ID   KDPC_CLOD6              Reviewed;         208 AA.
AC   Q186E8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, 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=CD630_15930;
OS   Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=272563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630;
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA   Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT   mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(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; AM180355; CAJ68458.1; -; Genomic_DNA.
DR   RefSeq; WP_009896752.1; NZ_CP010905.2.
DR   RefSeq; YP_001088094.1; NC_009089.1.
DR   AlphaFoldDB; Q186E8; -.
DR   SMR; Q186E8; -.
DR   STRING; 272563.CD630_15930; -.
DR   EnsemblBacteria; CAJ68458; CAJ68458; CD630_15930.
DR   GeneID; 66354002; -.
DR   KEGG; cdf:CD630_15930; -.
DR   KEGG; pdc:CDIF630_01766; -.
DR   PATRIC; fig|272563.120.peg.1668; -.
DR   eggNOG; COG2156; Bacteria.
DR   OMA; KYFWPRP; -.
DR   PhylomeDB; Q186E8; -.
DR   BioCyc; PDIF272563:G12WB-1731-MON; -.
DR   Proteomes; UP000001978; 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; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..208
FT                   /note="Potassium-transporting ATPase KdpC subunit"
FT                   /id="PRO_1000022280"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00276"
SQ   SEQUENCE   208 AA;  22242 MW;  88FB3139FB4BAE71 CRC64;
     MKTLKPALLV SIVLLVVCGL VYPLVLTGVS QVAFKDKANG SMIEVNGVKV GSELIGQSFT
     DARFFKGRVS SVNYNTYTKE DLVPDKDGNT SYGGVSSGSF NYGATNPELH DRVQKDIEKF
     LKDNPTVKRE DIPTDLLTAS GSGLDPNISP ASAKIQIPAI AKASGISESK LQKIVDDNTS
     KKLFGVLGED RVNVLKVNVE VAKILGLI