KDPA_HALSA
ID KDPA_HALSA Reviewed; 582 AA.
AC P57684;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 25-MAY-2022, entry version 115.
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}; OrderedLocusNames=VNG_6176G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OG Plasmid pNRC200.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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.
CC {ECO:0000255|HAMAP-Rule:MF_00275}.
CC -!- SUBUNIT: The system is composed of three essential subunits: KdpA, KdpB
CC and KdpC. {ECO:0000255|HAMAP-Rule:MF_00275}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00275};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00275}.
CC -!- SIMILARITY: Belongs to the KdpA family. {ECO:0000255|HAMAP-
CC Rule:MF_00275}.
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DR EMBL; AE004438; AAG20843.1; -; Genomic_DNA.
DR RefSeq; WP_010904056.1; NZ_BK010831.1.
DR AlphaFoldDB; P57684; -.
DR SMR; P57684; -.
DR EnsemblBacteria; AAG20843; AAG20843; VNG_6176G.
DR GeneID; 5954969; -.
DR GeneID; 62888114; -.
DR KEGG; hal:VNG_6176G; -.
DR PATRIC; fig|64091.14.peg.2200; -.
DR HOGENOM; CLU_018614_3_0_2; -.
DR InParanoid; P57684; -.
DR OMA; RQGWAIL; -.
DR OrthoDB; 12407at2157; -.
DR PhylomeDB; P57684; -.
DR Proteomes; UP000000554; Plasmid pNRC200.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008556; F:P-type potassium transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0030955; F:potassium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
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 3: Inferred from homology;
KW Cell membrane; Ion transport; Membrane; Plasmid; Potassium;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..582
FT /note="Potassium-transporting ATPase potassium-binding
FT subunit"
FT /id="PRO_0000166541"
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
