KDPC_BACCN
ID KDPC_BACCN Reviewed; 192 AA.
AC A7GLG5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 88.
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=Bcer98_0626;
OS Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=315749;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98;
RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "Extending the Bacillus cereus group genomics to putative food-borne
RT pathogens of different toxicity.";
RL Chem. Biol. Interact. 171:236-249(2008).
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; CP000764; ABS20973.1; -; Genomic_DNA.
DR RefSeq; WP_011983729.1; NC_009674.1.
DR AlphaFoldDB; A7GLG5; -.
DR SMR; A7GLG5; -.
DR STRING; 315749.Bcer98_0626; -.
DR EnsemblBacteria; ABS20973; ABS20973; Bcer98_0626.
DR GeneID; 56416217; -.
DR KEGG; bcy:Bcer98_0626; -.
DR eggNOG; COG2156; Bacteria.
DR HOGENOM; CLU_077094_1_0_9; -.
DR OMA; KYFWPRP; -.
DR OrthoDB; 1912405at2; -.
DR Proteomes; UP000002300; 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..192
FT /note="Potassium-transporting ATPase KdpC subunit"
FT /id="PRO_1000078791"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00276"
SQ SEQUENCE 192 AA; 21119 MW; 7EA9F2D602F806FD CRC64;
MTEKQNLFGP VVRLTGVLVV LCGLIYPAMV TGIAQGVMKD HADGSLIYEK GEIIGSKRIG
QEFTSAKYFH GRISSIAYKA EGSGSNNYAP SNPELRQRTE ESIEKWKEDN PSVPVREVPI
DLVTNSGSGL DPDISPKAAY AQVDRVAKET KISKEELKAI IASHIEGRAF GLYGEERVNV
LQLNMEVKKR IQ
