ID   KDPA_KLEP7              Reviewed;         559 AA.
AC   A6T6D9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 81.
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};
GN   OrderedLocusNames=KPN78578_06990; ORFNames=KPN_00717;
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=272620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578;
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000647; ABR76160.1; -; Genomic_DNA.
DR   RefSeq; WP_012068461.1; NC_009648.1.
DR   AlphaFoldDB; A6T6D9; -.
DR   SMR; A6T6D9; -.
DR   STRING; 272620.KPN_00717; -.
DR   EnsemblBacteria; ABR76160; ABR76160; KPN_00717.
DR   KEGG; kpn:KPN_00717; -.
DR   HOGENOM; CLU_018614_3_0_6; -.
DR   OMA; RQGWAIL; -.
DR   Proteomes; UP000000265; 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..559
FT                   /note="Potassium-transporting ATPase potassium-binding
FT                   subunit"
FT                   /id="PRO_1000022227"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        63..83
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        173..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        254..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        282..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        327..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        356..376
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        379..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        416..436
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        483..503
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   559 AA;  59442 MW;  6E382214F00EE4B0 CRC64;
     MAAQGFLLLA SYLLVLLVLA RPLGMCLARM VNDIPLPGLA GVERVLWRVA GIRAEEMGWL
     QYLLAILLFN ALGGLALFAL LMLQGVLPFN PQHLPGLSWD LALNTAISFI SNTNWQAYAG
     ESTMSYLSQM VGLTVQNFLS AATGIAVVFA LTRAFARQKM STLGNAWVDL TRITLWLLLP
     LSLLVALFFI QQGVPQNLQA YQPFITLEGV HQLLPMGPVA SQEAIKLLGT NGGGFFNANS
     AHPFENPTAL TNLVQMLAIF LIPTALCFAF GEVVSDRRQG RAILWAMTLI FILCVAVVMW
     AETRGNPHLL TLGADSSLNM EGKESRFGIL ASSLFAVITT AASCGAVNAM HDSFTALGGM
     VPMWLMQIGE VVFGGVGSGL YGMLLFVMLA VFIAGLMVGR TPEYLGKKID VREMKMIALA
     ILVTPTLVLL GTALAMMTDA GRAGMFNPGP HGFSEVLYAV TSAANNNGSA FAGLGAATPF
     WNLLLAFCML VGRFAVIIPV MAIAGSLVAK KIQPASPGTL ATHDALFIGL LIGTVLLVGA
     LTFIPALALG PLAEHFSLL