ID KDPC_ECOLI Reviewed; 190 AA. AC P03961; DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-1986, sequence version 1. DT 05-JUN-2019, entry version 149. 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}; GN OrderedLocusNames=b0696, JW0684; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6146979; DOI=10.1073/pnas.81.15.4746; RA Hesse J.E., Wieczorek L., Altendorf K., Reicin A.S., Dorus E., RA Epstein W.; RT "Sequence homology between two membrane transport ATPases, the Kdp- RT ATPase of Escherichia coli and the Ca2+-ATPase of sarcoplasmic RT reticulum."; RL Proc. Natl. Acad. Sci. U.S.A. 81:4746-4750(1984). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=8905232; DOI=10.1093/dnares/3.3.137; RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., RA Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., RA Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., RA Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., RA Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., RA Yano M., Horiuchi T.; RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome RT corresponding to the 12.7-28.0 min region on the linkage map."; RL DNA Res. 3:137-155(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 143-190. RX PubMed=1532388; DOI=10.1128/jb.174.7.2152-2159.1992; RA Walderhaug M.O., Polarek J.W., Voelkner P., Daniel J.M., Hesse J.E., RA Altendorf K., Epstein W.; RT "KdpD and KdpE, proteins that control expression of the kdpABC operon, RT are members of the two-component sensor-effector class of RT regulators."; RL J. Bacteriol. 174:2152-2159(1992). RN [6] RP FUNCTION IN POTASSIUM TRANSPORT, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=2849541; DOI=10.1111/j.1432-1033.1988.tb14438.x; RA Siebers A., Altendorf K.; RT "The K+-translocating Kdp-ATPase from Escherichia coli. Purification, RT enzymatic properties and production of complex- and subunit-specific RT antisera."; RL Eur. J. Biochem. 178:131-140(1988). RN [7] RP INDUCTION. RC STRAIN=K12; RX PubMed=1532387; DOI=10.1128/jb.174.7.2145-2151.1992; RA Polarek J.W., Williams G., Epstein W.; RT "The products of the kdpDE operon are required for expression of the RT Kdp ATPase of Escherichia coli."; RL J. Bacteriol. 174:2145-2151(1992). RN [8] RP FUNCTION IN POTASSIUM TRANSPORT. RC STRAIN=K12; RX PubMed=8499455; DOI=10.1016/0005-2728(93)90216-3; RA Kollmann R., Altendorf K.; RT "ATP-driven potassium transport in right-side-out membrane vesicles RT via the Kdp system of Escherichia coli."; RL Biochim. Biophys. Acta 1143:62-66(1993). RN [9] RP SUBUNIT. RC STRAIN=K12; RX PubMed=9858692; DOI=10.1016/S0005-2736(98)00179-5; RA Gassel M., Siebers A., Epstein W., Altendorf K.; RT "Assembly of the Kdp complex, the multi-subunit K+-transport ATPase of RT Escherichia coli."; RL Biochim. Biophys. Acta 1415:77-84(1998). RN [10] RP SUBUNIT. RC STRAIN=K12; RX PubMed=10608856; DOI=10.1074/jbc.274.53.37901; RA Gassel M., Mollenkamp T., Puppe W., Altendorf K.; RT "The KdpF subunit is part of the K(+)-translocating Kdp complex of RT Escherichia coli and is responsible for stabilization of the complex RT in vitro."; RL J. Biol. Chem. 274:37901-37907(1999). RN [11] RP SUBUNIT. RX PubMed=18298081; DOI=10.1021/bi702038e; RA Heitkamp T., Kalinowski R., Boettcher B., Boersch M., Altendorf K., RA Greie J.C.; RT "K+-translocating KdpFABC P-type ATPase from Escherichia coli acts as RT a functional and structural dimer."; RL Biochemistry 47:3564-3575(2008). RN [12] RP FUNCTION, ATP-BINDING, AND MUTAGENESIS OF 140-GLN--LEU-150. RX PubMed=21711450; DOI=10.1111/j.1742-4658.2011.08224.x; RA Irzik K., Pfroetzschner J., Goss T., Ahnert F., Haupt M., Greie J.C.; RT "The KdpC subunit of the Escherichia coli K+-transporting KdpB P-type RT ATPase acts as a catalytic chaperone."; RL FEBS J. 278:3041-3053(2011). RN [13] RP FUNCTION. RX PubMed=23930894; DOI=10.1021/bi400729e; RA Damnjanovic B., Weber A., Potschies M., Greie J.C., Apell H.J.; RT "Mechanistic analysis of the pump cycle of the KdpFABC P-type RT ATPase."; RL Biochemistry 52:5563-5576(2013). CC -!- FUNCTION: Part of the high-affinity ATP-driven potassium transport CC (or Kdp) system, which catalyzes the hydrolysis of ATP coupled CC with the electrogenic transport of potassium into the cytoplasm CC (PubMed:2849541, PubMed:8499455, PubMed:23930894). This subunit CC acts as a catalytic chaperone that increases the ATP-binding CC affinity of the ATP-hydrolyzing subunit KdpB by the formation of a CC transient KdpB/KdpC/ATP ternary complex (PubMed:21711450). CC {ECO:0000269|PubMed:21711450, ECO:0000269|PubMed:23930894, CC ECO:0000269|PubMed:2849541, ECO:0000269|PubMed:8499455}. CC -!