KDPA_DEIRA
ID KDPA_DEIRA Reviewed; 568 AA.
AC Q9RZN7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 128.
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=DR_B0086;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OG Plasmid megaplasmid MP1.
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
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; AE001826; AAF12536.1; -; Genomic_DNA.
DR PIR; D75627; D75627.
DR RefSeq; NP_051619.1; NC_000958.1.
DR RefSeq; WP_010883954.1; NZ_CP015083.1.
DR AlphaFoldDB; Q9RZN7; -.
DR SMR; Q9RZN7; -.
DR EnsemblBacteria; AAF12536; AAF12536; DR_B0086.
DR KEGG; dra:DR_B0086; -.
DR PATRIC; fig|243230.17.peg.84; -.
DR HOGENOM; CLU_018614_3_0_0; -.
DR InParanoid; Q9RZN7; -.
DR OMA; RQGWAIL; -.
DR OrthoDB; 296671at2; -.
DR BRENDA; 7.2.2.6; 1856.
DR Proteomes; UP000002524; Plasmid megaplasmid MP1.
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..568
FT /note="Potassium-transporting ATPase potassium-binding
FT subunit"
FT /id="PRO_0000166492"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 421..441
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 471..491
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 492..512
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 528..548
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
SQ SEQUENCE 568 AA; 60359 MW; 4576955BC99F82B7 CRC64;
MSASLLQFVV LLGVMAALVV PVGNWLYGVA TGQKDTALER LTYRVIGINP RERMDWKRYG
LAIVVSNLVM LLLAYLLIRL QGALPWNPAG LAAQSPDLAW NTVVSFMTNT NWQAYSGEQS
LSYFSQMAVI TTFMFTSAAT GFAAALAFMR GLAGRDGTNL GNFWVDVTRL IYRVLLPVCF
GLALVFVWQG MPQTLGAYAN ATTLEGAAQR IALGPVASLE SIKHVGTNGG GFFSMNAAHP
FENPTPLTNA LHILSMLLLP SALTYVFGRM LGNLKQGWVI FGGMLVMFVG FLGTVYSFEQ
AGNPILSKLG AEQAITATQA GGNMEGKEVR FGIAQTSLFA TTTTAATTGS VDSMHDSYTG
MGGFVPMLQM MLNNVFGGKG VGFINFVQYL VLGVFIAGLM VGRTPEFLGK KIEAKEVKLT
MLAVLAHPLS ILGFTALACV LPGALNSLNN PGPHGFSEIL YAYTSGTANN GSAFAGLSAN
TFFYNLTIGL SMLMGRYLTL LPMLAVAGML AAKRRVPAGS GTLPTDTALF GALTVFVILI
VGALTFLPAL TLGPVADHLQ MLRGVVLK
