Identification
Name:ATP synthase subunit delta
Synonyms:
  • ATP synthase F(1) sector subunit delta
  • F-type ATPase subunit delta
  • F-ATPase subunit delta
Gene Name:atpH
Enzyme Class:Not Available
Biological Properties
General Function:Involved in hydrogen ion transporting ATP synthase activity, rotational mechanism
Specific Function:This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction
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
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Component
cell part
macromolecular complex
membrane
plasma membrane
protein complex
proton-transporting ATP synthase complex, catalytic core F(1)
proton-transporting two-sector ATPase complex, catalytic domain
Function
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
substrate-specific transmembrane transporter activity
transmembrane transporter activity
transporter activity
Process
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
Blattner:b3735
Gene OrientationCounterclockwise
Centisome Percentage:84.44
Left Sequence End3917893
Right Sequence End3918426
Gene Sequence:
>534 bp
ATGAAAACGCGTATTCATGTTGTGCAGGGTGATATTACCAAACTGGCCGTTGATGTGATT
GTGAATGCGGCTAATCCGTCATTAATGGGAGGCGGCGGCGTCGATGGGGCCATTCATCGC
GCAGCGGGTCCGGCCCTGCTGGATGCTTGTTTAAAAGTCAGGCAACAGCAGGGCGATTGC
CCTACGGGGCATGCCGTTATTACGCTTGCAGGCGATCTTCCCGCTAAAGCCGTAGTGCAC
ACCGTCGGGCCAGTCTGGCGTGGTGGTGAACAAAACGAAGACCAGCTTTTGCAGGATGCC
TATCTCAATAGCCTACGACTGGTGGCGGCAAACAGCTATACGTCAGTGGCTTTTCCTGCA
ATCAGTACTGGGGTTTATGGTTACCCTCGTGCGGCAGCGGCTGAAATCGCAGTAAAAACC
GTTTCAGAATTTATTACCCGTCACGCTTTACCCGAACAGGTATACTTTGTCTGTTATGAT
GAAGAAAACGCCCACCTCTACGAAAGACTCCTTACCCAACAAGGAGATGAATGA
Protein Properties
Pfam Domain Function:
Protein Residues:177
Protein Molecular Weight:19332
Protein Theoretical pI:5
PDB File:1ABV
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>ATP synthase subunit delta
MSEFITVARPYAKAAFDFAVEHQSVERWQDMLAFAAEVTKNEQMAELLSGALAPETLAES
FIAVCGEQLDENGQNLIRVMAENGRLNALPDVLEQFIHLRAVSEATAEVDVISAAALSEQ
QLAKISAAMEKRLSRKVKLNCKIDKSVMAGVIIRAGDMVIDGSVRGRLERLADVLQS
References
External Links:
ResourceLink
Uniprot ID:P0ABA4
Uniprot Name:ATPD_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4062616
PDB ID:1ABV
Ecogene ID:EG10105
Ecocyc:EG10105
ColiBase:b3735
Kegg Gene:b3735
EchoBASE ID:EB0103
CCDB:ATPD_ECOLI
BacMap:16131603
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
  • 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
  • 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
  • Mabuchi, K., Kanazawa, H., Kayano, T., Futai, M. (1981). "Nucleotide sequence of the gene coding for the delta subunit of proton translocating ATPase of Escherichia coli." Biochem Biophys Res Commun 102:172-179. Pubmed: 6458296
  • 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
  • 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
  • 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
  • Wilkens, S., Dunn, S. D., Chandler, J., Dahlquist, F. W., Capaldi, R. A. (1997). "Solution structure of the N-terminal domain of the delta subunit of the E. coli ATPsynthase." Nat Struct Biol 4:198-201. Pubmed: 9164460