KDPA_PSEPK
ID KDPA_PSEPK Reviewed; 564 AA.
AC Q88FD7;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Potassium-transporting ATPase potassium-binding subunit {ECO:0000255|HAMAP-Rule:MF_00275};
DE AltName: Full=ATP phosphohydrolase [potassium-transporting] A chain {ECO:0000255|HAMAP-Rule:MF_00275};
DE AltName: Full=Potassium-binding and translocating subunit A {ECO:0000255|HAMAP-Rule:MF_00275};
DE AltName: Full=Potassium-translocating ATPase A chain {ECO:0000255|HAMAP-Rule:MF_00275};
GN Name=kdpA {ECO:0000255|HAMAP-Rule:MF_00275}; OrderedLocusNames=PP_4161;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
CC -!- FUNCTION: Part of the high-affinity ATP-driven potassium transport (or
CC Kdp) system, which catalyzes the hydrolysis of ATP coupled with the
CC electrogenic transport of potassium into the cytoplasm. This subunit
CC binds the periplasmic potassium ions and delivers the ions to the
CC membrane domain of KdpB through an intramembrane tunnel.
CC {ECO:0000255|HAMAP-Rule:MF_00275}.
CC -!- SUBUNIT: The system is composed of three essential subunits: KdpA, KdpB
CC and KdpC. {ECO:0000255|HAMAP-Rule:MF_00275}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00275}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00275}.
CC -!- SIMILARITY: Belongs to the KdpA family. {ECO:0000255|HAMAP-
CC Rule:MF_00275}.
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DR EMBL; AE015451; AAN69742.1; -; Genomic_DNA.
DR RefSeq; NP_746278.1; NC_002947.4.
DR RefSeq; WP_010954929.1; NC_002947.4.
DR AlphaFoldDB; Q88FD7; -.
DR SMR; Q88FD7; -.
DR STRING; 160488.PP_4161; -.
DR EnsemblBacteria; AAN69742; AAN69742; PP_4161.
DR KEGG; ppu:PP_4161; -.
DR PATRIC; fig|160488.4.peg.4423; -.
DR eggNOG; COG2060; Bacteria.
DR HOGENOM; CLU_018614_3_0_6; -.
DR OMA; AWSNLFE; -.
DR PhylomeDB; Q88FD7; -.
DR BioCyc; PPUT160488:G1G01-4427-MON; -.
DR Proteomes; UP000000556; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0008556; F:P-type potassium transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0030955; F:potassium ion binding; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00275; KdpA; 1.
DR InterPro; IPR004623; KdpA.
DR PANTHER; PTHR30607; PTHR30607; 1.
DR Pfam; PF03814; KdpA; 1.
DR PIRSF; PIRSF001294; K_ATPaseA; 1.
DR TIGRFAMs; TIGR00680; kdpA; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Ion transport; Membrane; Potassium;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..564
FT /note="Potassium-transporting ATPase potassium-binding
FT subunit"
FT /id="PRO_0000166514"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 487..507
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 533..553
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
SQ SEQUENCE 564 AA; 59879 MW; ECF7CFFA982B18EB CRC64;
MHSYDFALLL AFFVIVLLPA PWLGRFYYKV MEGQRTWLTP VLGPVEQGCY RLAGVNASQE
QNWRQYTLAL LAFNLVGFLL LFAVLLLQGY LPLNPQNLPG QEWSLAFNTA VSFVTNTNWQ
AYSGEASVSY LSQMLGLTVQ NFVSPATGLA VLVVLCRGIA RRSATTLGNF WVDMTRATLY
GLLPLCLLLA LLLVWQGVPQ TFADYAHALT LQGADQTIPL GPAASQIAIK QLGTNGGGFF
GVNSAHPFEN PTAWSNLFEV ASIILIPVAL VFTFGHYVKD LRQSRAILAC MLALFLIGGS
TALWSEHQPN PALESTQVQQ TAPLEGKESR FGTTGSVLWA VTTTAASNGS VNAMHDSLNP
LTGMVAMVNM MVGEVIFGGV GAGLYGMLLF VLIAVFLAGL MIGRTPEYLG KKLQAREVQL
LVATLLVMPV GVLVLGAIAA SLPGPAGAVT NPGAHGFSQL LYAYTSGSAN NGSAFAGFGA
NTVYHNLMIG LAMLIGRFGY ILPILALAGS LAAKKSAPLG QNSFPTHGPL FTGLLLVTIL
LVGGLTFLPT LALGPIAEHL SLGF
