KDPA_RHOOB
ID KDPA_RHOOB Reviewed; 561 AA.
AC C1AUJ4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=ROP_09550;
OS Rhodococcus opacus (strain B4).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=632772;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4;
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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; AP011115; BAH49202.1; -; Genomic_DNA.
DR RefSeq; WP_012688190.1; NC_012522.1.
DR AlphaFoldDB; C1AUJ4; -.
DR SMR; C1AUJ4; -.
DR STRING; 632772.ROP_09550; -.
DR EnsemblBacteria; BAH49202; BAH49202; ROP_09550.
DR KEGG; rop:ROP_09550; -.
DR PATRIC; fig|632772.20.peg.1018; -.
DR HOGENOM; CLU_018614_3_0_11; -.
DR OMA; RQGWAIL; -.
DR OrthoDB; 296671at2; -.
DR Proteomes; UP000002212; 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..561
FT /note="Potassium-transporting ATPase potassium-binding
FT subunit"
FT /id="PRO_1000190744"
FT TRANSMEM 5..25
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 86..106
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 177..197
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 281..301
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 488..508
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 537..557
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
SQ SEQUENCE 561 AA; 57687 MW; 54B29B9429CACC16 CRC64;
MTPALAAGLQ VVFVLAVLAV AYVPVGDYMA RVYESRRHLR VESVLYRLCR IDPHAEQTWY
GYAGSVLGFS AASVLFLYAL QRIQGVLPLS GDLSGVSPAV AFNTAVSFVT NTNWQSYAPE
TTMSNLTQPV GLAVQNFVSA AVGMAVAVAL IRGFVRVSRG GEIGNFWVDL TRGSLRILLP
FSFVIALILL SQGVIQSFHP GFASTGLDGN SVTNALAPVA SQEAIKELGT NGGGILAANS
AHPFENPTPV SNIVEILAIL LIPVSLTRTF GTMVGERKQG LTLLAVMGIL WGSLLAVTLA
AESGRRGVAA TAAGAMMEGK EVRFGIPGTA LFAVSTTGTS TGAVNSAHDS LSPLGGGAVL
LNMLLGEIAP GGVGTGLYGI LVLALIAVFV GGLLVGRTPE YLGKKLRQRE ITLAALSVLV
MPALVLIGTG ITVILSSTTG YQGNSGDPGS PGSIHGFSEV LYAFASASNN NGSAFGGLTV
TSDWFQTALG LCMLFGRFLP IIFVLALAGS LASQKKTAAG TGTLPTAGPM FTGLLTGTVV
LVAALTFFPA LALGPIAEAL Q