KDPA_ACIC5
ID KDPA_ACIC5 Reviewed; 590 AA.
AC C1FA47;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 66.
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=ACP_0429;
OS Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / BCRC 80197 / JCM
OS 7670 / NBRC 15755 / NCIMB 13165 / 161).
OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae;
OC Acidobacterium.
OX NCBI_TaxID=240015;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51196 / DSM 11244 / BCRC 80197 / JCM 7670 / NBRC 15755 / NCIMB
RC 13165 / 161;
RX PubMed=19201974; DOI=10.1128/aem.02294-08;
RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT "Three genomes from the phylum Acidobacteria provide insight into the
RT lifestyles of these microorganisms in soils.";
RL Appl. Environ. Microbiol. 75:2046-2056(2009).
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; CP001472; ACO31481.1; -; Genomic_DNA.
DR RefSeq; WP_012680823.1; NC_012483.1.
DR AlphaFoldDB; C1FA47; -.
DR SMR; C1FA47; -.
DR STRING; 240015.ACP_0429; -.
DR EnsemblBacteria; ACO31481; ACO31481; ACP_0429.
DR KEGG; aca:ACP_0429; -.
DR eggNOG; COG2060; Bacteria.
DR HOGENOM; CLU_018614_3_0_0; -.
DR OMA; RQGWAIL; -.
DR OrthoDB; 296671at2; -.
DR Proteomes; UP000002207; 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..590
FT /note="Potassium-transporting ATPase potassium-binding
FT subunit"
FT /id="PRO_1000190726"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 64..84
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 273..293
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 511..531
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 552..572
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
SQ SEQUENCE 590 AA; 63326 MW; E245DD209919C1F0 CRC64;
MTVNGWLQIG IFIAAVLLGA KPLGVYMAAV FERRHTWLDP VLVPVEKLLY RLTAVKAEEE
MHWTAYCASM LIFSAATMLL TYLIERVQQF LPLNPQHLGG VPAQLAWNTA ISFTTNTNWQ
AYTPESTMSY LTQMVGLATH NFWSAAVGIA LAIAFIRGIA RKEMKTLGNF WVDMTRAILW
VLLPICVVFA LVLTSQGVIQ NLKSYTVAHV VQPQSQTQTV NGKTVTTTDS TQTIAQGPVA
SQEAIKMLGT NGGGFFNANS SHPFENPTPL SNMLEMISIF LIPAGLTVTL GQMTGSPRHG
WAVLGAMLIL WFAGVATCYW AEAQPNPLFH GVNQQATALQ AGGNMEGKEV RFGIADSALF
ATVTTDASCG AVNAMHDSFM PLGGMVPLTN IMLGEIVFGG VGAGLYGMLV FVIVAVFIAG
LMVGRTPEYL GNKIQAYDVQ MAMLYLLIFP LIILGFSAVA VLTPHLGLPS ISNPGPHGLT
QILYAYSSAT GNNGSAFAGL NANTSWYNLS LGFAMFIGRF LMIVPMLALA GNLAQKKNVP
ETLGTFPVTT PLFTVLLTSV IIVVGALTFL PALSLGPILE HLLLQAGRTF
