KDPC_HALS3
ID KDPC_HALS3 Reviewed; 216 AA.
AC B0R9M1;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Potassium-transporting ATPase KdpC subunit {ECO:0000255|HAMAP-Rule:MF_00276};
DE AltName: Full=ATP phosphohydrolase [potassium-transporting] C chain {ECO:0000255|HAMAP-Rule:MF_00276};
DE AltName: Full=Potassium-binding and translocating subunit C {ECO:0000255|HAMAP-Rule:MF_00276};
DE AltName: Full=Potassium-translocating ATPase C chain {ECO:0000255|HAMAP-Rule:MF_00276};
GN Name=kdpC {ECO:0000255|HAMAP-Rule:MF_00276, ECO:0000312|EMBL:CAP15448.1};
GN OrderedLocusNames=OE_5054F {ECO:0000312|EMBL:CAP15448.1};
OS Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OG Plasmid PHS3 {ECO:0000312|EMBL:CAP15448.1}.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=478009;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT R1 compared to that of strain NRC-1.";
RL Genomics 91:335-346(2008).
RN [2]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=18633573; DOI=10.1007/s00792-008-0177-3;
RA Strahl H., Greie J.C.;
RT "The extremely halophilic archaeon Halobacterium salinarum R1 responds to
RT potassium limitation by expression of the K+-transporting KdpFABC P-type
RT ATPase and by a decrease in intracellular K+.";
RL Extremophiles 12:741-752(2008).
RN [3]
RP INDUCTION.
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=21947979; DOI=10.1007/s00792-011-0395-y;
RA Kixmueller D., Strahl H., Wende A., Greie J.C.;
RT "Archaeal transcriptional regulation of the prokaryotic KdpFABC complex
RT mediating K(+) uptake in H. salinarum.";
RL Extremophiles 15:643-652(2011).
RN [4]
RP FUNCTION, AND INDUCTION.
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=23757278; DOI=10.1111/j.1758-2229.2012.00326.x;
RA Kixmueller D., Greie J.C.;
RT "An ATP-driven potassium pump promotes long-term survival of Halobacterium
RT salinarum within salt crystals.";
RL Environ. Microbiol. Rep. 4:234-241(2012).
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 acts as a catalytic chaperone that increases the ATP-binding affinity
CC of the ATP-hydrolyzing subunit KdpB by the formation of a transient
CC KdpB/KdpC/ATP ternary complex (By similarity). The Kdp system is
CC essential for growth under K(+) limitation, and for survival under
CC desiccation and salt crystal inclusion (PubMed:18633573,
CC PubMed:23757278). {ECO:0000250|UniProtKB:P03961,
CC ECO:0000269|PubMed:18633573, ECO:0000269|PubMed:23757278}.
CC -!- SUBUNIT: The system is composed of three essential subunits: KdpA, KdpB
CC and KdpC. The complex also contains KdpF, a small non-essential
CC subunit. {ECO:0000250|UniProtKB:P03961}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00276};
CC Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00276}.
CC -!- INDUCTION: Up-regulated in response to K(+) limitation
CC (PubMed:18633573, PubMed:21947979). Induced under desiccating
CC conditions (PubMed:23757278). {ECO:0000269|PubMed:18633573,
CC ECO:0000269|PubMed:21947979, ECO:0000269|PubMed:23757278}.
CC -!- DISRUPTION PHENOTYPE: kdpFABCQ and kdpFABC deletion strains are only
CC able to grow in the presence of K(+) concentrations above 60 uM.
CC {ECO:0000269|PubMed:18633573}.
CC -!- SIMILARITY: Belongs to the KdpC family. {ECO:0000255|HAMAP-
CC Rule:MF_00276}.
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DR EMBL; AM774418; CAP15448.1; -; Genomic_DNA.
DR RefSeq; WP_010904058.1; NC_010368.1.
DR AlphaFoldDB; B0R9M1; -.
DR SMR; B0R9M1; -.
DR EnsemblBacteria; CAP15448; CAP15448; OE_5054F.
DR GeneID; 5954967; -.
DR GeneID; 62888116; -.
DR KEGG; hsl:OE_5054F; -.
DR HOGENOM; CLU_077094_1_0_2; -.
DR OMA; KYFWPRP; -.
DR PhylomeDB; B0R9M1; -.
DR Proteomes; UP000001321; Plasmid PHS3.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008556; F:P-type potassium transmembrane transporter activity; IEA:InterPro.
DR HAMAP; MF_00276; KdpC; 1.
DR InterPro; IPR003820; KdpC.
DR PANTHER; PTHR30042; PTHR30042; 1.
DR Pfam; PF02669; KdpC; 1.
DR PIRSF; PIRSF001296; K_ATPase_KdpC; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Ion transport; Membrane; Nucleotide-binding;
KW Plasmid; Potassium; Potassium transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..216
FT /note="Potassium-transporting ATPase KdpC subunit"
FT /id="PRO_0000433791"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00276"
FT REGION 197..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 216 AA; 23768 MW; 976616E5C59E6107 CRC64;
MNRQDLAVPL RLLGVSLLVF GLLYQGSLMA IGDAVFPNSS AGSPVYVDGQ EQPVGSQMIG
QQFRPGQPED VQYFWSRPSA NDYNAMTSAS TNWGPTNPLL SERVRADLQN ISQYETPDDS
VPVNLVSESG SSYDAHISPA AAEYQVLRVA NQTGISEQRL NEMIDEATKE PWLGIWGHER
VNVLELNLMV RDALNEQNET DQNSDMNASE IANGDH
