ATPE_ECOLI
ID ATPE_ECOLI Reviewed; 139 AA.
AC P0A6E6; P00832; Q2M849;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=ATP synthase epsilon chain;
DE AltName: Full=ATP synthase F1 sector epsilon subunit;
DE AltName: Full=F-ATPase epsilon subunit;
GN Name=atpC; Synonyms=papG, uncC; OrderedLocusNames=b3731, JW3709;
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=6395859; DOI=10.1042/bj2240799;
RA Walker J.E., Gay N.J., Saraste M., Eberle A.N.;
RT "DNA sequence around the Escherichia coli unc operon. Completion of the
RT sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS and
RT phoS.";
RL Biochem. J. 224:799-815(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6285901; DOI=10.1016/0006-291x(82)90922-6;
RA Kanazawa H., Kayano T., Kiyasu T., Futai M.;
RT "Nucleotide sequence of the genes for beta and epsilon subunits of proton-
RT translocating ATPase from Escherichia coli.";
RL Biochem. Biophys. Res. Commun. 105:1257-1264(1982).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6301339; DOI=10.1111/j.1749-6632.1982.tb25731.x;
RA Kanazawa H., Futai M.;
RT "Structure and function of H+-ATPase: what we have learned from Escherichia
RT coli H+-ATPase.";
RL Ann. N. Y. Acad. Sci. 402:45-64(1982).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6272217; DOI=10.1093/nar/9.20.5287;
RA Saraste M., Gay N.J., Eberle A., Runswick M.J., Walker J.E.;
RT "The atp operon: nucleotide sequence of the genes for the gamma, beta, and
RT epsilon subunits of Escherichia coli ATP synthase.";
RL Nucleic Acids Res. 9:5287-5296(1981).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [6]
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 [7]
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 [8]
RP PROTEIN SEQUENCE OF 2-21.
RC STRAIN=K12;
RX PubMed=9868784; DOI=10.1111/j.1574-6968.1998.tb13343.x;
RA Wasinger V.C., Humphery-Smith I.;
RT "Small genes/gene-products in Escherichia coli K-12.";
RL FEMS Microbiol. Lett. 169:375-382(1998).
RN [9]
RP PROTEIN SEQUENCE OF 2-9.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.;
RL Submitted (FEB-1996) to UniProtKB.
RN [10]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=BL21-DE3;
RX PubMed=16079137; DOI=10.1074/jbc.m506479200;
RA Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA von Heijne G., Daley D.O.;
RT "Protein complexes of the Escherichia coli cell envelope.";
RL J. Biol. Chem. 280:34409-34419(2005).
RN [11]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=21778229; DOI=10.1074/jbc.m111.245696;
RA Fontaine F., Fuchs R.T., Storz G.;
RT "Membrane localization of small proteins in Escherichia coli.";
RL J. Biol. Chem. 286:32464-32474(2011).
RN [12]
RP STRUCTURE BY NMR.
RX PubMed=7583669; DOI=10.1038/nsb1195-961;
RA Wilkens S., Dahlquist F.W., McIntosh L.P., Donaldson L.W., Capaldi R.A.;
RT "Structural features of the epsilon subunit of the Escherichia coli ATP
RT synthase determined by NMR spectroscopy.";
RL Nat. Struct. Biol. 2:961-967(1995).
RN [13]
RP STRUCTURE BY NMR.
RX PubMed=9756905; DOI=10.1074/jbc.273.41.26645;
RA Wilkens S., Capaldi R.A.;
RT "Solution structure of the epsilon subunit of the F1-ATPase from
RT Escherichia coli and interactions of this subunit with beta subunits in the
RT complex.";
RL J. Biol. Chem. 273:26645-26651(1998).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=9331422; DOI=10.1016/s0969-2126(97)00272-4;
RA Uhlin U., Cox G.B., Guss J.M.;
RT "Crystal structure of the epsilon subunit of the proton-translocating ATP
RT synthase from Escherichia coli.";
RL Structure 5:1219-1230(1997).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC subunits: a, b and c. {ECO:0000269|PubMed:16079137}.
CC -!- INTERACTION:
CC P0A6E6; P0ABB0: atpA; NbExp=3; IntAct=EBI-544362, EBI-368707;
CC P0A6E6; P0ABA6: atpG; NbExp=5; IntAct=EBI-544362, EBI-544306;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:16079137,
CC ECO:0000269|PubMed:21778229}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:21778229}.
CC -!- SIMILARITY: Belongs to the ATPase epsilon chain family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA23528.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; J01594; AAA24738.1; -; Genomic_DNA.
DR EMBL; X01631; CAA25783.1; -; Genomic_DNA.
DR EMBL; V00311; CAA23595.1; -; Genomic_DNA.
DR EMBL; M25464; AAA83876.1; -; Genomic_DNA.
DR EMBL; V00267; CAA23528.1; ALT_FRAME; Genomic_DNA.
DR EMBL; L10328; AAA62083.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76754.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77557.1; -; Genomic_DNA.
DR PIR; B90106; PWECE.
DR RefSeq; NP_418187.1; NC_000913.3.
DR RefSeq; WP_001251965.1; NZ_STEB01000015.1.
DR PDB; 1AQT; X-ray; 2.30 A; A=4-139.
DR PDB; 1BSH; NMR; -; A=2-139.
DR PDB; 1BSN; NMR; -; A=2-139.
DR PDB; 1FS0; X-ray; 2.10 A; E=2-139.
DR PDB; 1QO1; X-ray; 3.90 A; J=4-139.
DR PDB; 3OAA; X-ray; 3.26 A; H/P/X/f=2-139.
