KDPB_CLOBA
ID KDPB_CLOBA Reviewed; 688 AA.
AC B2V2P3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=CLH_0916;
OS Clostridium botulinum (strain Alaska E43 / Type E3).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=508767;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alaska E43 / Type E3;
RA Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.S.;
RT "Complete genome sequence of Clostridium botulinum E3 str. Alaska E43.";
RL Submitted (MAY-2008) 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 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; CP001078; ACD53783.1; -; Genomic_DNA.
DR RefSeq; WP_012451616.1; NC_010723.1.
DR AlphaFoldDB; B2V2P3; -.
DR SMR; B2V2P3; -.
DR KEGG; cbt:CLH_0916; -.
DR HOGENOM; CLU_025728_2_0_9; -.
DR OMA; KSPVMFV; -.
DR OrthoDB; 237367at2; -.
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 membrane; Ion transport; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Potassium;
KW Potassium transport; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..688
FT /note="Potassium-transporting ATPase ATP-binding subunit"
FT /id="PRO_1000114949"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT TRANSMEM 65..85
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 262..282
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT TRANSMEM 594..614
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT TRANSMEM 622..642
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT TRANSMEM 668..688
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT ACT_SITE 313
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 350
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 354
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 383..390
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 401
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 524
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 528
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
SQ SEQUENCE 688 AA; 73100 MW; 8EF1B81E7551CAA6 CRC64;
MNENKGNFAN KKMIKRAIKD SFIKLSPKTQ MENPVMFLVY ISSILTTILY AVSLVGIRDS
KSSFILGITI ILWLTVLFAN FAEAIAEGRG KAQADSLRAA KKDVEAHKIP SIEKRDEITK
VSSALLKKGD IVIVVAGEQV PADGEVIDGA ASVDESAITG ESAPVIRESG GDRSAVTGGT
TVISDWLIIE VTSEAGESFL DKMISMVEGA ARKKTPNEIA LQILLISLTI IFLLVTVSLY
SYSIFSANQA GVVNPISVTS LVALLVCLAP TTIGALLSSI GIAGMSRLNQ ANVLAMSGRA
IEAAGDVDIL MLDKTGTITL GNREACEFIP VNGVNENELA DAAQLSSLAD ETPEGRSIVV
LAKEKFGIRG RNIRESNMEF IPFTAKTRMS GVNYNNSEIR KGAAETVKDY VISRGGCYSK
ECDEVVARIS NKGGTPLVVA KDNKVLGVVY LKDIIKQGVQ EKFADLRKMG IKTIMITGDN
PLTAAAIAAE AGVDDFLAEA TPEGKLEMIR DFQIKGHLVA MTGDGTNDAP ALAQADVAVA
MNTGTQAAKE AGNMVDLDSS PTKLIDIVRI GKQLLMTRGS LTTFSIANDL AKYFAIIPAL
FIGLYPGLSA LNIMNLHSAE SAIFSAIIYN ALIIVALIPL ALKGVKYREV SAGKLLSRNL
LVYGLGGIIV PFIAIKVIDV LITAIGIV
