KDPC_ACIC5
ID KDPC_ACIC5 Reviewed; 184 AA.
AC C1F0T4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 69.
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=ACP_0431;
OS Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / BCRC 80197 / JCM
OS 7670 / NBRC 15755 / NCIMB 13165 / 161).
OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae;
OC Acidobacterium.
OX NCBI_TaxID=240015;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51196 / DSM 11244 / BCRC 80197 / JCM 7670 / NBRC 15755 / NCIMB
RC 13165 / 161;
RX PubMed=19201974; DOI=10.1128/aem.02294-08;
RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT "Three genomes from the phylum Acidobacteria provide insight into the
RT lifestyles of these microorganisms in soils.";
RL Appl. Environ. Microbiol. 75:2046-2056(2009).
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; CP001472; ACO31418.1; -; Genomic_DNA.
DR RefSeq; WP_012680825.1; NC_012483.1.
DR AlphaFoldDB; C1F0T4; -.
DR SMR; C1F0T4; -.
DR STRING; 240015.ACP_0431; -.
DR EnsemblBacteria; ACO31418; ACO31418; ACP_0431.
DR KEGG; aca:ACP_0431; -.
DR eggNOG; COG2156; Bacteria.
DR HOGENOM; CLU_077094_2_0_0; -.
DR OMA; KYFWPRP; -.
DR OrthoDB; 1912405at2; -.
DR Proteomes; UP000002207; 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; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..184
FT /note="Potassium-transporting ATPase KdpC subunit"
FT /id="PRO_1000190746"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00276"
SQ SEQUENCE 184 AA; 19512 MW; 7D8924290CBBCD2F CRC64;
MNHLRTAVLY TIISAVFLGL GYPLIMTGLA QWIFPRQANG SLIVRNGQVI GSKLIGQTFS
GAGYFHSRPS AAGNGYDAES SGGSNLAPTN HALIQQVEQR AAAEQVGATK VPVDLVTASA
SGLDPDITPA AAYYQAPRIA KARHLPLAAV RKLIAEQTTA RQFGLLGEPR VNVLAINLKL
DQMH