KDPB_POLAQ
ID KDPB_POLAQ Reviewed; 691 AA.
AC A4SZG8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=Pnuc_1669;
OS Polynucleobacter asymbioticus (strain DSM 18221 / CIP 109841 /
OS QLW-P1DMWA-1) (Polynucleobacter necessarius subsp. asymbioticus).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Polynucleobacter.
OX NCBI_TaxID=312153;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18221 / CIP 109841 / QLW-P1DMWA-1;
RX PubMed=22675600; DOI=10.4056/sigs.2395367;
RA Meincke L., Copeland A., Lapidus A., Lucas S., Berry K.W., Del Rio T.G.,
RA Hammon N., Dalin E., Tice H., Pitluck S., Richardson P., Bruce D.,
RA Goodwin L., Han C., Tapia R., Detter J.C., Schmutz J., Brettin T.,
RA Larimer F., Land M., Hauser L., Kyrpides N.C., Ivanova N., Goker M.,
RA Woyke T., Wu Q.L., Pockl M., Hahn M.W., Klenk H.P.;
RT "Complete genome sequence of Polynucleobacter necessarius subsp.
RT asymbioticus type strain (QLW-P1DMWA-1(T)).";
RL Stand. Genomic Sci. 6:74-83(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 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; CP000655; ABP34882.1; -; Genomic_DNA.
DR RefSeq; WP_011903505.1; NC_009379.1.
DR AlphaFoldDB; A4SZG8; -.
DR SMR; A4SZG8; -.
DR STRING; 312153.Pnuc_1669; -.
DR EnsemblBacteria; ABP34882; ABP34882; Pnuc_1669.
DR GeneID; 31482057; -.
DR KEGG; pnu:Pnuc_1669; -.
DR eggNOG; COG2216; Bacteria.
DR HOGENOM; CLU_025728_2_0_4; -.
DR OMA; ILWLWFT; -.
DR Proteomes; UP000000231; 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; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..691
FT /note="Potassium-transporting ATPase ATP-binding subunit"
FT /id="PRO_1000078863"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT TRANSMEM 600..620
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT TRANSMEM 628..648
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT TRANSMEM 671..691
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT ACT_SITE 319
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 356
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 360
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 389..396
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 407
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 530
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 534
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
SQ SEQUENCE 691 AA; 73380 MW; 4BA7623D3F6DC1C4 CRC64;
MTKRKLGMFD AELVKPAIVD SFRKLSPSIQ WRNPVMFVVY IGSILTTLLW IQSLYGEGEA
SSSFILGVML WLWFTVLFAN FAEALAEGRS KAQAASLRGL KKETWAKKVK AANIPENWDN
RPASELVSAT QLRKGDIFIA EANDVIAADG EVIAGVASVD ESAITGESAP VIRESGGDFS
SVTGGTRVLS DWIVVRVTVN PGETFIDRMI SMVENAKRQK TPNEIALTIL LVALTIVFLV
VVATLLPFSM FSVAASGSGS PIQITVLIAL LVCLIPTTIA GLLSAIGVAG MSRMMAANVI
ATSGRAVEAA GDVDVLLLDK TGTITLGNRQ ASNFVAASGV TEAELADIAQ LASLADETPE
GRSIVVLAKQ KFNIREREIN SIGAQFVPFT AQTRMSGVDM NGEQIRKGAA SAIQKHIESL
GGHFPQEVLK AVDDVSRRGS TPLVVSQGTR VMGVVELKDI VKGGIKERFN ELRQMGIRTI
MITGDNKLTA AAIAAEAGVD DFLAEATPED KLALIRKHQS EGRLVAMTGD GTNDAPALAQ
ADVAVAMNSG TQAAKEAGNM VDLDSNPTKL IEVVETGKQM LMTRGSLTTF SIANDVAKYF
AIIPAAFVAT YPQLEALNVM HLSSPSSAIL SAVIFNALII IFLIPLALKG VTYKPLGAAA
LLRRNMTIYG LGGLIAPFIG IKIIDLIISV I
