Name:ATP synthase subunit c
  • ATP synthase F(0) sector subunit c
  • Dicyclohexylcarbodiimide-binding protein
  • F-type ATPase subunit c
  • F-ATPase subunit c
  • Lipid-binding protein
Gene Name:atpE
Enzyme Class:Not Available
Biological Properties
General Function:Involved in hydrogen ion transmembrane transporter activity
Specific Function:Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of 10 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits
Cellular Location:Cell inner membrane; Multi-pass 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, coupling factor F(o)
proton-transporting two-sector ATPase complex, proton-transporting domain
cation transmembrane transporter activity
hydrogen ion transmembrane transporter activity
inorganic cation transmembrane transporter activity
ion transmembrane transporter activity
monovalent inorganic cation transmembrane transporter activity
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:84.47
Left Sequence End3918973
Right Sequence End3919212
Gene Sequence:
>240 bp
Protein Properties
Pfam Domain Function:
Protein Residues:79
Protein Molecular Weight:8256
Protein Theoretical pI:4
PDB File:1C0V
Signaling Regions:
  • None
Transmembrane Regions:
  • 11-31
  • 53-73
Protein Sequence:
>ATP synthase subunit c
External Links:
Uniprot ID:P68699
Uniprot Name:ATPL_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85675138
Ecogene ID:EG10102
Kegg Gene:b3737
EchoBASE ID:EB0100
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
  • Daley, D. O., Rapp, M., Granseth, E., Melen, K., Drew, D., von Heijne, G. (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308:1321-1323. Pubmed: 15919996
  • Fimmel, A. L., Jans, D. A., Langman, L., James, L. B., Ash, G. R., Downie, J. A., Senior, A. E., Gibson, F., Cox, G. B. (1983). "The F1F0-ATPase of Escherichia coli. Substitution of proline by leucine at position 64 in the c-subunit causes loss of oxidative phosphorylation." Biochem J 213:451-458. Pubmed: 6193778
  • Gay, N. J., Walker, J. E. (1981). "The atp operon: nucleotide sequence of the promoter and the genes for the membrane proteins, and the delta subunit of Escherichia coli ATP-synthase." Nucleic Acids Res 9:3919-3926. Pubmed: 6272190
  • Girvin, M. E., Fillingame, R. H. (1995). "Determination of local protein structure by spin label difference 2D NMR: the region neighboring Asp61 of subunit c of the F1F0 ATP synthase." Biochemistry 34:1635-1645. Pubmed: 7849023
  • Girvin, M. E., Rastogi, V. K., Abildgaard, F., Markley, J. L., Fillingame, R. H. (1998). "Solution structure of the transmembrane H+-transporting subunit c of the F1F0 ATP synthase." Biochemistry 37:8817-8824. Pubmed: 9636021
  • Groth, G., Walker, J. E. (1997). "Model of the c-subunit oligomer in the membrane domain of F-ATPases." FEBS Lett 410:117-123. Pubmed: 9237612
  • 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
  • Jans, D. A., Fimmel, A. L., Langman, L., James, L. B., Downie, J. A., Senior, A. E., Ash, G. R., Gibson, F., Cox, G. B. (1983). "Mutations in the uncE gene affecting assembly of the c-subunit of the adenosine triphosphatase of Escherichia coli." Biochem J 211:717-726. Pubmed: 6309138
  • Jiang, W., Hermolin, J., Fillingame, R. H. (2001). "The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10." Proc Natl Acad Sci U S A 98:4966-4971. Pubmed: 11320246
  • Kanazawa, H., Mabuchi, K., Kayano, T., Tamura, F., Futai, M. (1981). "Nucleotide sequence of genes coding for dicyclohexylcarbodiimide-binding protein and the alpha subunit of proton-translocating ATPase of Escherichia coli." Biochem Biophys Res Commun 100:219-225. Pubmed: 6266400
  • Nielsen, J., Hansen, F. G., Hoppe, J., Friedl, P., von Meyenburg, K. (1981). "The nucleotide sequence of the atp genes coding for the F0 subunits a, b, c and the F1 subunit delta of the membrane bound ATP synthase of Escherichia coli." Mol Gen Genet 184:33-39. Pubmed: 6278247
  • Norwood, T. J., Crawford, D. A., Steventon, M. E., Driscoll, P. C., Campbell, I. D. (1992). "Heteronuclear 1H-15N nuclear magnetic resonance studies of the c subunit of the Escherichia coli F1F0 ATP synthase: assignment and secondary structure." Biochemistry 31:6285-6290. Pubmed: 1385726
  • Rastogi, V. K., Girvin, M. E. (1999). "Structural changes linked to proton translocation by subunit c of the ATP synthase." Nature 402:263-268. Pubmed: 10580496
  • Wachter, E., Schmid, R., Deckers, G., Altendorf, K. (1980). "Amino acid replacement in dicyclohexylcarbodiimide-reactive proteins from mutant strains of Escherichia coli defective in the energy-transducing ATPase complex." FEBS Lett 113:265-270. Pubmed: 6446460
  • 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