ID   KDPC_RHORT              Reviewed;         193 AA.
AC   Q2RV87;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 86.
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=Rru_A1157;
OS   Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS   NCIMB 8255 / S1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=269796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX   PubMed=21886856; DOI=10.4056/sigs.1804360;
RA   Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA   Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA   Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y.,
RA   Roberts G.P., Reslewic S., Schwartz D.C.;
RT   "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL   Stand. Genomic Sci. 4:293-302(2011).
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; CP000230; ABC21958.1; -; Genomic_DNA.
DR   RefSeq; WP_011388912.1; NC_007643.1.
DR   RefSeq; YP_426245.1; NC_007643.1.
DR   AlphaFoldDB; Q2RV87; -.
DR   SMR; Q2RV87; -.
DR   STRING; 269796.Rru_A1157; -.
DR   EnsemblBacteria; ABC21958; ABC21958; Rru_A1157.
DR   KEGG; rru:Rru_A1157; -.
DR   PATRIC; fig|269796.9.peg.1219; -.
DR   eggNOG; COG2156; Bacteria.
DR   HOGENOM; CLU_077094_2_0_5; -.
DR   OMA; KYFWPRP; -.
DR   OrthoDB; 1912405at2; -.
DR   PhylomeDB; Q2RV87; -.
DR   Proteomes; UP000001929; 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 inner membrane; Cell membrane; Ion transport; Membrane;
KW   Nucleotide-binding; Potassium; Potassium transport; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..193
FT                   /note="Potassium-transporting ATPase KdpC subunit"
FT                   /id="PRO_1000022309"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00276"
SQ   SEQUENCE   193 AA;  20053 MW;  0975B1CEC8FADDEC CRC64;
     MLRTLRPALV LFAALTLLTG VAYPLAVTGL AQVLFPEQAN GSLIERGGTV IGSALIAQAF
     TGEAYFHPRP SMAGTGYEAN NSGASNLGPT NQGLVDQVAA RITAAKEANP GNYGGVPADL
     VTASGSGLDP HISQAAARWQ AARVAKARGL DLQRAVALVY EFTSPRQLGI LGEPRVNVLA
     INLALDERFP LAH