ATP synthase gamma chain (P0ABA6)

Identification
Name:ATP synthase gamma chain
Synonyms:
  • ATP synthase F1 sector gamma subunit
  • F-ATPase gamma subunit
Gene Name:atpG
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. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex
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+1.0Thumb ↔ 1.0Thumb+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
macromolecular complex
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
proton-transporting ATPase activity, rotational mechanism
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:b3733
Gene OrientationCounterclockwise
Centisome Percentage:84.39
Left Sequence End3915425
Right Sequence End3916288
Gene Sequence:
>864 bp
GTGTGGGCGCTAACTGCGGATGCGGATTTTCTGGCGCAGCGGGGGCAAGGACAGGTTGAA
CAGGTCTTTGCCAGAGCGGTAAATATCGCACTCCCGGCTCGCCAGCAGTTGCTGACGCTG
CTTTGTGAAGAGTACGACAATGCGCCAAACAGTTGTCGGTTGGCACTCACTCACTTTGAT
GATCTGTTCCGGCATGGTGATAAGGTTCAGTTTGACGATCAAGGTATTACGGTTGGTCAA
CATCTTCATATAGAGATGAGTCGTTGTCGGCGTTGGCTGTCCCCAACCTTGCAAATGACC
GCTGTGAATTTTCACCTTATCGCCTGGCTACAGTGGCACGACATTATTCATCAGCACCTG
GGGGAAAATGAAACCCTGTTTAATTATCGCGGCGATAATCCGTTTTATCAGGCGTTAAAT
AAAGAATTACATATTAAACGACGGGCAGTTATTCAGGCCGTAAACGATAAACAAAATATC
GCCTCAGCGGTCGCCAGTATGATGGGGTTAGGGATTGGCCTTACGCCATCAGCCGACGAT
TATTTAACAGGTCTGGCGCTTATTTTATTTATTCCCGGGCATCCGGCGGAAAAATACAAA
GAGGAATTTTATCTCGGTCTGCAACGCGGCAAAAATAATACCACATTATTAAGTGCCATA
ACGCTGGAAGCCGCATTACAACAACGCTGCCGGGAAAATATTCATCGTTTTATTCACAAC
ATTATTTATGACATCCCTGGGAACGCAACTCAGGCAATAGAAAAAATTAAACATATTGGC
TCCAGTTCCGGCTGCGACATGCTGTATGGCATGGCCGATGGTTGTGCGCTGAGCCAAACC
TACGGAGGGAATTATGTCAGTTAA
Protein Properties
Pfam Domain Function:
Protein Residues:287
Protein Molecular Weight:31577
Protein Theoretical pI:9
PDB File:1FS0
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>ATP synthase gamma chain
MAGAKEIRSKIASVQNTQKITKAMEMVAASKMRKSQDRMAASRPYAETMRKVIGHLAHGN
LEYKHPYLEDRDVKRVGYLVVSTDRGLCGGLNINLFKKLLAEMKTWTDKGVQCDLAMIGS
KGVSFFNSVGGNVVAQVTGMGDNPSLSELIGPVKVMLQAYDEGRLDKLYIVSNKFINTMS
QVPTISQLLPLPASDDDDLKHKSWDYLYEPDPKALLDTLLRRYVESQVYQGVVENLASEQ
AARMVAMKAATDNGGSLIKELQLVYNKARQASITQELTEIVSGAAAV
References
External Links:
ResourceLink
Uniprot ID:P0ABA6
Uniprot Name:ATPG_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674462
PDB ID:1FS0
Ecogene ID:EG10104
Ecocyc:EG10104
ColiBase:b3733
Kegg Gene:b3733
EchoBASE ID:EB0102
CCDB:ATPG_ECOLI
BacMap:16131601
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
  • Hausrath, A. C., Gruber, G., Matthews, B. W., Capaldi, R. A. (1999). "Structural features of the gamma subunit of the Escherichia coli F(1) ATPase revealed by a 4.4-A resolution map obtained by x-ray crystallography." Proc Natl Acad Sci U S A 96:13697-13702. Pubmed: 10570135
  • 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
  • Iwamoto, A., Miki, J., Maeda, M., Futai, M. (1990). "H(+)-ATPase gamma subunit of Escherichia coli. Role of the conserved carboxyl-terminal region." J Biol Chem 265:5043-5048. Pubmed: 2138624
  • 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., Mabuchi, K., Futai, M. (1981). "Nucleotide sequence of the genes coding for alpha, beta and gamma subunits of the proton-translocating ATPase of Escherichia coli." Biochem Biophys Res Commun 103:604-612. Pubmed: 6277310
  • 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
  • Tang, C., Wilkens, S., Capaldi, R. A. (1994). "Structure of the gamma subunit of Escherichia coli F1 ATPase probed in trypsin digestion and biotin-avidin binding studies." J Biol Chem 269:4467-4472. Pubmed: 7508444
  • 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