KDPC_RHOPT
ID KDPC_RHOPT Reviewed; 201 AA.
AC B3Q8S9;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=Rpal_3411;
OS Rhodopseudomonas palustris (strain TIE-1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=395960;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TIE-1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Emerson D.,
RA Newman D.K., Roden E., Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris TIE-1.";
RL Submitted (MAY-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; CP001096; ACF01913.1; -; Genomic_DNA.
DR RefSeq; WP_012496480.1; NC_011004.1.
DR AlphaFoldDB; B3Q8S9; -.
DR SMR; B3Q8S9; -.
DR EnsemblBacteria; ACF01913; ACF01913; Rpal_3411.
DR KEGG; rpt:Rpal_3411; -.
DR HOGENOM; CLU_077094_2_0_5; -.
DR OMA; KYFWPRP; -.
DR OrthoDB; 1912405at2; -.
DR BioCyc; RPAL395960:RPAL_RS16855-MON; -.
DR Proteomes; UP000001725; 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..201
FT /note="Potassium-transporting ATPase KdpC subunit"
FT /id="PRO_1000114736"
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00276"
FT REGION 69..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 201 AA; 20652 MW; 6785B6A0A7A65189 CRC64;
MLKEVRPAVV SLLALTMITG LAYPLAVTGL ATVLFPYQAQ GSLVERGGKV VGSALIGQEF
KGDEYFHGRP SATVAPDPAD SSKTVSAPYN AANSGGSNLG PTSKALADRL SEDVAKLKAE
NPAAPIPVDL VTTSGSGLDP DISPEGALFQ VPRVAKARGV TEEQIRKLVG ASIEQPLGGV
LGESRVNVLK LNLALDAAAP R