ID KDPC_STAHJ Reviewed; 185 AA. AC Q4LAI1; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 02-AUG-2005, sequence version 1. DT 27-MAR-2024, entry version 123. 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=SH0035; OS Staphylococcus haemolyticus (strain JCSC1435). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=279808; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCSC1435; RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005; RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., RA Hiramatsu K.; RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the RT extreme plasticity of its genome and the evolution of human-colonizing RT staphylococcal species."; RL J. Bacteriol. 187:7292-7308(2005). 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 membrane {ECO:0000255|HAMAP-Rule:MF_00276}; CC Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00276}. CC -!- SIMILARITY: Belongs to the KdpC family. {ECO:0000255|HAMAP- CC Rule:MF_00276}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP006716; BAE03344.1; -; Genomic_DNA. DR RefSeq; WP_011274390.1; NC_007168.1. DR AlphaFoldDB; Q4LAI1; -. DR SMR; Q4LAI1; -. DR KEGG; sha:SH0035; -. DR eggNOG; COG2156; Bacteria. DR HOGENOM; CLU_077094_2_0_9; -. DR OrthoDB; 9809491at2; -. DR Proteomes; UP000000543; Chromosome. 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; Cell membrane; Ion transport; Membrane; Nucleotide-binding; KW Potassium; Potassium transport; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1..185 FT /note="Potassium-transporting ATPase KdpC subunit" FT /id="PRO_0000197018" FT TRANSMEM 8..28 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00276" FT REGION 113..132 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 113..130 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 185 AA; 20136 MW; C5307020FE5083F0 CRC64; MQTIRKSLGL VLIMFVLCGF IFPLTVTALG QVLFPEQANG SLVKQDGKVI GSKLIGQQWT EPKYFHGRIS AVNYNMNANE VKESGGPASG GSNYGNSNPE LKKRVQETIK QEGQKLSSDA VTTSGSGLDP DITVDNAKQQ VKCIAKERNI DASKINHLID ENKQASPMAD DYVNVLKLNI TLDKL //