- SUBUNIT: The system is composed of three essential subunits: KdpA, CC KdpB and KdpC (PubMed:2849541, PubMed:9858692). The complex also CC contains KdpF, a small non-essential subunit (PubMed:10608856). CC The KdpFABC complex exists as a dimer above concentrations of 30- CC 50 nM, whereas the complex exists as a functional monomer at lower CC concentrations (PubMed:18298081). {ECO:0000269|PubMed:10608856, CC ECO:0000269|PubMed:18298081, ECO:0000269|PubMed:2849541, CC ECO:0000269|PubMed:9858692}. CC -!- INTERACTION: CC P03960:kdpB; NbExp=2; IntAct=EBI-6997216, EBI-1116956; CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00276, ECO:0000269|PubMed:2849541}; Single-pass membrane CC protein {ECO:0000255|HAMAP-Rule:MF_00276}. CC -!- INDUCTION: Transcriptionally regulated by the KdpD/KdpE two- CC component regulatory system. {ECO:0000269|PubMed:1532387}. 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; K02670; AAB96337.1; -; Genomic_DNA. DR EMBL; U00096; AAC73790.1; -; Genomic_DNA. DR EMBL; AP009048; BAA35353.1; -; Genomic_DNA. DR PIR; A01073; PWECCK. DR RefSeq; NP_415224.1; NC_000913.3. DR RefSeq; WP_001300431.1; NZ_LN832404.1. DR PDB; 5MRW; X-ray; 2.90 A; C/G/K=4-190. DR PDB; 6HRA; EM; 3.70 A; C=1-190. DR PDB; 6HRB; EM; 4.00 A; C=1-190. DR PDBsum; 5MRW; -. DR PDBsum; 6HRA; -. DR PDBsum; 6HRB; -. DR SMR; P03961; -. DR BioGrid; 4259349; 20. DR ComplexPortal; CPX-3564; KdpFABC potassium import complex. DR IntAct; P03961; 2. DR MINT; P03961; -. DR STRING; 511145.b0696; -. DR TCDB; 3.A.3.7.1; the p-type atpase (p-atpase) superfamily. DR PaxDb; P03961; -. DR PRIDE; P03961; -. DR EnsemblBacteria; AAC73790; AAC73790; b0696. DR EnsemblBacteria; BAA35353; BAA35353; BAA35353. DR GeneID; 947508; -. DR KEGG; ecj:JW0684; -. DR KEGG; eco:b0696; -. DR PATRIC; fig|1411691.4.peg.1579; -. DR EchoBASE; EB0510; -. DR EcoGene; EG10515; kdpC. DR eggNOG; ENOG4108R80; Bacteria. DR eggNOG; COG2156; LUCA. DR HOGENOM; HOG000244124; -. DR InParanoid; P03961; -. DR KO; K01548; -. DR PhylomeDB; P03961; -. DR BioCyc; EcoCyc:EG10515-MONOMER; -. DR BioCyc; ECOL316407:JW0684-MONOMER; -. DR BioCyc; MetaCyc:EG10515-MONOMER; -. DR PRO; PR:P03961; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule. DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc. DR GO; GO:0031004; C:potassium ion-transporting ATPase complex; IDA:EcoCyc. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0008556; F:potassium-transporting ATPase activity; IDA:EcoCyc. DR GO; GO:0099132; P:ATP hydrolysis coupled cation transmembrane transport; IDA:EcoCyc. DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:EcoCyc. 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 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; KW Complete proteome; Ion transport; Membrane; Nucleotide-binding; KW Potassium; Potassium transport; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 190 Potassium-transporting ATPase KdpC FT subunit. FT /FTId=PRO_0000196990. FT TOPO_DOM 1 9 Periplasmic. FT {ECO:0000305|PubMed:21711450}. FT TRANSMEM 10 30 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00276}. FT TOPO_DOM 31 190 Cytoplasmic. FT {ECO:0000305|PubMed:21711450}. FT MUTAGEN 140 150 QIPRVAKARNL->AIPAASKSANA: Cell does not FT grow at low potassium concentrations. FT {ECO:0000269|PubMed:21711450}. FT HELIX 5 19 {ECO:0000244|PDB:5MRW}. FT HELIX 21 33 {ECO:0000244|PDB:5MRW}. FT HELIX 35 38 {ECO:0000244|PDB:5MRW}. FT STRAND 42 45 {ECO:0000244|PDB:5MRW}. FT STRAND 48 52 {ECO:0000244|PDB:5MRW}. FT TURN 53 55 {ECO:0000244|PDB:5MRW}. FT STRAND 62 64 {ECO:0000244|PDB:5MRW}. FT STRAND 73 75 {ECO:0000244|PDB:5MRW}. FT TURN 79 81 {ECO:0000244|PDB:5MRW}. FT HELIX 92 108 {ECO:0000244|PDB:5MRW}. FT STRAND 114 116 {ECO:0000244|PDB:5MRW}. FT HELIX 118 121 {ECO:0000244|PDB:5MRW}. FT STRAND 125 127 {ECO:0000244|PDB:5MRW}. FT HELIX 134 139 {ECO:0000244|PDB:5MRW}. FT HELIX 141 148 {ECO:0000244|PDB:5MRW}. FT HELIX 152 161 {ECO:0000244|PDB:5MRW}. FT TURN 169 171 {ECO:0000244|PDB:5MRW}. FT STRAND 175 177 {ECO:0000244|PDB:5MRW}. FT HELIX 178 189 {ECO:0000244|PDB:5MRW}. SQ SEQUENCE 190 AA; 20267 MW; 17F58EC839B6B95A CRC64; MSGLRPALST FIFLLLITGG VYPLLTTVLG QWWFPWQANG SLIREGDTVR GSALIGQNFT GNGYFHGRPS ATAEMPYNPQ ASGGSNLAVS NPELDKLIAA RVAALRAANP DASASVPVEL VTASASGLDN NITPQAAAWQ IPRVAKARNL SVEQLTQLIA KYSQQPLVKY IGQPVVNIVE LNLALDKLDE //