KDPC_BACC1
ID KDPC_BACC1 Reviewed; 193 AA.
AC Q73DA2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
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}; OrderedLocusNames=BCE_0811;
OS Bacillus cereus (strain ATCC 10987 / NRS 248).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=222523;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10987 / NRS 248;
RX PubMed=14960714; DOI=10.1093/nar/gkh258;
RA Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL Nucleic Acids Res. 32:977-988(2004).
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. {ECO:0000255|HAMAP-Rule:MF_00276}.
CC -!- SUBUNIT: The system is composed of three essential subunits: KdpA, KdpB
CC and KdpC. {ECO:0000255|HAMAP-Rule:MF_00276}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00276};
CC Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00276}.
CC -!- SIMILARITY: Belongs to the KdpC family. {ECO:0000255|HAMAP-
CC Rule:MF_00276}.
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DR EMBL; AE017194; AAS39743.1; -; Genomic_DNA.
DR RefSeq; WP_001085561.1; NC_003909.8.
DR AlphaFoldDB; Q73DA2; -.
DR SMR; Q73DA2; -.
DR EnsemblBacteria; AAS39743; AAS39743; BCE_0811.
DR GeneID; 59158569; -.
DR KEGG; bca:BCE_0811; -.
DR HOGENOM; CLU_077094_1_0_9; -.
DR OMA; KYFWPRP; -.
DR Proteomes; UP000002527; Chromosome.
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.
DR TIGRFAMs; TIGR00681; kdpC; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Ion transport; Membrane; Nucleotide-binding;
KW Potassium; Potassium transport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..193
FT /note="Potassium-transporting ATPase KdpC subunit"
FT /id="PRO_1000022257"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00276"
SQ SEQUENCE 193 AA; 21224 MW; 19C3B7C13A0D364E CRC64;
MAKKQSILSP IIRITFTFLV LCGLVYPLIV TGIAQAVMKD NADGSLIYND KNEVIGSKLI
GQNFTDPRYF HGRVSSIEYK AEASGSNNYA PSNPDLEKRV EKSIEEWKKQ NPTVPVTEVP
IDLVTNSGSG LDPDISPKAA SVQVERISKI TNIPKETLNQ LIKDQTEGAA LGLFGETRVN
VLKLNLELQK LLK