ID A0A345WPA1_9SPHN Unreviewed; 199 AA.
AC A0A345WPA1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Potassium-transporting ATPase KdpC subunit {ECO:0000256|HAMAP-Rule:MF_00276};
DE AltName: Full=ATP phosphohydrolase [potassium-transporting] C chain {ECO:0000256|HAMAP-Rule:MF_00276};
DE AltName: Full=Potassium-binding and translocating subunit C {ECO:0000256|HAMAP-Rule:MF_00276};
DE AltName: Full=Potassium-translocating ATPase C chain {ECO:0000256|HAMAP-Rule:MF_00276};
GN Name=kdpC {ECO:0000256|HAMAP-Rule:MF_00276};
GN ORFNames=DM480_08205 {ECO:0000313|EMBL:AXJ95503.1};
OS Sphingomonas sp. FARSPH.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=2219696 {ECO:0000313|EMBL:AXJ95503.1, ECO:0000313|Proteomes:UP000254856};
RN [1] {ECO:0000313|EMBL:AXJ95503.1, ECO:0000313|Proteomes:UP000254856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FARSPH {ECO:0000313|EMBL:AXJ95503.1,
RC ECO:0000313|Proteomes:UP000254856};
RA Bendezu Eguis J., Morales Ruiz S., Montesinos R., Quispe Conislla J.,
RA Tataje-Lavanda L., Fernandez-Sanchez M., Fernandez-Diaz M.;
RT "Cell Culture Contaminant.";
RL Submitted (JUN-2018) 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:0000256|HAMAP-Rule:MF_00276}.
CC -!- SUBUNIT: The system is composed of three essential subunits: KdpA, KdpB
CC and KdpC. {ECO:0000256|HAMAP-Rule:MF_00276}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00276};
CC Single-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00276}.
CC -!- SIMILARITY: Belongs to the KdpC family. {ECO:0000256|HAMAP-
CC Rule:MF_00276}.
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DR EMBL; CP029985; AXJ95503.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345WPA1; -.
DR KEGG; sphf:DM480_08205; -.
DR OrthoDB; 9788285at2; -.
DR Proteomes; UP000254856; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 NCBIfam; TIGR00681; kdpC; 1.
DR PANTHER; PTHR30042; POTASSIUM-TRANSPORTING ATPASE C CHAIN; 1.
DR PANTHER; PTHR30042:SF2; POTASSIUM-TRANSPORTING ATPASE KDPC SUBUNIT; 1.
DR Pfam; PF02669; KdpC; 1.
DR PIRSF; PIRSF001296; K_ATPase_KdpC; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00276};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00276};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW Rule:MF_00276};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00276};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00276};
KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_00276};
KW Potassium transport {ECO:0000256|ARBA:ARBA00022538, ECO:0000256|HAMAP-
KW Rule:MF_00276}; Reference proteome {ECO:0000313|Proteomes:UP000254856};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00276};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_00276};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00276}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00276"
SQ SEQUENCE 199 AA; 20486 MW; 2C0ADC3253124B15 CRC64;
MGKDFSSALR PAIVMTILFA ALLGLAYPLA MTGIGQAVFP GQANGSLVRD TGGKVIGSTV
VGQAFVADRY FQTRPSAAGK GYDGLNSSGS NFGPTSKALV DRVKADIAKR RSEGVAGALP
ADLVTASGSG LDPDLSPDAA WAQAPRVARV RGVSIDRIRA LVSQNVETSL FGDPHVNVLA
LNRALDALQP VPAFATPAR
//
