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KDPC_YERE8
ID   KDPC_YERE8              Reviewed;         200 AA.
AC   A1JQS4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=YE2962;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(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 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; AM286415; CAL13001.1; -; Genomic_DNA.
DR   RefSeq; WP_011816821.1; NC_008800.1.
DR   RefSeq; YP_001007151.1; NC_008800.1.
DR   AlphaFoldDB; A1JQS4; -.
DR   SMR; A1JQS4; -.
DR   STRING; 393305.YE2962; -.
DR   EnsemblBacteria; CAL13001; CAL13001; YE2962.
DR   KEGG; yen:YE2962; -.
DR   PATRIC; fig|393305.7.peg.3153; -.
DR   eggNOG; COG2156; Bacteria.
DR   HOGENOM; CLU_077094_2_0_6; -.
DR   OMA; KYFWPRP; -.
DR   Proteomes; UP000000642; 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; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..200
FT                   /note="Potassium-transporting ATPase KdpC subunit"
FT                   /id="PRO_1000022325"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00276"
SQ   SEQUENCE   200 AA;  21154 MW;  48EE5064D7ECCD61 CRC64;
     MSYLRPAVVL LILLTLITGI AYPLLTTGLA KLMFSQQANG SLVMLGDEVV GSSLIGQNFT
     QLGYFSGRPS ATAEMPYNSM ASGGSNLAIS NPELDKAITE RVKSLRQANP TQTGPVPVDL
     VTASASGLDP QISLAAAYYQ APRIASIRQM PLSEVKQLID SNVQKATPNF FGESVVNVLN
     LNMALDAQSH VKVPATSTKS
 
 
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