KDPA_METB6
ID KDPA_METB6 Reviewed; 584 AA.
AC A7I5F0;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 76.
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=Mboo_0443;
OS Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanoregulaceae; Methanoregula.
OX NCBI_TaxID=456442;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21154 / JCM 14090 / 6A8;
RX PubMed=25998264; DOI=10.1099/mic.0.000117;
RA Braeuer S., Cadillo-Quiroz H., Kyrpides N., Woyke T., Goodwin L.,
RA Detter C., Podell S., Yavitt J.B., Zinder S.H.;
RT "Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic
RT peatland environments.";
RL Microbiology 161:1572-1581(2015).
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; CP000780; ABS54961.1; -; Genomic_DNA.
DR AlphaFoldDB; A7I5F0; -.
DR SMR; A7I5F0; -.
DR STRING; 456442.Mboo_0443; -.
DR EnsemblBacteria; ABS54961; ABS54961; Mboo_0443.
DR KEGG; mbn:Mboo_0443; -.
DR eggNOG; arCOG04804; Archaea.
DR HOGENOM; CLU_018614_3_0_2; -.
DR OMA; RQGWAIL; -.
DR Proteomes; UP000002408; 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 Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..584
FT /note="Potassium-transporting ATPase potassium-binding
FT subunit"
FT /id="PRO_1000114688"
FT TRANSMEM 8..28
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 139..159
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 440..460
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 507..527
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 544..564
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
SQ SEQUENCE 584 AA; 62526 MW; DACB2E42296270BF CRC64;
MSVNDWAFLV LIGVILALLL IPTGEFMFRV YTGKKTFLSP LFVPVEAWIL KACGAGSDEE
MDWKSFAVAM MIFSVIGIVF VFILQEVQQF LPLNPLGATA VPWDLSLNTA VSFATNTNWQ
FYVPETTVSY LTQMIGLTVQ NFMSAAVGMV VLVAFIYGFS RRSSHTIGNF WVLLLRSIWI
LLPLSFVIAL VLVSQGAPQT LSGPVTVPLL NATNDSGGNI ITTQLISLGP AASQIAVKML
GTNGGGFFNA NSAHPFENPT WFTDLVEIVA ILLIPVSLCF MFGKMIGSVK KGIAILIAMM
ILFVPLLGLG IWSEIGGNPA FTPLGISQAP SHLQSGGNME GKEVRFGPVQ SAAFSVITTV
TSCGAVNSMH DSFMPLGGLV QIFDIQLGEI VFGGVGSGLY CMLVFVIIAM FIAGLMVGRT
PELYGKKIEP YEMKLSTIHI LIPIFLILIG TAIAVSITAG TSMTANPGPH GFSEILYAFS
SVSQNNGSAF AGLSSDTFYN LTTAFCMFVG RYAIAIITLA LAGAFVAKKI VPPGEGTLQD
HRPLFIIWVV FTILIIGALS FLPALSLGPV VEFLIQMGRG VIHV