DR PDB; 5T4O; EM; 6.90 A; H=1-139.
DR PDB; 5T4P; EM; 7.77 A; H=1-139.
DR PDB; 5T4Q; EM; 8.53 A; H=1-139.
DR PDB; 6OQR; EM; 3.10 A; H=1-139.
DR PDB; 6OQS; EM; 3.30 A; H=1-139.
DR PDB; 6OQT; EM; 3.10 A; H=1-139.
DR PDB; 6OQU; EM; 3.20 A; H=1-139.
DR PDB; 6OQV; EM; 3.30 A; H=1-139.
DR PDB; 6OQW; EM; 3.10 A; H=1-139.
DR PDB; 6PQV; EM; 3.30 A; H=1-139.
DR PDB; 6WNQ; EM; 3.40 A; H=1-139.
DR PDB; 6WNR; EM; 3.30 A; H=1-139.
DR PDBsum; 1AQT; -.
DR PDBsum; 1BSH; -.
DR PDBsum; 1BSN; -.
DR PDBsum; 1FS0; -.
DR PDBsum; 1QO1; -.
DR PDBsum; 3OAA; -.
DR PDBsum; 5T4O; -.
DR PDBsum; 5T4P; -.
DR PDBsum; 5T4Q; -.
DR PDBsum; 6OQR; -.
DR PDBsum; 6OQS; -.
DR PDBsum; 6OQT; -.
DR PDBsum; 6OQU; -.
DR PDBsum; 6OQV; -.
DR PDBsum; 6OQW; -.
DR PDBsum; 6PQV; -.
DR PDBsum; 6WNQ; -.
DR PDBsum; 6WNR; -.
DR AlphaFoldDB; P0A6E6; -.
DR SMR; P0A6E6; -.
DR BioGRID; 4261177; 67.
DR BioGRID; 852547; 4.
DR ComplexPortal; CPX-4022; ATP synthase complex.
DR DIP; DIP-47828N; -.
DR IntAct; P0A6E6; 7.
DR STRING; 511145.b3731; -.
DR TCDB; 3.A.2.1.1; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR SWISS-2DPAGE; P0A6E6; -.
DR jPOST; P0A6E6; -.
DR PaxDb; P0A6E6; -.
DR PRIDE; P0A6E6; -.
DR EnsemblBacteria; AAC76754; AAC76754; b3731.
DR EnsemblBacteria; BAE77557; BAE77557; BAE77557.
DR GeneID; 67417718; -.
DR GeneID; 948245; -.
DR KEGG; ecj:JW3709; -.
DR KEGG; eco:b3731; -.
DR PATRIC; fig|1411691.4.peg.2969; -.
DR EchoBASE; EB0098; -.
DR eggNOG; COG0355; Bacteria.
DR HOGENOM; CLU_084338_2_0_6; -.
DR InParanoid; P0A6E6; -.
DR OMA; MGGFAEI; -.
DR PhylomeDB; P0A6E6; -.
DR BioCyc; EcoCyc:ATPC-MON; -.
DR BioCyc; MetaCyc:ATPC-MON; -.
DR BRENDA; 7.1.2.2; 2026.
DR EvolutionaryTrace; P0A6E6; -.
DR PRO; PR:P0A6E6; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IC:ComplexPortal.
DR GO; GO:0045259; C:proton-transporting ATP synthase complex; IPI:ComplexPortal.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IDA:EcoliWiki.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IDA:EcoCyc.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IMP:ComplexPortal.
DR CDD; cd12152; F1-ATPase_delta; 1.
DR Gene3D; 2.60.15.10; -; 1.
DR HAMAP; MF_00530; ATP_synth_epsil_bac; 1.
DR InterPro; IPR036794; ATP_F1_dsu/esu_C_sf.
DR InterPro; IPR001469; ATP_synth_F1_dsu/esu.
DR InterPro; IPR020547; ATP_synth_F1_dsu/esu_C.
DR InterPro; IPR020546; ATP_synth_F1_dsu/esu_N.
DR InterPro; IPR036771; ATPsynth_dsu/esu_N.
DR PANTHER; PTHR13822; PTHR13822; 1.
DR Pfam; PF00401; ATP-synt_DE; 1.
DR Pfam; PF02823; ATP-synt_DE_N; 1.
DR SUPFAM; SSF46604; SSF46604; 1.
DR SUPFAM; SSF51344; SSF51344; 1.
DR TIGRFAMs; TIGR01216; ATP_synt_epsi; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP synthesis; Cell inner membrane; Cell membrane; CF(1);
KW Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9868784, ECO:0000269|Ref.9"
FT CHAIN 2..139
FT /note="ATP synthase epsilon chain"
FT /id="PRO_0000188132"
FT CONFLICT 13
FT /note="E -> K (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 5..13
FT /evidence="ECO:0007829|PDB:1FS0"
FT STRAND 15..35
FT /evidence="ECO:0007829|PDB:1FS0"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:1FS0"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:1FS0"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:1AQT"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:1FS0"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:1FS0"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:1FS0"
FT HELIX 88..103
FT /evidence="ECO:0007829|PDB:1FS0"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:1AQT"
FT HELIX 115..133
FT /evidence="ECO:0007829|PDB:1FS0"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:1BSH"
SQ SEQUENCE 139 AA; 15068 MW; 5EFF7DE911745A62 CRC64;
MAMTYHLDVV SAEQQMFSGL VEKIQVTGSE GELGIYPGHA PLLTAIKPGM IRIVKQHGHE
EFIYLSGGIL EVQPGNVTVL ADTAIRGQDL DEARAMEAKR KAEEHISSSH GDVDYAQASA
ELAKAIAQLR VIELTKKAM
