KDPA_CLOAB
ID KDPA_CLOAB Reviewed; 557 AA.
AC O32327;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 25-MAY-2022, entry version 127.
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=CA_C3682;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=9226259; DOI=10.1128/jb.179.14.4501-4512.1997;
RA Treuner-Lange A., Kuhn A., Duerre P.;
RT "The kdp system of Clostridium acetobutylicum: cloning, sequencing, and
RT transcriptional regulation in response to potassium concentration.";
RL J. Bacteriol. 179:4501-4512(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
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 -!- INDUCTION: By low potassium concentration.
CC -!- SIMILARITY: Belongs to the KdpA family. {ECO:0000255|HAMAP-
CC Rule:MF_00275}.
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DR EMBL; U44892; AAC45477.1; -; Genomic_DNA.
DR EMBL; AE001437; AAK81603.1; -; Genomic_DNA.
DR PIR; H97351; H97351.
DR PIR; T46842; T46842.
DR RefSeq; NP_350263.1; NC_003030.1.
DR RefSeq; WP_010966943.1; NC_003030.1.
DR AlphaFoldDB; O32327; -.
DR SMR; O32327; -.
DR STRING; 272562.CA_C3682; -.
DR EnsemblBacteria; AAK81603; AAK81603; CA_C3682.
DR GeneID; 45000180; -.
DR KEGG; cac:CA_C3682; -.
DR PATRIC; fig|272562.8.peg.3871; -.
DR eggNOG; COG2060; Bacteria.
DR HOGENOM; CLU_018614_3_0_9; -.
DR OMA; RQGWAIL; -.
DR OrthoDB; 296671at2; -.
DR BRENDA; 7.2.2.6; 1452.
DR Proteomes; UP000000814; 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 2: Evidence at transcript level;
KW Cell membrane; Ion transport; Membrane; Potassium; Potassium transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..557
FT /note="Potassium-transporting ATPase potassium-binding
FT subunit"
FT /id="PRO_0000166491"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 371..391
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 482..502
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"
FT CONFLICT 145
FT /note="G -> P (in Ref. 1; AAC45477)"
FT /evidence="ECO:0000305"
FT CONFLICT 300..319
FT /note="AEKAGNPALSRIGLSQSMGN -> LRKQEISTLTYRLKSEHGK (in Ref.
FT 1; AAC45477)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 557 AA; 59790 MW; B2840F9AAF016109 CRC64;
MEILQIAIIL IVFVLLCIPI GRYMYKVSEH KKTLLDPVLD KIDGFIYKLS GIQKEEEMNW
KQYIFALLMC NAVPAIIGYI ILRIQAVGIF NPNHVKGMEQ GLTFNTIISF LTNTNLQDYA
GETGASYLSQ MIVITFFMFF AAATGIAVAL AFIRALSGKK KLGNFYVDLV RITTRILLPL
SIIVAIFYIG QGVPQTLSAN KTVTTIEGKL QNIPLGPVAS LEAIKLIGTN GGGFFSANSS
HPFENPTPLT NSVQIITLLL LAGSMVVCFG HMIKKKKQAV AIFAAMMVLL LAGAAICFSA
EKAGNPALSR IGLSQSMGNL EGKEERFGIA GSSLFTTVTT DTSCGAVNNM HDSLTPIGGA
VPLINMMLNV IFGGVGVGFM NMIMYAILTV FLCGLMVGRT PEFLNKKIEG KEIKLVAFAI
IVHPFLILMS SALALTTKQG LAGISNPGFH GLTQVLYQFT SSAANNGSGF EGLIDNTMFW
NVSAGVVMFL GRYLSIIILL AVASSFAAKR AVPATQGTFK TDNTIFTVTL IVIIVIIGAL
TFLPAVALGP ISEYLTL
