KDPA_HALS3
ID KDPA_HALS3 Reviewed; 582 AA.
AC B0R9L9;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Potassium-transporting ATPase potassium-binding subunit {ECO:0000255|HAMAP-Rule:MF_00275};
DE AltName: Full=ATP phosphohydrolase [potassium-transporting] A chain {ECO:0000255|HAMAP-Rule:MF_00275};
DE AltName: Full=Potassium-binding and translocating subunit A {ECO:0000255|HAMAP-Rule:MF_00275};
DE AltName: Full=Potassium-translocating ATPase A chain {ECO:0000255|HAMAP-Rule:MF_00275};
GN Name=kdpA {ECO:0000255|HAMAP-Rule:MF_00275, ECO:0000312|EMBL:CAP15446.1};
GN OrderedLocusNames=OE_5052F {ECO:0000312|EMBL:CAP15446.1};
OS Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OG Plasmid PHS3 {ECO:0000312|EMBL:CAP15446.1}.
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
CC binds the extracellular potassium ions and delivers the ions to the
CC membrane domain of KdpB through an intramembrane tunnel (By
CC similarity). The Kdp system is essential for growth under K(+)
CC limitation, and for survival under desiccation and salt crystal
CC inclusion (PubMed:18633573, PubMed:23757278). {ECO:0000255|HAMAP-
CC Rule:MF_00275, ECO:0000269|PubMed:18633573,
CC ECO:0000269|PubMed:23757278}.
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:P03959}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00275};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00275}.
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 KdpA family. {ECO:0000255|HAMAP-
CC Rule:MF_00275}.
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DR EMBL; AM774418; CAP15446.1; -; Genomic_DNA.
DR RefSeq; WP_010904056.1; NC_010368.1.
DR AlphaFoldDB; B0R9L9; -.
DR SMR; B0R9L9; -.
DR EnsemblBacteria; CAP15446; CAP15446; OE_5052F.
DR GeneID; 5954969; -.
DR GeneID; 62888114; -.
DR KEGG; hsl:OE_5052F; -.
DR HOGENOM; CLU_018614_3_0_2; -.
DR OMA; RQGWAIL; -.
DR PhylomeDB; B0R9L9; -.
DR Proteomes; UP000001321; Plasmid PHS3.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0008556; F:P-type potassium transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0030955; F:potassium ion binding; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00275; KdpA; 1.
DR InterPro; IPR004623; KdpA.
DR PANTHER; PTHR30607; PTHR30607; 1.
DR Pfam; PF03814; KdpA; 1.
DR PIRSF; PIRSF001294; K_ATPaseA; 1.
DR TIGRFAMs; TIGR00680; kdpA; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Ion transport; Membrane; Plasmid; Potassium;
KW Potassium transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..582
FT /note="Potassium-transporting ATPase potassium-binding
FT subunit"
FT /id="PRO_0000433779"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 401..421
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 551..571
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
SQ SEQUENCE 582 AA; 62353 MW; BED86E402335C5C5 CRC64;
MASPPPIVEY AVFFTILAVL VFVAGEYLAW VYREQANSDH RPPGYLSWFE RLDEIFTPIE
NGLYRLSGIN PRREMTWKGY LKAVLVFNVC IWVLLFVVLM FQDALPMNFV GVGGESWDLA
FHTASSFTSN TNQQHYSGET LSVFTHTFGI GIAMFLTPAT GLALMPAFAR AFTNKEDPRL
GNFYENVVRG LVRFLLPISL LIAIILMAEG SVQTILGGQL TANTFTMGIQ NIRIGPHAGI
EAIKMFGTNG GGINAANAAT AFENPTPLSN LVLTLAMPIG TFSAIYAWGA WVGNRSHGVA
IVAAFFVIYM ALTGVAVVGE TGTNAGMVVT GNGLHVDQTV GNMEGKETRF GPTASAIWGL
STTGTTNGGV NSMHNSWTAL GAFSLLFAFA TNNISNGVGT GLLNILMFVI LTAFIGALMI
GRRPQYLGKK LEWQEMRYVF VVILVLPILV LIPQAAAVVY QGAIDSMNNP GFRGFSEVLY
EFFSASANNG SGFEGLGDGT LFFNLVNGVQ VLLARYVPIT AQLAIAGYLA NKKVSPESKG
SLDTDTPAFV GLLIGVIIIV SALVFLPALV FGPIGELLSG GI
