KDPB_HALS3
ID KDPB_HALS3 Reviewed; 719 AA.
AC B0R9M0;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 90.
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, ECO:0000312|EMBL:CAP15447.1};
GN OrderedLocusNames=OE_5053F {ECO:0000312|EMBL:CAP15447.1};
OS Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OG Plasmid PHS3 {ECO:0000312|EMBL:CAP15447.1}.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=478009;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT R1 compared to that of strain NRC-1.";
RL Genomics 91:335-346(2008).
RN [2]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=18633573; DOI=10.1007/s00792-008-0177-3;
RA Strahl H., Greie J.C.;
RT "The extremely halophilic archaeon Halobacterium salinarum R1 responds to
RT potassium limitation by expression of the K+-transporting KdpFABC P-type
RT ATPase and by a decrease in intracellular K+.";
RL Extremophiles 12:741-752(2008).
RN [3]
RP INDUCTION.
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=21947979; DOI=10.1007/s00792-011-0395-y;
RA Kixmueller D., Strahl H., Wende A., Greie J.C.;
RT "Archaeal transcriptional regulation of the prokaryotic KdpFABC complex
RT mediating K(+) uptake in H. salinarum.";
RL Extremophiles 15:643-652(2011).
RN [4]
RP FUNCTION, AND INDUCTION.
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=23757278; DOI=10.1111/j.1758-2229.2012.00326.x;
RA Kixmueller D., Greie J.C.;
RT "An ATP-driven potassium pump promotes long-term survival of Halobacterium
RT salinarum within salt crystals.";
RL Environ. Microbiol. Rep. 4:234-241(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 (By similarity). The Kdp
CC system is essential for growth under K(+) limitation, and for survival
CC under desiccation and salt crystal inclusion (PubMed:18633573,
CC PubMed:23757278). {ECO:0000255|HAMAP-Rule:MF_00285,
CC ECO:0000269|PubMed:18633573, ECO:0000269|PubMed:23757278}.
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. The complex also contains KdpF, a small non-essential
CC subunit. {ECO:0000250|UniProtKB:P03960}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00285};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00285}.
CC -!- INDUCTION: Up-regulated in response to K(+) limitation
CC (PubMed:18633573, PubMed:21947979). Induced under desiccating
CC conditions (PubMed:23757278). {ECO:0000269|PubMed:18633573,
CC ECO:0000269|PubMed:21947979, ECO:0000269|PubMed:23757278}.
CC -!- DISRUPTION PHENOTYPE: kdpFABCQ and kdpFABC deletion strains are only
CC able to grow in the presence of K(+) concentrations above 60 uM.
CC {ECO:0000269|PubMed:18633573}.
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; AM774418; CAP15447.1; -; Genomic_DNA.
DR RefSeq; WP_010904057.1; NC_010368.1.
DR AlphaFoldDB; B0R9M0; -.
DR SMR; B0R9M0; -.
DR EnsemblBacteria; CAP15447; CAP15447; OE_5053F.
DR GeneID; 5954966; -.
DR GeneID; 62888115; -.
DR KEGG; hsl:OE_5053F; -.
DR HOGENOM; CLU_025728_2_0_2; -.
DR OMA; ILWLWFT; -.
DR PhylomeDB; B0R9M0; -.
DR Proteomes; UP000001321; Plasmid PHS3.
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; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Ion transport; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Plasmid; Potassium;
KW Potassium transport; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..719
FT /note="Potassium-transporting ATPase ATP-binding subunit"
FT /id="PRO_0000433790"
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 228..248
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 624..644
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT TRANSMEM 652..672
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT TRANSMEM 698..718
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT REGION 372..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 318
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 355
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 416..423
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 435
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 554
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 558
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
SQ SEQUENCE 719 AA; 75986 MW; DC3AE79A596BD85A CRC64;
MAEITVTIDT DQQKQAISDS FAKLDPQYLV KNPVLFVVEL GTIIGLVMTI APGLFGATGS
RVYYAVITVL LGFTVIFANY AEAYAELEGE AQADSLRALQ TEAEGKLLQN DDVDIEDISE
DDYEVVASTE IEQDAVVFVD EGDIIPRDGT VVEGSASVDE SAITGESEPV IRQSGGDRTS
VVGGTEVLSD RIKVEVTSEE GESFLDQMIG LVEDAQRQKT PNEIAMTILL SGLTLVFVVA
VATMFFFGEY LASFVGGFAG LDVAELVALL VALMPTTIGA LLAAIRVAGM TRVTRRNVIA
KSGRAVEAAG DLDALILDKT GTITTGERVA QDFHPLGDAD DADVVRASYQ SSLYDETTEG
RSIVKLAEKM NGKVQTDGGQ SASEELDEPG DSVDAPRDVS VTLDAEGLSE SNFVPFSAET
RMSGIDLSDG TEIRKGAVDA VEEYATTVPG KLRQKSNAIS ESGGTPLAIA VDGQVVGIIE
LQDELKPGIA DRIAEIQKMG VETIMATGDN QRTARWVADQ VGIDEFHAEF DPEEKIELVE
DIQDDGKLVG MTGDGTNDAP ALAKADVGLA MNAGTNAAKE AGNMVDLDSN PSKIIEVVGI
GKQLLMTRGS LTTFSVANDV AKYFVLLPAI LAAAIPGLGA MDILNLSTPA SAVTATLMYN
AFIIPLLIPL ALRGVDYKAQ SGAQLLRKNL IVYGGGGLIA PFIFIKAIDM LFVALGVFQ
