ID A0A2H9VQJ1_9SPHI Unreviewed; 185 AA.
AC A0A2H9VQJ1;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=CLV57_0051 {ECO:0000313|EMBL:PJJ83074.1};
OS Mucilaginibacter auburnensis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1457233 {ECO:0000313|EMBL:PJJ83074.1, ECO:0000313|Proteomes:UP000242687};
RN [1] {ECO:0000313|EMBL:PJJ83074.1, ECO:0000313|Proteomes:UP000242687}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28175 {ECO:0000313|EMBL:PJJ83074.1,
RC ECO:0000313|Proteomes:UP000242687};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): From Individual Species to Whole Genera.";
RL Submitted (NOV-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PJJ83074.1}.
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DR EMBL; PGFJ01000001; PJJ83074.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H9VQJ1; -.
DR OrthoDB; 9809491at2; -.
DR Proteomes; UP000242687; Unassembled WGS sequence.
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:UP000242687};
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}.
SQ SEQUENCE 185 AA; 19899 MW; 05A00DFC8EE2B22E CRC64;
MKKYILPAIR LTVVLTVLLC VIYPLLISAV GKLAKGKGDG ETIILNGKVV GYANVGQKFD
KPGYFWGRPS AVDYNAAGSA GSNKGPTNPD YLKQVSDRAD TLLKYHPYLK RTDIPADMVT
ASGSGLDPDI SVAGATIQIK RIAADRKLDE QTIAKLVAEH TEKPVFGPAH VNVLKLNVAL
DELKK
//
