ID   KDPA_PSEPF              Reviewed;         564 AA.
AC   Q3K8Y4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 101.
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=Pfl01_4033;
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1;
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
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; CP000094; ABA75770.1; -; Genomic_DNA.
DR   RefSeq; WP_011335330.1; NC_007492.2.
DR   AlphaFoldDB; Q3K8Y4; -.
DR   SMR; Q3K8Y4; -.
DR   STRING; 205922.Pfl01_4033; -.
DR   EnsemblBacteria; ABA75770; ABA75770; Pfl01_4033.
DR   KEGG; pfo:Pfl01_4033; -.
DR   eggNOG; COG2060; Bacteria.
DR   HOGENOM; CLU_018614_3_0_6; -.
DR   OMA; AWSNLFE; -.
DR   Proteomes; UP000002704; 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; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..564
FT                   /note="Potassium-transporting ATPase potassium-binding
FT                   subunit"
FT                   /id="PRO_1000022241"
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        528..548
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
SQ   SEQUENCE   564 AA;  60103 MW;  AF90BE02165A4FDC CRC64;
     MHSYDYWLIL AFFAVVLLPA PFLGRFYYKV MEGQSTWLTP ILGPVERGCY RIAGVNPQDE
     QSWQKYTLAL LAFNLAGFLL LFAILLFQDH LPLNPQNLPG QEWTLAFNTA VSFMTNTNWQ
     AYSGEASLSY LSQMVGLTVQ NFVSAATGLA VLVALCRGIG RKSTKTLGNF WVDMTRATLY
     GLLPLCLLLA LYLVWQGVPQ TFAQYVNAVT MQGVDQVIPL GPAASQIAIK QLGTNGGGFF
     GVNSAHPFEN PTAWSNLFEV ASIILIPVAL VFTFGHYVKD LRQSRAIIGC MLALFIIGGA
     TSLWAEYQPN PALNNVTVEQ AAPLEGKEAR FGTTATVLWS VTTTAASNGS VNGMHDSLNP
     LSGMVALVNM MVGEVIFGGV GAGLYGMLLN VLIAVFLAGL MIGRTPEYLG KKLQAREVQL
     LVVTLLVMPV GVLVLGAIAA SLPGPVAAVS NPGPHGFSQL LYAYTSASAN NGSAFGGFGA
     NTAFHNLMLG LGMLIGRFGY ILPVLALAGS LAMKKTAPIG QNSFPTHGPL FVTLLTVTIL
     LLGGLTFLPT LALGPIAEHL SMGF