ID   KDPB_ERWT9              Reviewed;         682 AA.
AC   B2VJK3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Potassium-transporting ATPase ATP-binding subunit {ECO:0000255|HAMAP-Rule:MF_00285};
DE            EC=7.2.2.6 {ECO:0000255|HAMAP-Rule:MF_00285};
DE   AltName: Full=ATP phosphohydrolase [potassium-transporting] B chain {ECO:0000255|HAMAP-Rule:MF_00285};
DE   AltName: Full=Potassium-binding and translocating subunit B {ECO:0000255|HAMAP-Rule:MF_00285};
DE   AltName: Full=Potassium-translocating ATPase B chain {ECO:0000255|HAMAP-Rule:MF_00285};
GN   Name=kdpB {ECO:0000255|HAMAP-Rule:MF_00285}; OrderedLocusNames=ETA_33640;
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 is
CC       responsible for energy coupling to the transport system and for the
CC       release of the potassium ions to the cytoplasm. {ECO:0000255|HAMAP-
CC       Rule:MF_00285}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + K(+)(out) = ADP + H(+) + K(+)(in) + phosphate;
CC         Xref=Rhea:RHEA:16777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29103, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=7.2.2.6; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00285};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16778;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00285};
CC   -!- SUBUNIT: The system is composed of three essential subunits: KdpA, KdpB
CC       and KdpC. {ECO:0000255|HAMAP-Rule:MF_00285}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00285}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00285}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IA subfamily. {ECO:0000255|HAMAP-Rule:MF_00285}.
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DR   EMBL; CU468135; CAO98410.1; -; Genomic_DNA.
DR   RefSeq; WP_012443033.1; NC_010694.1.
DR   AlphaFoldDB; B2VJK3; -.
DR   SMR; B2VJK3; -.
DR   STRING; 465817.ETA_33640; -.
DR   EnsemblBacteria; CAO98410; CAO98410; ETA_33640.
DR   KEGG; eta:ETA_33640; -.
DR   eggNOG; COG2216; Bacteria.
DR   HOGENOM; CLU_025728_2_0_6; -.
DR   OMA; TNPGETF; -.
DR   OrthoDB; 237367at2; -.
DR   Proteomes; UP000001726; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008556; F:P-type potassium transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR   CDD; cd02078; P-type_ATPase_K; 1.
DR   Gene3D; 3.40.1110.10; -; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   HAMAP; MF_00285; KdpB; 1.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR   InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR006391; P-type_ATPase_bsu_IA.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   PANTHER; PTHR43743; PTHR43743; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   SUPFAM; SSF81653; SSF81653; 1.
DR   SUPFAM; SSF81665; SSF81665; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR   TIGRFAMs; TIGR01497; kdpB; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Ion transport; Magnesium;
KW   Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Potassium;
KW   Potassium transport; Reference proteome; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..682
FT                   /note="Potassium-transporting ATPase ATP-binding subunit"
FT                   /id="PRO_1000114954"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   TRANSMEM        219..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   TRANSMEM        254..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   TRANSMEM        577..597
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   TRANSMEM        616..636
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   TRANSMEM        656..676
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   ACT_SITE        307
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   BINDING         344
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   BINDING         348
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   BINDING         377..384
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   BINDING         395
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   BINDING         518
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   BINDING         522
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
SQ   SEQUENCE   682 AA;  71717 MW;  31162B3780A278F9 CRC64;
     MSRNQLALFD AALMRVALLD ALKKLDPRTQ VRNPVMFVVW LGSVVTTLLA VAMAAGKTPG
     DTGFTVAISV WLWFTVLFAN FAEALAEGRS KAQANSLKGV TKTSFAKKLN EAKYGTSHYP
     VAADTLRKGD WVLVEAGDII PCDGEVLEGG ASVDESAITG ESAPVIRESG GDFSSVTGGT
     RILSDWLVVQ CSVNPGETFL DRMIAMVEGA TRRKTPNEIA LTILLLALTI VLLLATVTLW
     PFSAWGGNPV SITVLVALLV CLIPTTIGGL LSAIGVAGMS RMLGANVIAT SGRAVEAAGD
     VDVLLLDKTG TITLGNRQAT QFLPAAGVSE EQLADAAQLA SLADETPEGR SIVVLAKQKF
     NLRERDLNSM GATFIPFSAQ TRMSGVNVQQ RAIRKGAADA VRRYIDSNGG QFPGEVNSLV
     DRVARAGGTP LVVSDGNRVM GVVALKDIVK GGIKERFAEL RKMGIKTVMI TGDNPLTAAA
     IAAEAGVDDF LSEATPEAKL ALIRQYQAEG RLVAMTGDGT NDAPALAQAD VAVAMNSGTQ
     AAKEAGNMVD LDSNPTKLLE VVHIGKQMLM TRGSLTTFSI ANDVAKYFAI LPAAFAATYP
     QLNQLNVMGL HSPASAILSA VIFNALVIVF LIPLALKGVS YRALSAAALL RRNLWIYGVG
     GLLVPFLGIK LIDMLLTVTG LA