KDPC_ECOLI
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 03-AUG-2022, entry version 167.
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., Epstein W.;
RT "Sequence homology between two membrane transport ATPases, the Kdp-ATPase
RT of Escherichia coli and the Ca2+-ATPase of sarcoplasmic 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., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT 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., Mau B.,
RA 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 MG1655
RT 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, are
RT members of the two-component sensor-effector class of 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 Kdp
RT 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 via the
RT 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 in
RT 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 a
RT 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 ATPase.";
RL Biochemistry 52:5563-5576(2013).
RN [14] {ECO:0007744|PDB:5MRW}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 4-190 IN COMPLEX WITH KDPA; KDPB
RP AND KDPF, SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=28636601; DOI=10.1038/nature22970;
RA Huang C.S., Pedersen B.P., Stokes D.L.;
RT "Crystal structure of the potassium-importing KdpFABC membrane complex.";
RL Nature 546:681-685(2017).
RN [15] {ECO:0007744|PDB:6HRA, ECO:0007744|PDB:6HRB}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.70 ANGSTROMS) OF KDPFABC COMPLEX IN E1
RP AND E2 STATE, SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=30478378; DOI=10.1038/s41467-018-07319-2;
RA Stock C., Hielkema L., Tascon I., Wunnicke D., Oostergetel G.T.,
RA Azkargorta M., Paulino C., Haenelt I.;
RT "Cryo-EM structures of KdpFABC suggest a K+ transport mechanism via two
RT inter-subunit half-channels.";
RL Nat. Commun. 9:4971-4971(2018).
RN [16] {ECO:0007744|PDB:7BGY, ECO:0007744|PDB:7BH1, ECO:0007744|PDB:7BH2, ECO:0007744|PDB:7LC3, ECO:0007744|PDB:7LC6}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.90 ANGSTROMS) OF KDPFABC COMPLEX IN
RP MAJOR ENZYMATIC STATES.
RX PubMed=34272288; DOI=10.1073/pnas.2105195118;
RA Sweet M.E., Larsen C., Zhang X., Schlame M., Pedersen B.P., Stokes D.L.;
RT "Structural basis for potassium transport in prokaryotes by KdpFABC.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
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 (PubMed:2849541,
CC PubMed:8499455, PubMed:23930894). This subunit acts as a catalytic
CC chaperone that increases the ATP-binding affinity of the ATP-
CC hydrolyzing subunit KdpB by the formation of a transient KdpB/KdpC/ATP
CC ternary complex (PubMed:21711450). {ECO:0000269|PubMed:21711450,
CC ECO:0000269|PubMed:23930894, ECO:0000269|PubMed:2849541,
CC ECO:0000269|PubMed:8499455}.
CC -!- SUBUNIT: The system is composed of three essential subunits: KdpA, KdpB
CC and KdpC (PubMed:2849541, PubMed:9858692, PubMed:28636601,
CC PubMed:30478378). The complex also contains KdpF, a small non-essential
CC subunit (PubMed:10608856, PubMed:28636601, PubMed:30478378). The
CC KdpFABC complex exists as a dimer above concentrations of 30-50 nM,
CC 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:28636601, ECO:0000269|PubMed:30478378,
CC ECO:0000269|PubMed:9858692}.
CC -!- INTERACTION:
CC P03961; 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, ECO:0000269|PubMed:28636601,
CC ECO:0000269|PubMed:30478378}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00276, ECO:0000269|PubMed:28636601,
CC ECO:0000269|PubMed:30478378}.
CC -!- INDUCTION: Transcriptionally regulated by the KdpD/KdpE two-component
CC regulatory system. {ECO:0000269|PubMed:1532387}.
CC -!- SIMILARITY: Belongs to the KdpC family. {ECO:0000255|HAMAP-
CC Rule:MF_00276}.
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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_SSZK01000045.1.
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 PDB; 7BGY; EM; 2.90 A; C=1-190.
DR PDB; 7BH1; EM; 3.38 A; C=1-190.
DR PDB; 7BH2; EM; 3.00 A; C=1-190.
DR PDB; 7LC3; EM; 3.23 A; C=1-190.
DR PDB; 7LC6; EM; 3.70 A; C=1-190.
DR PDBsum; 5MRW; -.
DR PDBsum; 6HRA; -.
DR PDBsum; 6HRB; -.
DR PDBsum; 7BGY; -.
DR PDBsum; 7BH1; -.
DR PDBsum; 7BH2; -.
DR PDBsum; 7LC3; -.
DR PDBsum; 7LC6; -.
DR AlphaFoldDB; P03961; -.
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 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 eggNOG; COG2156; Bacteria.
DR HOGENOM; CLU_077094_2_0_6; -.
DR InParanoid; P03961; -.
DR OMA; KYFWPRP; -.
DR PhylomeDB; P03961; -.
DR BioCyc; EcoCyc:EG10515-MON; -.
DR BioCyc; MetaCyc:EG10515-MON; -.
DR BRENDA; 7.2.2.6; 2026.
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:ComplexPortal.
DR GO; GO:0031004; C:potassium ion-transporting ATPase complex; IDA:EcoCyc.
DR GO; GO:1903103; C:potassium:proton antiporter complex; IPI:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008556; F:P-type potassium transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0098655; P:cation transmembrane transport; IDA:EcoCyc.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:EcoCyc.
DR GO; GO:0006813; P:potassium ion transport; IDA:ComplexPortal.
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 Ion transport; Membrane; Nucleotide-binding; Potassium;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..190
FT /note="Potassium-transporting ATPase KdpC subunit"
FT /id="PRO_0000196990"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28636601,
FT ECO:0000269|PubMed:30478378"
FT TRANSMEM 6..34
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28636601,
FT ECO:0000269|PubMed:30478378, ECO:0007744|PDB:5MRW,
FT ECO:0007744|PDB:6HRA"
FT TOPO_DOM 35..190
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:28636601,
FT ECO:0000269|PubMed:30478378"
FT MUTAGEN 140..150
FT /note="QIPRVAKARNL->AIPAASKSANA: Cell does not grow at low
FT potassium concentrations."
FT /evidence="ECO:0000269|PubMed:21711450"
FT HELIX 5..19
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 21..33
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:5MRW"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:5MRW"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 92..108
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:7BH1"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 134..139
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 141..148
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 152..161
FT /evidence="ECO:0007829|PDB:5MRW"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 178..189
FT /evidence="ECO:0007829|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
