KDPF_ECOLI
ID KDPF_ECOLI Reviewed; 29 AA.
AC P36937; Q2EEQ9;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Potassium-transporting ATPase KdpF subunit {ECO:0000305};
DE AltName: Full=ATP phosphohydrolase [potassium-transporting] F chain {ECO:0000305};
DE AltName: Full=Potassium-binding and translocating subunit F {ECO:0000305};
DE AltName: Full=Potassium-translocating ATPase F chain {ECO:0000305};
GN Name=kdpF; OrderedLocusNames=b4513, JW0687;
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 IDENTIFICATION.
RX PubMed=1288322; DOI=10.1111/j.1749-6632.1992.tb43799.x;
RA Altendorf K., Siebers A., Epstein W.;
RT "The KDP ATPase of Escherichia coli.";
RL Ann. N. Y. Acad. Sci. 671:228-243(1992).
RN [6]
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 [7]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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 [8]
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 [9]
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 [10] {ECO:0007744|PDB:5MRW}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 1-27 IN COMPLEX WITH KDPA; KDPB
RP AND KDPC, 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 [11] {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 [12] {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
CC (PubMed:23930894). This subunit may be involved in stabilization of the
CC complex (PubMed:10608856). {ECO:0000269|PubMed:10608856,
CC ECO:0000269|PubMed:23930894}.
CC -!- SUBUNIT: The system is composed of three essential subunits: KdpA, KdpB
CC and KdpC (PubMed:10608856, PubMed:28636601, PubMed:30478378). The
CC complex also contains KdpF, a small non-essential subunit
CC (PubMed:10608856, PubMed:28636601, PubMed:30478378). The KdpFABC
CC complex exists as a dimer above concentrations of 30-50 nM, whereas the
CC complex exists as a functional monomer at lower concentrations
CC (PubMed:18298081). {ECO:0000269|PubMed:10608856,
CC ECO:0000269|PubMed:18298081, ECO:0000269|PubMed:28636601,
CC ECO:0000269|PubMed:30478378}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:28636601,
CC ECO:0000269|PubMed:30478378, ECO:0000305|PubMed:10608856}; Single-pass
CC membrane protein {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 -!- DISRUPTION PHENOTYPE: Inactivation of kdpF still leads to a functional
CC KdpABC complex in vivo. Deletion impairs ATPase activity of the complex
CC in vitro. {ECO:0000269|PubMed:10608856}.
CC -!- SIMILARITY: Belongs to the KdpF family. {ECO:0000305}.
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DR EMBL; K02670; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U00096; ABD18643.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35357.1; -; Genomic_DNA.
DR PIR; T48910; T48910.
DR RefSeq; WP_001272653.1; NZ_SSZK01000045.1.
DR RefSeq; YP_588443.1; NC_000913.3.
DR PDB; 5MRW; X-ray; 2.90 A; D/H/L=1-27.
DR PDB; 6HRA; EM; 3.70 A; D=1-29.
DR PDB; 6HRB; EM; 4.00 A; D=1-29.
DR PDB; 7BGY; EM; 2.90 A; D=1-29.
DR PDB; 7BH1; EM; 3.38 A; D=1-29.
DR PDB; 7BH2; EM; 3.00 A; D=1-29.
DR PDB; 7LC3; EM; 3.23 A; D=1-29.
DR PDB; 7LC6; EM; 3.70 A; D=1-29.
DR PDB; 7NNL; EM; 3.10 A; D=1-27.
DR PDB; 7NNP; EM; 3.20 A; D=1-27.
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 PDBsum; 7NNL; -.
DR PDBsum; 7NNP; -.
DR AlphaFoldDB; P36937; -.
DR SMR; P36937; -.
DR BioGRID; 4259926; 3.
DR ComplexPortal; CPX-3564; KdpFABC potassium import complex.
DR IntAct; P36937; 1.
DR STRING; 511145.b4513; -.
DR TCDB; 3.A.3.7.1; the p-type atpase (p-atpase) superfamily.
DR PaxDb; P36937; -.
DR EnsemblBacteria; ABD18643; ABD18643; b4513.
DR EnsemblBacteria; BAA35357; BAA35357; BAA35357.
DR GeneID; 67413745; -.
DR GeneID; 948946; -.
DR KEGG; ecj:JW0687; -.
DR KEGG; eco:b4513; -.
DR PATRIC; fig|511145.12.peg.729; -.
DR EchoBASE; EB2047; -.
DR HOGENOM; CLU_202373_1_1_6; -.
DR BioCyc; EcoCyc:MON0-12; -.
DR BioCyc; MetaCyc:MON0-12; -.
DR BRENDA; 7.2.2.6; 2026.
DR PRO; PR:P36937; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
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: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 GO; GO:0043462; P:regulation of ATP-dependent activity; IEA:InterPro.
DR InterPro; IPR011726; KdpF.
DR Pfam; PF09604; Potass_KdpF; 1.
DR TIGRFAMs; TIGR02115; potass_kdpF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Ion transport; Membrane;
KW Potassium; Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..29
FT /note="Potassium-transporting ATPase KdpF subunit"
FT /id="PRO_0000084299"
FT TOPO_DOM 1..2
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:28636601,
FT ECO:0000269|PubMed:30478378"
FT TRANSMEM 3..24
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 25..29
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28636601,
FT ECO:0000269|PubMed:30478378"
FT HELIX 3..24
FT /evidence="ECO:0007829|PDB:5MRW"
FT TURN 25..28
FT /evidence="ECO:0007829|PDB:7BGY"
SQ SEQUENCE 29 AA; 3072 MW; A925E36F96B17820 CRC64;
MSAGVITGVL LVFLLLGYLV YALINAEAF
