ID A0A2M9IPQ2_9ACTN Unreviewed; 210 AA.
AC A0A2M9IPQ2;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-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=CG719_04750 {ECO:0000313|EMBL:PJM96516.1};
OS Streptomyces sp. CB01373.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2020325 {ECO:0000313|EMBL:PJM96516.1, ECO:0000313|Proteomes:UP000232070};
RN [1] {ECO:0000313|Proteomes:UP000232070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01373 {ECO:0000313|Proteomes:UP000232070};
RA Pan G., Xu Z., Guo Z., Ma M., Yang D., Zhou H., Gansemans Y., Zhu X.,
RA Zhao L.-X., Jiang Y., Cheng J., van Nieuwerburgh F., Suh J.W., Duan Y.,
RA Shen B.;
RT "Discovery of the Leinamycin Family of Natural Products by Mining
RT Actinobacterial Genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:0-0(2017).
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:PJM96516.1}.
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DR EMBL; NNBK01000003; PJM96516.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M9IPQ2; -.
DR OrthoDB; 9788285at2; -.
DR Proteomes; UP000232070; 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:UP000232070};
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..33
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00276"
SQ SEQUENCE 210 AA; 22274 MW; 22530AB0F88D29EE CRC64;
MNQSLVNTGR QLAAGLRALL ALTLLTGVVY PLVVTGVAQA FLGHRANGSE AEEGGRVVGS
SLIGQQHYGL DYFQPRPAAG LSANTVNTQY KLLVSGATNL AANNPKLVQA VERARAEVVR
VNSTSGYKVK PSQVPADAVT SSGSGLDPDI SPAYALLQAH RVAERNHLPV ARVEHLVREQ
TESRTLGFIG EPRVNVLQLN VALRELTTGH
//
