(data stored in ACNUC29543 zone)

SWISSPROT: A5GQ38_SYNR3

ID   A5GQ38_SYNR3            Unreviewed;       140 AA.
AC   A5GQ38;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 60.
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=SynRCC307_0094 {ECO:0000313|EMBL:CAK26997.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK26997.1, ECO:0000313|Proteomes:UP000001115};
RN   [1] {ECO:0000313|Proteomes:UP000001115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RG   Genoscope;
RL   Submitted (MAY-2006) 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 inner 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; CT978603; CAK26997.1; -; Genomic_DNA.
DR   RefSeq; WP_011934512.1; NC_009482.1.
DR   STRING; 316278.SynRCC307_0094; -.
DR   EnsemblBacteria; CAK26997; CAK26997; SynRCC307_0094.
DR   KEGG; syr:SynRCC307_0094; -.
DR   eggNOG; ENOG41086BQ; Bacteria.
DR   eggNOG; ENOG410XUV1; LUCA.
DR   HOGENOM; HOG000052573; -.
DR   KO; K06199; -.
DR   OMA; HFEPMVP; -.
DR   OrthoDB; 1942863at2; -.
DR   BioCyc; SSP316278:G1GJL-95-MONOMER; -.
DR   Proteomes; UP000001115; 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; A5GQ38.
DR   SWISS-2DPAGE; A5GQ38.
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00454};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00454,
KW   ECO:0000256|SAAS:SAAS00702610};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001115};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00454,
KW   ECO:0000256|SAAS:SAAS00702614};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001115};
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      6     27       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00454}.
FT   TRANSMEM     47     66       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00454}.
FT   TRANSMEM     78     99       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00454}.
FT   TRANSMEM    111    133       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00454}.
SQ   SEQUENCE   140 AA;  15028 MW;  D025305FBEC55845 CRC64;
     MSEVVAPAPF YWEAILVALG AVPGAWLRLR VVNHFEPVVP HKHWGTFFVN VSAAFFLGLF
     SGLHTLQLKA CSGVDGTAPM MLLVGVGFFG SLSTFSTFVV ELLNTLQSRQ FLQFVGLMVF
     SLVIGLLAAA AGYQLGLSHG
//

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