ID   KDPA_ERWT9              Reviewed;         561 AA.
AC   B2VJK4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-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=ETA_33650;
OS   Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB
OS   4357 / Et1/99).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=465817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99;
RX   PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA   Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA   Geider K.;
RT   "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT   bacterium in the genus Erwinia.";
RL   Environ. Microbiol. 10:2211-2222(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 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; CU468135; CAO98411.1; -; Genomic_DNA.
DR   RefSeq; WP_012443034.1; NC_010694.1.
DR   AlphaFoldDB; B2VJK4; -.
DR   SMR; B2VJK4; -.
DR   STRING; 465817.ETA_33650; -.
DR   EnsemblBacteria; CAO98411; CAO98411; ETA_33650.
DR   KEGG; eta:ETA_33650; -.
DR   eggNOG; COG2060; Bacteria.
DR   HOGENOM; CLU_018614_3_0_6; -.
DR   OMA; RQGWAIL; -.
DR   OrthoDB; 296671at2; -.
DR   Proteomes; UP000001726; 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..561
FT                   /note="Potassium-transporting ATPase potassium-binding
FT                   subunit"
FT                   /id="PRO_1000114681"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        132..152
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        253..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        283..303
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        526..546
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
SQ   SEQUENCE   561 AA;  59750 MW;  370267B43F1D096B CRC64;
     MMASASLLIG SYLLLLMLLA RPLGKGLAHL VADRPLHGFA TAERGLWRVS GVENQGMRWQ
     RYLLAILLFN AAGLLLLLLI LMNQASLPLN PQQMPNLSWD LALNTAVSFI TNTDWQAYAG
     ESTLSYFSQM AGLTVQNFLS AATGIAVAFA LMRGFVNREQ GELGNAWRDI TRITLYVLLP
     LSLLMALFLV SQGTLQNLHG YLDLTTLEGA KQTLPMGPVA SQEAIKMLGT NGGGFFNANS
     AHPFENPTAL SNFVQMLAIF LIPAALCFAF GDVVRDRRQG HALLWSMSLM FVAAVVVVMW
     AEVKGNPHFL TLGADSAANM EGKETRFGIL NSSLFAVITT AASCGAVNAM HDSFTALGGM
     VPMWLMQIGE VVFGGVGSGL YGMLLFVLLA VFIAGLMIGR SPEYLGKKID VWEMKMTALA
     ILVTPVLVLL GAALAMMTDA GRSAMLNPGT HGFSEVLYAL SSAANNNGSA FAGLNANTPF
     WNMLLAFCML VGRFGIIVPV LAIAGSLAMK KVQPAGNGTL PTHGTLFIAL LIGTVMLVGA
     LTFIPALALG PVAEHLHMSG H