ID A0A132C123_9RHOB Unreviewed; 482 AA.
AC A0A132C123;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Trk system potassium uptake protein {ECO:0000256|PIRNR:PIRNR006247};
GN Name=trkH {ECO:0000313|EMBL:KUP94278.1};
GN ORFNames=TRIHO_08350 {ECO:0000313|EMBL:KUP94278.1};
OS Tritonibacter horizontis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Tritonibacter.
OX NCBI_TaxID=1768241 {ECO:0000313|EMBL:KUP94278.1, ECO:0000313|Proteomes:UP000068382};
RN [1] {ECO:0000313|EMBL:KUP94278.1, ECO:0000313|Proteomes:UP000068382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O3.65 {ECO:0000313|EMBL:KUP94278.1,
RC ECO:0000313|Proteomes:UP000068382};
RA Poehlein A., Giebel H.A., Voget S., Brinkhoff T.;
RT "Genome sequence of the marine Rhodobacteraceae strain O3.65, Candidatus
RT Tritonibacter horizontis.";
RL Submitted (DEC-2015) 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|PIRNR:PIRNR006247}; Multi-pass membrane protein
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|PIRNR:PIRNR006247}.
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:KUP94278.1}.
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DR EMBL; LPUY01000021; KUP94278.1; -; Genomic_DNA.
DR RefSeq; WP_068240680.1; NZ_LPUY01000021.1.
DR AlphaFoldDB; A0A132C123; -.
DR PATRIC; fig|1768241.3.peg.865; -.
DR OrthoDB; 9810952at2; -.
DR Proteomes; UP000068382; Unassembled WGS sequence.
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:SF3; TRK SYSTEM POTASSIUM UPTAKE PROTEIN; 1.
DR PANTHER; PTHR32024; 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|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:UP000068382};
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..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 71..92
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 129..151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 186..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 227..252
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 328..353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 389..412
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 112
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|PIRSR:PIRSR006247-1"
FT BINDING 113
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|PIRSR:PIRSR006247-1"
FT BINDING 220
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|PIRSR:PIRSR006247-1"
FT BINDING 315
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|PIRSR:PIRSR006247-1"
FT BINDING 431
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|PIRSR:PIRSR006247-1"
SQ SEQUENCE 482 AA; 51798 MW; AFE521561FB92785 CRC64;
MLDLRPVGYV IGLLVVILGG TMVFPLLLDL YDGKGEWPVF LESAILCLLA GGLLALSCAN
GVGRGLTIRQ TFLLTTMVWV ALPFFGAIPL ILGATQLSFT DAFFEAMSGL TTTGSTVISG
LDELPRGLLL WRGILQWLGG IGIIVVAMVF LPELRVGGMQ IFKSEAFDTM GKILPRAQEI
AKQITVIYLV LTLVCALVYT VLGMGLFDAV VHAMTTMSTG GFSNYDASFG TFSGPAEYAS
AFFMVAAALP FVRYVQMVNG EALPLVRDSQ VRTFLATIAV LVVVTAGVLV TVFPHHPEQA
VREALFNIIS IMSGTGYASV DYMQWGPFLI MIFFFIGLIG GCAGSTACSV KIFRYQLLFA
SVRVQVQRIR SPHGVFIPRY EGRAVTPDVL SSVISFFMFF VITMGIVAWA LALTGLDFIT
AISGAATAVA NIGPGLGDII GPAGNFAPLN DTAKWILAIA MLIGRLELMA VYAILTVRFW
RS
//
