KDPA_RHOE4
ID KDPA_RHOE4 Reviewed; 561 AA.
AC C1A1E9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 75.
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=RER_37260;
OS Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC Rhodococcus erythropolis group.
OX NCBI_TaxID=234621;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887;
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-2005) 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; AP008957; BAH34434.1; -; Genomic_DNA.
DR RefSeq; WP_020908186.1; NC_012490.1.
DR AlphaFoldDB; C1A1E9; -.
DR SMR; C1A1E9; -.
DR STRING; 234621.RER_37260; -.
DR EnsemblBacteria; BAH34434; BAH34434; RER_37260.
DR GeneID; 57486366; -.
DR KEGG; rer:RER_37260; -.
DR eggNOG; COG2060; Bacteria.
DR HOGENOM; CLU_018614_3_0_11; -.
DR OMA; LMMWTEF; -.
DR Proteomes; UP000002204; 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_1000204789"
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 130..150
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 491..511
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 533..553
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
SQ SEQUENCE 561 AA; 57487 MW; F32C28E5855FCFE2 CRC64;
MSPALAAGLQ IAFVLAVLAI AYVPVGDYMA RVYSSTRDLR VESVIYRVGR IDSRAEQTWY
GYAASVLGFS LASALFLYFL QRIQGVLPLS DGLSGVSPAV AFNTAISFVA NTNWQSYTPE
TTMSNFVQPV GLAVQNFVSA AVGMAVAIAL VRGFIRVARG GEIGNFWVDL TRGSLRILLP
FSFVIALILL SQGVIQSFHS GFASTGLDGN AVTNALAPVA SQEAIKELGT NGGGILAANS
AHPFENPTPL SNIVEILAIL LIPVCLTRTF GTLVGDRRQG LTLLAVMGIL WSGLLAVTLA
AESGARGVAA TAAGSMMEGK EVRFGIPGSA LFAVATTGTS TGAVNSAHDS MSPLGGGAVL
LNMLLGEIAP GGVGTGLYGI LVLALIAVFV GGLLVGRTPE YLGKKLGRRE ITLAALSILV
MPALVLIGTA ITVILGSTTG YQGNGGDPGT PGSIHGFSEV LYAFASASNN NGSAFGGLTV
TSDWFQSSLG ICMLLGRFLP IIFVLALAGA LASQKKVAPT AGTLPTSGPM FTGLLTGTVV
LVAALTFFPA LALGPLAEAL Q