KDPA_THEVO
ID KDPA_THEVO Reviewed; 585 AA.
AC Q97BF7;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 104.
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=TV0499;
GN ORFNames=TVG0487282;
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000011; BAB59641.1; -; Genomic_DNA.
DR RefSeq; WP_010916757.1; NC_002689.2.
DR AlphaFoldDB; Q97BF7; -.
DR SMR; Q97BF7; -.
DR STRING; 273116.14324714; -.
DR EnsemblBacteria; BAB59641; BAB59641; BAB59641.
DR GeneID; 1441015; -.
DR KEGG; tvo:TVG0487282; -.
DR eggNOG; arCOG04804; Archaea.
DR HOGENOM; CLU_018614_3_0_2; -.
DR OMA; RQGWAIL; -.
DR OrthoDB; 12407at2157; -.
DR PhylomeDB; Q97BF7; -.
DR Proteomes; UP000001017; Chromosome.
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 3: Inferred from homology;
KW Cell membrane; Ion transport; Membrane; Potassium; Potassium transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..585
FT /note="Potassium-transporting ATPase potassium-binding
FT subunit"
FT /id="PRO_0000166543"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 437..457
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 502..522
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 547..567
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
SQ SEQUENCE 585 AA; 64701 MW; 0F552556A5D553AD CRC64;
MIFPAEDVYF WSKFFATERA VSGVIIIFIY LGITSIFSYV LSFYIAKIYR DEPTFLRKLT
GSVISFFEKI IGESENHQME FKEYFINLLL FNFFAGLISF LVIMYQKYLP FSYYATGMSP
SLDFNTVVSF LTNTNLQHYS NPFRLSYFSQ TFVITGLMFL SAGTGFAASM AFVRGLRTDV
GKIGNFYHDF LVSIFDLILP LSILVTIILI LAGVPETIQR FISVTPFFTN NTVNIPLGPV
ATLEAIKNIG TNGGGFYGAN AGFPFENPDW FTNLLEFVSF TIIPLGSLMA LGIVFEDRKF
GRMLYYVIMF FFVFDGLFAF FGEYVGVPFL HIGYYTGNML GKETAIGVSQ SSIFAVGATL
TSTGASDGAL VSYTPAGIIG VLIGLLLNDP LGGVGTGVLN IFMYIIFTVF IGSLMVGKLP
ELMSLRIGSK EIKYSTLSLV THPLLVVIPL GITLMIPHLS STFVNPNSSR ITELLYEFAS
AASNNGSEMG GFLTNQPYFN YLDGVIMLLG RYLLMGFQLV IAQSFSIKKA KVQYLRSIDT
SNSVFALLLI SAMLIIGLLS YFPIIVLGPL LSWTHDFSLI VGAIL
