ATP synthase subunit alpha (P0ABB0)

Identification
Name:ATP synthase subunit alpha
Synonyms:
  • ATP synthase F1 sector subunit alpha
  • F-ATPase subunit alpha
Gene Name:atpA
Enzyme Class:
Biological Properties
General Function:Involved in ATP binding
Specific Function:Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit
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
Complex Reactions:
1.0Thumb+1.0Thumb+1.0H(+)(In) → 1.0Thumb+1.0Thumb+1.0H(+)(Out)
1.0Adenosine triphosphate + 1.0Water + 1.0H(+)(In) → 1.0ADP + 1.0Inorganic phosphate + 1.0H(+)(Out)
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Component
macromolecular complex
protein complex
proton-transporting ATP synthase complex, catalytic core F(1)
proton-transporting two-sector ATPase complex
proton-transporting two-sector ATPase complex, catalytic domain
Function
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
binding
catalytic activity
cation transmembrane transporter activity
hydrogen ion transmembrane transporter activity
hydrogen ion transporting ATP synthase activity, rotational mechanism
hydrolase activity
hydrolase activity, acting on acid anhydrides
hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
inorganic cation transmembrane transporter activity
ion transmembrane transporter activity
monovalent inorganic cation transmembrane transporter activity
nucleoside binding
proton-transporting ATPase activity, rotational mechanism
purine nucleoside binding
substrate-specific transmembrane transporter activity
transmembrane transporter activity
transporter activity
Process
ATP biosynthetic process
ATP metabolic process
ATP synthesis coupled proton transport
cellular nitrogen compound metabolic process
establishment of localization
hydrogen transport
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
proton transport
purine nucleoside triphosphate biosynthetic process
purine nucleoside triphosphate metabolic process
purine nucleotide biosynthetic process
purine nucleotide metabolic process
purine ribonucleoside triphosphate biosynthetic process
purine ribonucleoside triphosphate metabolic process
transport
Gene Properties
Blattner:b3734
Gene OrientationCounterclockwise
Centisome Percentage:84.41
Left Sequence End3916339
Right Sequence End3917880
Gene Sequence:
>1542 bp
ATGCGTCTGGAAGTCTTTTGTGAAGACCGACTCGGTCTGACCCGCGAATTACTCGATCTA
CTCGTGCTAAGAGGCATTGATTTACGCGGTATTGAGATTGATCCCATTGGGCGAATCTAC
CTCAATTTTGCTGAACTGGAGTTTGAGAGTTTCAGCAGTCTGATGGCCGAAATACGCCGT
ATTGCGGGTGTTACCGATGTGCGTACTGTCCCGTGGATGCCTTCCGAACGTGAGCATCTG
GCGTTGAGCGCGTTACTGGAGGCGTTGCCTGAACCTGTGCTCTCTGTCGATATGAAAAGC
AAAGTGGATATGGCGAACCCGGCGAGCTGTCAGCTTTTTGGGCAAAAATTGGATCGCCTG
CGCAACCATACCGCCGCACAATTGATTAACGGCTTTAATTTTTTACGTTGGCTGGAAAGC
GAACCGCAAGATTCGCATAACGAGCATGTCGTTATTAATGGGCAGAATTTCCTGATGGAG
ATTACGCCTGTTTATCTTCAGGATGAAAATGATCAACACGTCCTGACCGGTGCGGTGGTG
ATGTTGCGATCAACGATTCGTATGGGCCGCCAGTTGCAAAATGTCGCCGCCCAGGACGTC
AGCGCCTTCAGTCAAATTGTCGCCGTCAGCCCGAAAATGAAGCATGTTGTCGAACAGGCG
CAGAAACTGGCGATGCTAAGCGCGCCGCTGCTGATTACGGGTGACACAGGTACAGGTAAA
GATCTCTTTGCCTACGCCTGCCATCAGGCAAGCCCCAGAGCGGGCAAACCTTACCTGGCG
CTGAACTGTGCGTCTATACCGGAAGATGCGGTCGAGAGTGAACTGTTTGGTCATGCTCCG
GAAGGGAAGAAAGGATTCTTTGAGCAGGCGAACGGTGGTTCGGTGCTGTTGGATGAAATA
GGGGAAATGTCACCACGGATGCAGGCGAAATTACTGCGTTTCCTTAATGATGGCACTTTC
CGTCGGGTTGGCGAAGACCATGAGGTGCATGTCGATGTGCGGGTGATTTGCGCTACGCAG
AAGAATCTGGTCGAACTGGTGCAAAAAGGCATGTTCCGTGAAGATCTCTATTATCGTCTG
AACGTGTTGACGCTCAATCTGCCGCCGCTACGTGACTGTCCGCAGGACATCATGCCGTTA
ACTGAGCTGTTCGTCGCCCGCTTTGCCGACGAGCAGGGCGTGCCGCGTCCGAAACTGGCC
GCTGACCTGAATACTGTACTTACGCGTTATGCGTGGCCGGGAAATGTGCGGCAGTTAAAG
AACGCTATCTATCGCGCACTGACACAACTGGACGGTTATGAGCTGCGTCCACAGGATATT
TTGTTGCCGGATTATGACGCCGCAACGGTAGCCGTGGGCGAAGATGCGATGGAAGGTTCG
CTGGACGAAATCACCAGCCGTTTTGAACGCTCGGTATTAACCCAGCTTTATCGCAATTAT
CCCAGCACGCGCAAACTGGCAAAACGTCTCGGCGTTTCACATACCGCGATTGCCAATAAG
TTGCGGGAATATGGTCTGAGTCAGAAGAAGAACGAAGAGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:513
Protein Molecular Weight:55222
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>ATP synthase subunit alpha
MQLNSTEISELIKQRIAQFNVVSEAHNEGTIVSVSDGVIRIHGLADCMQGEMISLPGNRY
AIALNLERDSVGAVVMGPYADLAEGMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGP
LDHDGFSAVEAIAPGVIERQSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQTGKTALAI
DAIINQRDSGIKCIYVAIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPY
AGCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLER
AARVNAEYVEAFTKGEVKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLF
NAGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQYRELAAFSQFASDLDDATRKQ
LDHGQKVTELLKQKQYAPMSVAQQSLVLFAAERGYLADVELSKIGSFEAALLAYVDRDHA
PLMQEINQTGGYNDEIEGKLKGILDSFKATQSW
References
External Links:
ResourceLink
Uniprot ID:P0ABB0
Uniprot Name:ATPA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1742168
Ecogene ID:EG10098
Ecocyc:EG10098
ColiBase:b3734
Kegg Gene:b3734
EchoBASE ID:EB0096
CCDB:ATPA_ECOLI
BacMap:16131602
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 region encoding the alpha-subunit of Escherichia coli ATP-synthase." Nucleic Acids Res 9:2187-2194. Pubmed: 6272228
  • 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
  • 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
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
  • 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
  • Rao, R., Pagan, J., Senior, A. E. (1988). "Directed mutagenesis of the strongly conserved lysine 175 in the proposed nucleotide-binding domain of alpha-subunit from Escherichia coli F1-ATPase." J Biol Chem 263:15957-15963. Pubmed: 2903146
  • Stan-Lotter, H., Clarke, D. M., Bragg, P. D. (1986). "Isolation of a fourth cysteinyl-containing peptide of the alpha-subunit of the F1 ATPase from Escherichia coli necessitates revision of the DNA sequence." FEBS Lett 197:121-124. Pubmed: 2868922
  • 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