KDPC_BACCZ
ID KDPC_BACCZ Reviewed; 193 AA.
AC Q63FQ9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=BCE33L0648;
OS Bacillus cereus (strain ZK / E33L).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=288681;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZK / E33L;
RX PubMed=16621833; DOI=10.1128/jb.188.9.3382-3390.2006;
RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D.,
RA Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R.,
RA Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M.,
RA Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R.,
RA Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA Brettin T.S., Gilna P.;
RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT thuringiensis isolates closely related to Bacillus anthracis.";
RL J. Bacteriol. 188:3382-3390(2006).
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; CP000001; AAU19593.1; -; Genomic_DNA.
DR RefSeq; WP_001085546.1; NZ_CP009968.1.
DR AlphaFoldDB; Q63FQ9; -.
DR SMR; Q63FQ9; -.
DR EnsemblBacteria; AAU19593; AAU19593; BCE33L0648.
DR KEGG; bcz:BCE33L0648; -.
DR PATRIC; fig|288681.22.peg.4939; -.
DR OMA; KYFWPRP; -.
DR Proteomes; UP000002612; 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_1000022259"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00276"
SQ SEQUENCE 193 AA; 21253 MW; 243BD4CC93D687D4 CRC64;
MAKKQSILSP IIRITFTFLV LCGLVYPLII TGIAQAVMKD NADGSLIYND KNEVIGSKLI
GQNFTDPRYF HGRVSSIEYK AEASGSNNYA PSNPDLEKRV EKSIEEWKKQ NPSVPVTEVP
IDLVTNSGSG LDPDISPKAA SVQVERISKL TKIPKETLEQ LIQDQTEGAA LGLFGETRVN
VLKLNLELQK LLK