ID A0A142LH06_9PROT Unreviewed; 659 AA.
AC A0A142LH06;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Potassium transporter {ECO:0000313|EMBL:AMS31502.1};
GN ORFNames=AEM42_02125 {ECO:0000313|EMBL:AMS31502.1};
OS Betaproteobacteria bacterium UKL13-2.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1690485 {ECO:0000313|EMBL:AMS31502.1, ECO:0000313|Proteomes:UP000075227};
RN [1] {ECO:0000313|Proteomes:UP000075227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Driscoll C.B.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 2 (CPA2)
CC transporter (TC 2.A.37) family. {ECO:0000256|ARBA:ARBA00005551}.
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DR EMBL; CP012157; AMS31502.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A142LH06; -.
DR STRING; 1690485.AEM42_02125; -.
DR KEGG; beb:AEM42_02125; -.
DR PATRIC; fig|1690485.4.peg.490; -.
DR Proteomes; UP000075227; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0008324; F:monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
DR GO; GO:1902600; P:proton transmembrane transport; IEA:InterPro.
DR Gene3D; 1.20.1530.20; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.30.70.1450; Regulator of K+ conductance, C-terminal domain; 1.
DR InterPro; IPR006153; Cation/H_exchanger.
DR InterPro; IPR004771; K/H_exchanger.
DR InterPro; IPR038770; Na+/solute_symporter_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006037; RCK_C.
DR InterPro; IPR036721; RCK_C_sf.
DR InterPro; IPR003148; RCK_N.
DR NCBIfam; TIGR00932; 2a37; 1.
DR PANTHER; PTHR46157; K(+) EFFLUX ANTIPORTER 3, CHLOROPLASTIC; 1.
DR PANTHER; PTHR46157:SF4; K(+) EFFLUX ANTIPORTER 3, CHLOROPLASTIC; 1.
DR Pfam; PF00999; Na_H_Exchanger; 1.
DR Pfam; PF02080; TrkA_C; 1.
DR Pfam; PF02254; TrkA_N; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF116726; TrkA C-terminal domain-like; 1.
DR PROSITE; PS51202; RCK_C; 1.
DR PROSITE; PS51201; RCK_N; 1.
PE 3: Inferred from homology;
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Potassium transport {ECO:0000256|ARBA:ARBA00022538};
KW Reference proteome {ECO:0000313|Proteomes:UP000075227};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 31..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 56..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 115..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 148..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 177..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 218..234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 271..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 294..316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 328..346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 352..375
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 410..532
FT /note="RCK N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51201"
FT DOMAIN 572..657
FT /note="RCK C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51202"
SQ SEQUENCE 659 AA; 70481 MW; B3899ADBBE367397 CRC64;
MLHSSTLSLV VMLLATAVVT VVLFRKINMP AILGYLIVGV AIGPHAAGLV PDSEGTRYLA
EFGVVFLMFS IGLEFSLPQL VAMRKVVFGF GLLQVMVTIV VAGTIALLAG QKWQAALVIG
GVLSMSSTAI ISKVLAEQAA LHSPHGKQTM GVLLFQDLAV IPLLVLVPAL SLSGEEMITS
VGFSLLKATA ALALILFLGQ RLMRPLFHVV AAQKSSELFV LTVLLVTLGL ALATELAGVS
LALGAFLAGM LIAETEYRYQ VEDDIKPFRD VLLGLFFITI GMLLNFSALW QNIFYVFVLI
IALMSIKLLI VLGLALAFGQ DRAVSLRVAL ALAPAGEFGF VLLSVADKSG TLPANALQVV
LAACIISMLF SPLLFKYMEK IVLYLVASEW EQRAVQLQQL AVQSMMKKGH VIIAGYGRSG
QSLARFLERE KISIIALDGD PMRVKQASAA GESVMFGDAS KREVLTAAGV ARASALVVSF
ADTHTAMRIL AHVRTLKPDL PVIVRTFDDT DVQKLRDAGA DEIVAEVVEG SLMLATQTML
LLGVPLNRVL SRLRTVRGER YELMRGFFPG ATDADDGVPD PDLPRLQSVM LDAGAAAIGQ
SIAELDIGSV GVFLIALRRG GVRQMEPDPQ LCLAVGDVLI LNGSPENLAR AEMRVLQGE
//
