ID   KDPA_RIPO1              Reviewed;         559 AA.
AC   B7JY03;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 67.
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=PCC8801_1929;
OS   Rippkaea orientalis (strain PCC 8801) (Cyanothece sp. (strain PCC 8801)).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Aphanothecaceae; Rippkaea; Rippkaea orientalis.
OX   NCBI_TaxID=41431;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 8801;
RX   PubMed=21972240; DOI=10.1128/mbio.00214-11;
RA   Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA   Sherman L.A., Pakrasi H.B.;
RT   "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT   unicellular nitrogen-fixing Cyanobacteria.";
RL   MBio 2:E214-E214(2011).
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; CP001287; ACK65967.1; -; Genomic_DNA.
DR   RefSeq; WP_012595239.1; NC_011726.1.
DR   AlphaFoldDB; B7JY03; -.
DR   SMR; B7JY03; -.
DR   STRING; 41431.PCC8801_1929; -.
DR   EnsemblBacteria; ACK65967; ACK65967; PCC8801_1929.
DR   KEGG; cyp:PCC8801_1929; -.
DR   eggNOG; COG2060; Bacteria.
DR   HOGENOM; CLU_018614_3_0_3; -.
DR   OMA; RQGWAIL; -.
DR   OrthoDB; 296671at2; -.
DR   Proteomes; UP000008204; 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_1000119334"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        69..89
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        177..197
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        280..300
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        354..374
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        378..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        413..433
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        482..502
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        531..551
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
SQ   SEQUENCE   559 AA;  60549 MW;  23586421E6E8E54F CRC64;
     MVQGLIQIAI TLLLLLIIVP NLGNYMAKVY LKQKTVLDPI LLPLENLIYA ISGLRSQREM
     TGWQYARSVI FSNILMGIFV FSLFSFQAIL PFNPTQLAAP SWHLALHTTI SFVTNTNQQH
     YSGETTFSYG SQLFALGFLM FTSAGTGLAV AMAFIRGLIG EPLGNFYVDL TRSITRILLP
     IALISGLILL SQGVPETLSP PASVTTLQGA TQTLARGPVA HFESIKQLGE NGGGFFGINS
     AHPFENPNGF SNLIETLLML CIPTSLIYTY GVMIGNKKQA WLLFSMIFII YVFLIAITAL
     GEYQGNPLVN NLLTTQQPNL EGKEIRFGWA QTVLWAISTT GTMCGAVNGM HDSLMPLGGL
     STLFNLFLQI IWGGQGTGTA YLFVFLIITV FLTGLMVGRS PEFLGRKIEK REIVFASVIL
     LVHPFAILVP GAITLVFPEI LSGISNPGFH GVSQVVYEYA SAAANNGSGF EGLGDNTLWW
     NLSTSVVLLL GRYVPIIALL LLAESMRQKQ PVPETTGTLR TDTGLFTAVT AGVILILGAL
     TFLPVLALGP IAEGFKLGW