ID A0A240U731_9BURK Unreviewed; 488 AA.
AC A0A240U731; A0A240UHC1;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Trk system potassium uptake protein {ECO:0000256|PIRNR:PIRNR006247};
GN ORFNames=CBP34_18160 {ECO:0000313|EMBL:ART53201.1}, CBP36_17820
GN {ECO:0000313|EMBL:ART60429.1};
OS Acidovorax carolinensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=553814 {ECO:0000313|EMBL:ART53201.1, ECO:0000313|Proteomes:UP000194432};
RN [1] {ECO:0000313|Proteomes:UP000194432, ECO:0000313|Proteomes:UP000194440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA3 {ECO:0000313|EMBL:ART53201.1}, and P4
RC {ECO:0000313|EMBL:ART60429.1};
RA Singleton D.R., Lee J., Dickey A.N., Stroud A., Scholl E.H., Wright F.A.,
RA Aitken M.D.;
RT "Polyphasic characterization of four soil-derived phenanthrene-degrading
RT Acidovorax strains and proposal of Acidovorax phenanthrenivorans sp. nov.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Low-affinity potassium transport system. Interacts with Trk
CC system potassium uptake protein TrkA. {ECO:0000256|PIRNR:PIRNR006247}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429, ECO:0000256|PIRNR:PIRNR006247}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004429,
CC ECO:0000256|PIRNR:PIRNR006247}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the TrkH potassium transport family.
CC {ECO:0000256|ARBA:ARBA00009137, ECO:0000256|PIRNR:PIRNR006247}.
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DR EMBL; CP021361; ART53201.1; -; Genomic_DNA.
DR EMBL; CP021366; ART60429.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A240U731; -.
DR KEGG; acin:CBP34_18160; -.
DR KEGG; acip:CBP36_17820; -.
DR OrthoDB; 9810952at2; -.
DR Proteomes; UP000194432; Chromosome.
DR Proteomes; UP000194440; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015379; F:potassium:chloride symporter activity; IEA:InterPro.
DR InterPro; IPR003445; Cat_transpt.
DR InterPro; IPR004772; TrkH.
DR PANTHER; PTHR32024; TRK SYSTEM POTASSIUM UPTAKE PROTEIN TRKG-RELATED; 1.
DR PANTHER; PTHR32024:SF2; TRK SYSTEM POTASSIUM UPTAKE PROTEIN TRKG-RELATED; 1.
DR Pfam; PF02386; TrkH; 1.
DR PIRSF; PIRSF006247; TrkH; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519,
KW ECO:0000256|PIRNR:PIRNR006247};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|PIRNR:PIRNR006247};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|PIRNR:PIRNR006247};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR006247};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR006247-1};
KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|PIRNR:PIRNR006247};
KW Potassium transport {ECO:0000256|ARBA:ARBA00022538,
KW ECO:0000256|PIRNR:PIRNR006247};
KW Reference proteome {ECO:0000313|Proteomes:UP000194432};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR006247}.
FT TRANSMEM 7..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 37..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 70..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 241..262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 334..357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 396..420
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 458..486
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 115
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|PIRSR:PIRSR006247-1"
FT BINDING 116
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|PIRSR:PIRSR006247-1"
FT BINDING 224
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|PIRSR:PIRSR006247-1"
FT BINDING 225
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|PIRSR:PIRSR006247-1"
FT BINDING 321
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|PIRSR:PIRSR006247-1"
FT BINDING 322
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|PIRSR:PIRSR006247-1"
SQ SEQUENCE 488 AA; 52778 MW; A82DFFDDB5837F07 CRC64;
MVDMFPVLRV LGILVMIFSL SMGLPLAVSL WTGDGVWHVY PLAMAGSLLA GAWLWWRLRL
FRQELQPRHG VMLVSLVWML LPLAAAVPLM LAGHHVGRPM SFTHAYFEAV SGLTTTGSTV
LTGLDSLPVS VNVWRTFLQW MGGMGILILA VAVLPLLGVG GSQLFKAEAA GPLKDTKLTP
RMTGTAKGLW GVYALFSTLC GLAYWAAGMA PLDALMHMFS TVSLGGLSPH DQSFGYFQSP
LLEAICIVFM LVASCNFALY FVAIRKGHWH GFWHDPELRA TLFTLVGGGL LVAALLWVKG
VYAPLDALRH GMFNLVSMAS TTGYATVDYL GWPVFAPVFM LLLSGVATSA GSTGCGIKMV
RMLILLKQAR REMNRLVHPR AVQPVRLGDA VVDNRVIFSV LAFMLVYGAT IFGLSMVLLL
TDLDPVTAFS AVLASVNCAG PGLGAVGPAS NFAVLTDFQI WVCTLAMLLG RLEILSFMAL
LTPAFWRR
//
