ID   KDPC_CERSK              Reviewed;         185 AA.
AC   B9KPZ0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 68.
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};
GN   OrderedLocusNames=RSKD131_2665;
OS   Cereibacter sphaeroides (strain KD131 / KCTC 12085) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=557760;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KD131 / KCTC 12085;
RX   PubMed=19028901; DOI=10.1128/jb.01565-08;
RA   Lim S.-K., Kim S.J., Cha S.H., Oh Y.-K., Rhee H.-J., Kim M.-S., Lee J.K.;
RT   "Complete genome sequence of Rhodobacter sphaeroides KD131.";
RL   J. Bacteriol. 191:1118-1119(2009).
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 inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00276}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00276}.
CC   -!- SIMILARITY: Belongs to the KdpC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00276}.
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DR   EMBL; CP001150; ACM02525.1; -; Genomic_DNA.
DR   RefSeq; WP_015921581.1; NC_011963.1.
DR   AlphaFoldDB; B9KPZ0; -.
DR   SMR; B9KPZ0; -.
DR   EnsemblBacteria; ACM02525; ACM02525; RSKD131_2665.
DR   GeneID; 67448037; -.
DR   KEGG; rsk:RSKD131_2665; -.
DR   HOGENOM; CLU_077094_2_0_5; -.
DR   OMA; KYFWPRP; -.
DR   Proteomes; UP000001597; Chromosome 1.
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 inner membrane; Cell membrane; Ion transport; Membrane;
KW   Nucleotide-binding; Potassium; Potassium transport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..185
FT                   /note="Potassium-transporting ATPase KdpC subunit"
FT                   /id="PRO_1000132524"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00276"
SQ   SEQUENCE   185 AA;  18658 MW;  13088C6E666AE5E0 CRC64;
     MMTHLRPALA SLLALSLLTG VAYPLALTGI AAVIAPDRAA GSLILREGQV VGSALIGQGF
     EGPGYLHPRP SASDWNAAGT SASNLGPTSA ALLAQVQERQ AAYEAQNGAS APVDAVTASG
     SGLDPHVSPA NARAQAGRIA RARGLEEAAV RRLIEAHVEP PLLGLWGQAR VNVLAVNLAL
     DAAGA