ID   KDPC_CLOAB              Reviewed;         204 AA.
AC   P94606;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   25-MAY-2022, entry version 127.
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=CA_C3680;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=9226259; DOI=10.1128/jb.179.14.4501-4512.1997;
RA   Treuner-Lange A., Kuhn A., Duerre P.;
RT   "The kdp system of Clostridium acetobutylicum: cloning, sequencing, and
RT   transcriptional regulation in response to potassium concentration.";
RL   J. Bacteriol. 179:4501-4512(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(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 membrane {ECO:0000255|HAMAP-Rule:MF_00276};
CC       Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00276}.
CC   -!- INDUCTION: By low potassium concentration.
CC   -!- SIMILARITY: Belongs to the KdpC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00276}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK81601.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U44892; AAC45479.1; -; Genomic_DNA.
DR   EMBL; U39673; AAB39093.1; -; Genomic_DNA.
DR   EMBL; AE001437; AAK81601.1; ALT_INIT; Genomic_DNA.
DR   PIR; F97351; F97351.
DR   PIR; T46844; T46844.
DR   RefSeq; NP_350261.1; NC_003030.1.
DR   RefSeq; WP_043943629.1; NC_003030.1.
DR   AlphaFoldDB; P94606; -.
DR   SMR; P94606; -.
DR   STRING; 272562.CA_C3680; -.
DR   EnsemblBacteria; AAK81601; AAK81601; CA_C3680.
DR   GeneID; 45000178; -.
DR   KEGG; cac:CA_C3680; -.
DR   PATRIC; fig|272562.8.peg.3869; -.
DR   eggNOG; COG2156; Bacteria.
DR   HOGENOM; CLU_077094_1_0_9; -.
DR   OMA; KYFWPRP; -.
DR   OrthoDB; 1912405at2; -.
DR   Proteomes; UP000000814; 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   2: Evidence at transcript level;
KW   ATP-binding; Cell membrane; Ion transport; Membrane; Nucleotide-binding;
KW   Potassium; Potassium transport; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..204
FT                   /note="Potassium-transporting ATPase KdpC subunit"
FT                   /id="PRO_0000196988"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00276"
FT   REGION          81..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..99
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   204 AA;  22202 MW;  ABC30A241BD42ADB CRC64;
     MKYFKSALRL GIVLIIICGL IYPLFITAVG QTVFHNKANG SIVTFKGKEV GSALLGQNFT
     DKRFFRGRVS SVNYNTYTKN DSNKDEVASG SQNLAPSNKD LKNRVKKDID DFLKTHPGVK
     KDEIPTDLLT SSGSGLDPDI SPKAAEIQVP SVSKATGISQ SKLKQIIKKC TEGRTLGVLG
     EERVNVLKVN LEVASMLKNS KIGE