ID C0Q3F6_SALPC Unreviewed; 483 AA.
AC C0Q3F6;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Trk system potassium uptake protein {ECO:0000256|PIRNR:PIRNR006247};
GN Name=trkH {ECO:0000313|EMBL:ACN48158.1};
GN OrderedLocusNames=SPC_4093 {ECO:0000313|EMBL:ACN48158.1};
OS Salmonella paratyphi C (strain RKS4594).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=476213 {ECO:0000313|EMBL:ACN48158.1, ECO:0000313|Proteomes:UP000001599};
RN [1] {ECO:0000313|EMBL:ACN48158.1, ECO:0000313|Proteomes:UP000001599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RKS4594 {ECO:0000313|EMBL:ACN48158.1,
RC ECO:0000313|Proteomes:UP000001599};
RX PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H.,
RA Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L.;
RT "Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis
RT and pathogenic convergence with Salmonella typhi.";
RL PLoS ONE 4:E4510-E4510(2009).
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; CP000857; ACN48158.1; -; Genomic_DNA.
DR RefSeq; WP_000545688.1; NC_012125.1.
DR AlphaFoldDB; C0Q3F6; -.
DR SMR; C0Q3F6; -.
DR KEGG; sei:SPC_4093; -.
DR HOGENOM; CLU_030708_0_2_6; -.
DR Proteomes; UP000001599; 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 NCBIfam; TIGR00933; 2a38; 1.
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 channel {ECO:0000256|ARBA:ARBA00023303};
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 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 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 38..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 69..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 136..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 237..255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 276..295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 331..363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 396..417
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 456..481
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 111
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|PIRSR:PIRSR006247-1"
FT BINDING 112
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 221
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|PIRSR:PIRSR006247-1"
FT BINDING 318
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|PIRSR:PIRSR006247-1"
FT BINDING 319
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|PIRSR:PIRSR006247-1"
FT BINDING 435
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|PIRSR:PIRSR006247-1"
FT BINDING 436
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|PIRSR:PIRSR006247-1"
SQ SEQUENCE 483 AA; 52902 MW; A84005C1CE28C0EC CRC64;
MHFRAITRIV GLLVILFSGT MILPGLVALI YRDGAGRAFT QTFFVALAIG SILWWPNRRE
KGELKSREGF LIVVLFWTVL GSVGALPFIF SESPNLTITD AFFESFSGLT TTGATTLVGL
DSLPHAILFY RQMLQWFGGM GIIVLAVAIL PILGVGGMQL YRAEMPGPLK DNKMRPRIAE
TAKTLWLIYV LLTVACALAL WFAGMPAFDA IGHSFSTIAI GGFSTHDASV GYFDSPTINT
IIAIFLLISG CNYGLHFSLL SGRSLKVYWR DPEFRMFIGV QLTLVVICTL VLWFHNIYDS
ALTTLNQAFF QVVSMATTAG FTTDSIARWP LFLPVLLLCS AFIGGCAGST GGGLKVIRIL
LLFKQGNREL KRLVHPNAVY SIKLGNRALP ERILEAVWGF FSAYALVFIV SMLAIIATGV
DDFSAFASVV ATLNNLGPGL GVVADNFASM NPVAKWILIA NMLFGRLEVF TLLVLFTPTF
WRE
//