ID   KDPB_LISMC              Reviewed;         681 AA.
AC   C1KZN5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=Lm4b_02654;
OS   Listeria monocytogenes serotype 4b (strain CLIP80459).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=568819;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIP80459;
RX   PubMed=22530965; DOI=10.1186/1471-2164-13-144;
RA   Hain T., Ghai R., Billion A., Kuenne C.T., Steinweg C., Izar B.,
RA   Mohamed W., Mraheil M., Domann E., Schaffrath S., Karst U., Goesmann A.,
RA   Oehm S., Puhler A., Merkl R., Vorwerk S., Glaser P., Garrido P.,
RA   Rusniok C., Buchrieser C., Goebel W., Chakraborty T.;
RT   "Comparative genomics and transcriptomics of lineages I, II, and III
RT   strains of Listeria monocytogenes.";
RL   BMC Genomics 13:144-144(2012).
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 membrane {ECO:0000255|HAMAP-Rule:MF_00285};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-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; FM242711; CAS06408.1; -; Genomic_DNA.
DR   RefSeq; WP_003727672.1; NC_012488.1.
DR   AlphaFoldDB; C1KZN5; -.
DR   SMR; C1KZN5; -.
DR   KEGG; lmc:Lm4b_02654; -.
DR   HOGENOM; CLU_025728_2_0_9; -.
DR   OMA; KSPVMFV; -.
DR   BioCyc; LMON568819:LM4B_RS13535-MON; -.
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   PRINTS; PR00120; HATPASE.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   SUPFAM; SSF81653; SSF81653; 1.
DR   SUPFAM; SSF81660; SSF81660; 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 membrane; Ion transport; Magnesium; Membrane;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Potassium;
KW   Potassium transport; Translocase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..681
FT                   /note="Potassium-transporting ATPase ATP-binding subunit"
FT                   /id="PRO_1000204851"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   TRANSMEM        216..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   TRANSMEM        255..275
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   TRANSMEM        587..607
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   TRANSMEM        615..635
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   TRANSMEM        661..681
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   ACT_SITE        306
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   BINDING         343
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   BINDING         347
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   BINDING         376..383
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   BINDING         394
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   BINDING         517
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   BINDING         521
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
SQ   SEQUENCE   681 AA;  72368 MW;  FF3BBAD8844B5F3F CRC64;
     MMEKGIWKDA LIQSTKKLSP KLQVKNPVML LVYVGAILAT SLYFLGFFGI SDEKSGYTLA
     IALILWFTVL FANFAEAIAE GRGRAQADSL KMARKDVLAR KLKNIDDKTD VIEIASNDLK
     KGDIVYVLAN EQIPMDGEVI EGAASVDESA ITGESAPVIR ESGGDRSAVT GGTTLVSDWL
     VVRVTAVSGE SFLDKMIAMV EGASRKKTPN EIALQILLVT LSIIFLAVSA TLLPFTEFAS
     KQAGAGSAIS ITNVIALLVC LAPTTIGALL SSIGIAGMSR LNQANVLAMS GRAIEAAGDV
     DVLLLDKTGT ITLGNRKASE FLPVDGVTEQ ELADAAQLSS IADETAEGRS IVVLAKERFD
     IRGRDFAEMH AEFVPFTATT RMSGIDYQEN TIRKGAADAV RAYVTANGGT YPKECDAIVS
     KVAGAGGTPL VVVRNNKVLG VIYLKDIVKN GVKERFLDLR KMGIKTIMIT GDNPMTAAAI
     AAEAGVDDFL AEATPEAKLE LIREYQREGH LVAMTGDGTN DAPALAQADV AVAMNTGTQA
     AKEAGNMVDL DSSPTKLIDI VRIGKQLLMT RGALTTFSVA NDLAKYFAII PVLFYGIFPQ
     LEALNLMGLT SPTSAILSAI IYNAVIIIIL IPLSLKGVKY REMPAGKLLS RNMLIYGLGG
     LIAPFIAIKL IDMLLTVLGI V