Name:ATP synthase epsilon chain
  • ATP synthase F1 sector epsilon subunit
  • F-ATPase epsilon subunit
Gene Name:atpC
Enzyme Class:Not Available
Biological Properties
General Function:Involved in hydrogen ion transporting ATP synthase activity, rotational mechanism
Specific Function:Produces ATP from ADP in the presence of a proton gradient across the membrane
Cellular Location:Cell inner membrane; Peripheral membrane protein
SMPDB Pathways:
  • Oxidative phosphorylation PW000919
  • purine nucleotides de novo biosynthesis PW000910
  • purine nucleotides de novo biosynthesis 1435709748 PW000960
  • purine nucleotides de novo biosynthesis 2 PW002033
KEGG Pathways:
SMPDB Reactions:
1.0Adenosine diphosphate+1.0Thumb+4.0Thumb+1.0Thumb1.0Thumb+3.0Thumb+1.0Thumb
1.0Adenosine diphosphate + 1.0Phosphate + 4.0Hydrogen ion + 1.0ADP ↔ 1.0Water + 3.0Hydrogen ion + 1.0Adenosine triphosphate
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
GO Classification:
macromolecular complex
protein complex
proton-transporting ATP synthase complex, catalytic core F(1)
proton-transporting two-sector ATPase complex, catalytic domain
cation transmembrane transporter activity
hydrogen ion transmembrane transporter activity
hydrogen ion transporting ATP synthase activity, rotational mechanism
inorganic cation transmembrane transporter activity
ion transmembrane transporter activity
monovalent inorganic cation transmembrane transporter activity
proton-transporting ATPase activity, rotational mechanism
substrate-specific transmembrane transporter activity
transmembrane transporter activity
transporter activity
ATP biosynthetic process
ATP synthesis coupled proton transport
cellular nitrogen compound metabolic process
metabolic process
nitrogen compound metabolic process
nucleobase, nucleoside and nucleotide metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleoside phosphate metabolic process
nucleotide metabolic process
purine nucleoside triphosphate biosynthetic process
purine nucleotide biosynthetic process
purine nucleotide metabolic process
purine ribonucleoside triphosphate biosynthetic process
Gene Properties
Gene OrientationCounterclockwise
Centisome Percentage:84.35
Left Sequence End3913576
Right Sequence End3913995
Gene Sequence:
>420 bp
Protein Properties
Pfam Domain Function:
Protein Residues:139
Protein Molecular Weight:15068
Protein Theoretical pI:6
PDB File:1FS0
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>ATP synthase epsilon chain
External Links:
Uniprot ID:P0A6E6
Uniprot Name:ATPE_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674556
Ecogene ID:EG10100
Kegg Gene:b3731
EchoBASE ID:EB0098
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Burland, V., Plunkett, G. 3rd, Daniels, D. L., Blattner, F. R. (1993). "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication." Genomics 16:551-561. Pubmed: 7686882
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Kanazawa, H., Futai, M. (1982). "Structure and function of H+-ATPase: what we have learned from Escherichia coli H+-ATPase." Ann N Y Acad Sci 402:45-64. Pubmed: 6301339
  • Kanazawa, H., Kayano, T., Kiyasu, T., Futai, M. (1982). "Nucleotide sequence of the genes for beta and epsilon subunits of proton-translocating ATPase from Escherichia coli." Biochem Biophys Res Commun 105:1257-1264. Pubmed: 6285901
  • Saraste, M., Gay, N. J., Eberle, A., Runswick, M. J., Walker, J. E. (1981). "The atp operon: nucleotide sequence of the genes for the gamma, beta, and epsilon subunits of Escherichia coli ATP synthase." Nucleic Acids Res 9:5287-5296. Pubmed: 6272217
  • Stenberg, F., Chovanec, P., Maslen, S. L., Robinson, C. V., Ilag, L. L., von Heijne, G., Daley, D. O. (2005). "Protein complexes of the Escherichia coli cell envelope." J Biol Chem 280:34409-34419. Pubmed: 16079137
  • Uhlin, U., Cox, G. B., Guss, J. M. (1997). "Crystal structure of the epsilon subunit of the proton-translocating ATP synthase from Escherichia coli." Structure 5:1219-1230. Pubmed: 9331422
  • Walker, J. E., Gay, N. J., Saraste, M., Eberle, A. N. (1984). "DNA sequence around the Escherichia coli unc operon. Completion of the sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS and phoS." Biochem J 224:799-815. Pubmed: 6395859
  • Wasinger, V. C., Humphery-Smith, I. (1998). "Small genes/gene-products in Escherichia coli K-12." FEMS Microbiol Lett 169:375-382. Pubmed: 9868784
  • Wilkens, S., Capaldi, R. A. (1998). "Solution structure of the epsilon subunit of the F1-ATPase from Escherichia coli and interactions of this subunit with beta subunits in the complex." J Biol Chem 273:26645-26651. Pubmed: 9756905
  • Wilkens, S., Dahlquist, F. W., McIntosh, L. P., Donaldson, L. W., Capaldi, R. A. (1995). "Structural features of the epsilon subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy." Nat Struct Biol 2:961-967. Pubmed: 7583669