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Database: UniProt
Entry: A0A1G9F5V5_9ACTN
LinkDB: A0A1G9F5V5_9ACTN
Original site: A0A1G9F5V5_9ACTN 
ID   A0A1G9F5V5_9ACTN        Unreviewed;       314 AA.
AC   A0A1G9F5V5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
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=SAMN05216298_1592 {ECO:0000313|EMBL:SDK83735.1};
OS   Glycomyces sambucus.
OC   Bacteria; Actinomycetota; Actinomycetes; Glycomycetales; Glycomycetaceae;
OC   Glycomyces.
OX   NCBI_TaxID=380244 {ECO:0000313|EMBL:SDK83735.1, ECO:0000313|Proteomes:UP000198662};
RN   [1] {ECO:0000313|EMBL:SDK83735.1, ECO:0000313|Proteomes:UP000198662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.3147 {ECO:0000313|EMBL:SDK83735.1,
RC   ECO:0000313|Proteomes:UP000198662};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNGF01000002; SDK83735.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9F5V5; -.
DR   STRING; 380244.SAMN05216298_1592; -.
DR   OrthoDB; 9788285at2; -.
DR   Proteomes; UP000198662; 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   PANTHER; PTHR30042; POTASSIUM-TRANSPORTING ATPASE C CHAIN; 1.
DR   PANTHER; PTHR30042:SF2; POTASSIUM-TRANSPORTING ATPASE KDPC SUBUNIT; 1.
DR   Pfam; PF02669; KdpC; 2.
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};
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   314 AA;  32157 MW;  D6FA1878007D4694 CRC64;
     MARLPRWVSQ HLAALRALLV LTAVTGILYP LAVLAVAQLP GLDHKAEGSL VYDEDGAVVG
     SSLLGQSFTD EDGNAIAAYF QSRPSMAAGE NGDYDPLVSG ASNLGPESVV DALPDPALGW
     DGDELATKSL LTQVCERSYA IGEREGVDGS RPYCTESGAG AVGAVLGVFY AEGTTGDVVR
     VVSLNEACDA VAAPFLAEYE GVPVECAVYG EDYAAAIVTP VEGDASGEPA VPADAVTASG
     SGLDPHISPE YAELQTARVA AERGASTEDV EALVEEHTTG RFLGFMGDPA VNVVELNLAL
     DSVFPAGDEA GPVG
//
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