ID   KDPC_SALTY              Reviewed;         194 AA.
AC   Q8ZQW3;
DT   06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=STM0704;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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; AE006468; AAL19648.1; -; Genomic_DNA.
DR   RefSeq; NP_459689.1; NC_003197.2.
DR   RefSeq; WP_000579804.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZQW3; -.
DR   SMR; Q8ZQW3; -.
DR   STRING; 99287.STM0704; -.
DR   PaxDb; Q8ZQW3; -.
DR   EnsemblBacteria; AAL19648; AAL19648; STM0704.
DR   GeneID; 1252224; -.
DR   KEGG; stm:STM0704; -.
DR   PATRIC; fig|99287.12.peg.737; -.
DR   HOGENOM; CLU_077094_2_0_6; -.
DR   OMA; KYFWPRP; -.
DR   PhylomeDB; Q8ZQW3; -.
DR   BioCyc; SENT99287:STM0704-MON; -.
DR   Proteomes; UP000001014; 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; IBA:GO_Central.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
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..194
FT                   /note="Potassium-transporting ATPase KdpC subunit"
FT                   /id="PRO_0000197008"
FT   TRANSMEM        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00276"
SQ   SEQUENCE   194 AA;  20439 MW;  F0CA57CD9D5B6BDF CRC64;
     MIGLRPAFST MLFLLLLTGG VYPLLTTALG QWWFPWQANG SLIHKDNVIR GSALIGQSFT
     AAGYFHGRPS ATADTPYNPL ASGGSNLAAS NPELDAQIQA RVAALRAANP QASSAVPVEL
     ATASASGLDN NLTPGAAAWQ IPRVAAARQL PVEQVAQLVA EYTHRPLARF LGQPVVNIVE
     LNLALDALQG HRAK