KDPA_RHORT
ID KDPA_RHORT Reviewed; 569 AA.
AC Q2RV89;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 92.
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=Rru_A1155;
OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS NCIMB 8255 / S1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=269796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX PubMed=21886856; DOI=10.4056/sigs.1804360;
RA Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y.,
RA Roberts G.P., Reslewic S., Schwartz D.C.;
RT "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL Stand. Genomic Sci. 4:293-302(2011).
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 periplasmic 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 inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00275}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00275}.
CC -!- SIMILARITY: Belongs to the KdpA family. {ECO:0000255|HAMAP-
CC Rule:MF_00275}.
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DR EMBL; CP000230; ABC21956.1; -; Genomic_DNA.
DR RefSeq; WP_011388910.1; NC_007643.1.
DR RefSeq; YP_426243.1; NC_007643.1.
DR AlphaFoldDB; Q2RV89; -.
DR SMR; Q2RV89; -.
DR STRING; 269796.Rru_A1155; -.
DR EnsemblBacteria; ABC21956; ABC21956; Rru_A1155.
DR KEGG; rru:Rru_A1155; -.
DR PATRIC; fig|269796.9.peg.1217; -.
DR eggNOG; COG2060; Bacteria.
DR HOGENOM; CLU_018614_3_0_5; -.
DR OMA; RQGWAIL; -.
DR OrthoDB; 296671at2; -.
DR PhylomeDB; Q2RV89; -.
DR Proteomes; UP000001929; 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 inner membrane; Cell membrane; Ion transport; Membrane; Potassium;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..569
FT /note="Potassium-transporting ATPase potassium-binding
FT subunit"
FT /id="PRO_1000022242"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 383..403
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 461..481
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 531..551
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
SQ SEQUENCE 569 AA; 59474 MW; B3EC47A83130D369 CRC64;
MDANAILQVV LFCAIILGLT PLLGGYMARV FSGERVLLSV VFGPLERGLY RLSGVRPKEE
QHWAAYALSM LVFNLAGLLG LYLILRVQGW LPLNPAGLGA VAPDLAFNTA VSFVTNTNWQ
AYGGESTLSY FSQMVGLTVQ NFVSAATGIA VLVALIRGFA RRSARTLGNF WVDLTRTVLY
LLLPLAFVTA LVLVWQGAPQ TLGDYVQAAP LEGGSQVIAL GPVASQEAIK QLGSNGGGFF
SVNSAHPFEN PTPLSNLIEM VLLLAVAAGL TNTFGRMVGD TRQGWALFAA MSLMFVVGLG
VTLWQESAAN PAMVVAGIEA GGGNMEGKEV RLGVANSAIW AVATTAASNG SVNAMHDSFM
PLAGMVPMIN MMLGEVIFGG VGAGLYGMLI FVMVTVFIAG LMVGRTPEYL GKKIEAREMK
LAVISLLVPP LCILGFGAVA LTWPQAAASV QDPGPHGLTE ALYAYVSGTA NNGSAFAGFA
ANVFPHNLMI GLAMLIGRFL VILPVLAIAG SLGAKKIVPV SAGTFPTHGG LFIGLLVGVI
VVVGGLTYFP VLALGPILEQ LMLRSGSLF
