KDPC_PSEPW
ID KDPC_PSEPW Reviewed; 183 AA.
AC B1JAS8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 81.
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=PputW619_3484;
OS Pseudomonas putida (strain W619).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=390235;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W619;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Taghavi S., Vangronsveld D., van der Lelie D.,
RA Richardson P.;
RT "Complete sequence of Pseudomonas putida W619.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000949; ACA73967.1; -; Genomic_DNA.
DR RefSeq; WP_012315321.1; NC_010501.1.
DR AlphaFoldDB; B1JAS8; -.
DR SMR; B1JAS8; -.
DR STRING; 390235.PputW619_3484; -.
DR EnsemblBacteria; ACA73967; ACA73967; PputW619_3484.
DR KEGG; ppw:PputW619_3484; -.
DR eggNOG; COG2156; Bacteria.
DR HOGENOM; CLU_077094_2_0_6; -.
DR OMA; PDLKWFQ; -.
DR OrthoDB; 1912405at2; -.
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..183
FT /note="Potassium-transporting ATPase KdpC subunit"
FT /id="PRO_1000114734"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00276"
SQ SEQUENCE 183 AA; 18904 MW; 27E9EB3691015FE9 CRC64;
MNTYVRPALS LILLLAVVTG ALYPLAVTGV AQVVFPEQAN GSLVRDEQGQ VRGSALIAQD
FQGDGWFHSR PSAGAYATVA SSASNLSPSN PALAERVAGD AAKLYQAGQG PVPQALLTTS
GSGLDPHLPP QAVAYQIPRV AAARQIPVER LQALLEGATL HPLIGPPVVN VLALNQALSK
FGL
