAGK EGDGA
//
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