KDPA_DECAR
ID KDPA_DECAR Reviewed; 592 AA.
AC Q47H38;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 94.
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=Daro_1087;
OS Dechloromonas aromatica (strain RCB).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC Dechloromonas.
OX NCBI_TaxID=159087;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCB;
RX PubMed=19650930; DOI=10.1186/1471-2164-10-351;
RA Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G.,
RA Lapidus A.;
RT "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB:
RT indications of a surprisingly complex life-style and cryptic anaerobic
RT pathways for aromatic degradation.";
RL BMC Genomics 10:351-351(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; CP000089; AAZ45843.1; -; Genomic_DNA.
DR RefSeq; WP_011286852.1; NC_007298.1.
DR AlphaFoldDB; Q47H38; -.
DR SMR; Q47H38; -.
DR STRING; 159087.Daro_1087; -.
DR EnsemblBacteria; AAZ45843; AAZ45843; Daro_1087.
DR KEGG; dar:Daro_1087; -.
DR eggNOG; COG2060; Bacteria.
DR HOGENOM; CLU_018614_3_0_4; -.
DR OMA; RQGWAIL; -.
DR OrthoDB; 296671at2; -.
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; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..592
FT /note="Potassium-transporting ATPase potassium-binding
FT subunit"
FT /id="PRO_1000022218"
FT TRANSMEM 7..27
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 132..152
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 175..195
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 310..330
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 449..469
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 513..533
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 556..576
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
SQ SEQUENCE 592 AA; 62871 MW; FA0FCA5EC03975C1 CRC64;
MSNHAWILLG IFLVVLLLTV KPLGTYIANV MEGRFRLAGK IESPIYRLCG IRPDEEMGWL
KYACAILLFN VLGVLAVYAL QRLQAELPLN PQVFPAVSPD SAFNTAISFA TNTNWQGYVG
EATMSYLTQM LALAVQNFFS AATGIVVVIA LIRGFARHTA KTFGNAWVDL TRITLHVLLP
ISIIYAVFLT GQGVIQNFNA YKDVTTLEVT SFDNPKLDDA GQPLKDDKGA VVTEPAQTQT
QTLAMGPVAS QEAIKMLGTN GGGFMNANSA HPYENPTPLS NFIQMLSIFL IPAALCFTFG
RIVGDTRQGW AVLAAMTLMF VALAYTAMHF EQQANPLLTQ LGVDPASGNM EGKETRFGIG
DSGLFATITT LASCGAVNAM HDSFTPLGGL VPLIDMQLGE VVFGGVGTGL YGMLVFAIMA
VFIAGLMIGR TPEYLGKKIE AFEMKMVSIA ILVTPLLVLV GTAIAVMLAD GKAGIANPGA
HGFSEILYAF TSAANNNGSA FAGLSANTPF YNVMLGIAMW FGRFGVIVPV LAIAGSLAAK
KRIAVGAGTL PTHGPLFVTL LIGTVLLVGL LNYVPALALG PVIEHLVLWA AH