ID   KDPA_STRGG              Reviewed;         554 AA.
AC   B1W3K2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   25-MAY-2022, entry version 76.
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=SGR_2679;
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=455632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350;
RX   PubMed=18375553; DOI=10.1128/jb.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT   griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(2008).
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 extracellular 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 membrane {ECO:0000255|HAMAP-Rule:MF_00275};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00275}.
CC   -!- SIMILARITY: Belongs to the KdpA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00275}.
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DR   EMBL; AP009493; BAG19508.1; -; Genomic_DNA.
DR   RefSeq; WP_012379377.1; NC_010572.1.
DR   AlphaFoldDB; B1W3K2; -.
DR   SMR; B1W3K2; -.
DR   STRING; 455632.SGR_2679; -.
DR   EnsemblBacteria; BAG19508; BAG19508; SGR_2679.
DR   GeneID; 6211109; -.
DR   KEGG; sgr:SGR_2679; -.
DR   PATRIC; fig|455632.4.peg.2729; -.
DR   eggNOG; COG2060; Bacteria.
DR   HOGENOM; CLU_018614_3_0_11; -.
DR   OMA; LMMWTEF; -.
DR   OrthoDB; 296671at2; -.
DR   Proteomes; UP000001685; 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 membrane; Ion transport; Membrane; Potassium; Potassium transport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..554
FT                   /note="Potassium-transporting ATPase potassium-binding
FT                   subunit"
FT                   /id="PRO_1000114707"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        174..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        246..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        279..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        323..343
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        352..372
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        375..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        412..432
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        481..501
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        525..545
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
SQ   SEQUENCE   554 AA;  58109 MW;  F613F7B75F0E1099 CRC64;
     MSSQVAGLLQ LTALIAALAL AYRPLGDYMA RVYSSEKHYR PEKWMYKAIG ANPAAEMRWP
     AYLRGVLAFS AMSVLFLYLM QRVQGSLPGS LGFSSIDPDQ AFNTAASFVA NTNWQSYYGE
     QAMGHVVQTG GLAVQNFLSA AVGMAVAVAL VRGFARSRTG ELGNFWADLV RGTVRILVPI
     SVIGAIVLVA AGAIQNFSGI HQVGQFAGGT QEWNGGAVAS QEAIKELGTN GGGYFNANSA
     HPFENPNPLS NLFEVFLILL IPFALTRTFG RMAGSLKQGY AILGAMAVIW IGFTALMMWT
     EFAHRGPAFE IAGGAMEGKE ARFGIAGSSI FAVATTLTST GAVNSFHSSY TGFGGGITLL
     GMQLGEIAPG GVGSGLYGML IMAIIAVFIA GLMVGRTPEY LGKKIGTRQI KFAACYILIT
     PALVLGFTAV AMALPTPADS MTNSGAHGFS EILYAYTSGA NNNGSAFAGL NADTQWFNTT
     IGIAMLLGRF LPMVFVLALA GSLAEQQPVP ETAGTLRTDK PLYSGLLVGT ILIITGLTYF
     PALALGPLAE GLAS