ATP synthase subunit b

Details

Name
ATP synthase subunit b
Synonyms
  • ATP synthase F(0) sector subunit b
  • ATPase subunit I
  • F-ATPase subunit b
  • F-type ATPase subunit b
  • papF
  • uncF
Gene Name
atpF
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0016650|ATP synthase subunit b
MNLNATILGQAIAFVLFVLFCMKYVWPPLMAAIEKRQKEIADGLASAERAHKDLDLAKAS
ATDQLKKAKAEAQVIIEQANKRRSQILDEAKAEAEQERTKIVAQAQAEIEAERKRAREEL
RKQVAILAVAGAEKIIERSVDEAANSDIVDKLVAEL
Number of residues
156
Molecular Weight
17263.735
Theoretical pI
6.04
GO Classification
Functions
proton-transporting ATP synthase activity, rotational mechanism / proton-transporting ATPase activity, rotational mechanism
Processes
plasma membrane ATP synthesis coupled proton transport
Components
anchored component of membrane / integral component of membrane / plasma membrane / proton-transporting ATP synthase complex, coupling factor F(o)
General Function
Proton-transporting atpase activity, rotational mechanism
Specific Function
F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Pfam Domain Function
Transmembrane Regions
11-31
Cellular Location
Cell inner membrane
Gene sequence
>lcl|BSEQ0016651|ATP synthase subunit b (atpF)
GTGAATCTTAACGCAACAATCCTCGGCCAGGCCATCGCGTTTGTCCTGTTCGTTCTGTTC
TGCATGAAGTACGTATGGCCGCCATTAATGGCAGCCATCGAAAAACGTCAAAAAGAAATT
GCTGACGGCCTTGCTTCCGCAGAACGAGCACATAAGGACCTTGACCTTGCAAAGGCCAGC
GCGACCGACCAGCTGAAAAAAGCGAAAGCGGAAGCCCAGGTAATCATCGAGCAGGCGAAC
AAACGCCGCTCGCAGATTCTGGACGAAGCGAAAGCTGAGGCAGAACAGGAACGTACTAAA
ATCGTGGCCCAGGCGCAGGCGGAAATTGAAGCCGAGCGTAAACGTGCCCGTGAAGAGCTG
CGTAAGCAAGTTGCTATCCTGGCTGTTGCTGGCGCCGAGAAGATCATCGAACGTTCCGTG
GATGAAGCTGCTAACAGCGACATCGTGGATAAACTTGTCGCTGAACTGTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0ABA0
UniProtKB Entry NameATPF_ECOLI
GenBank Gene IDJ01594
General References
  1. Walker JE, Gay NJ, Saraste M, Eberle AN: 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. 1984 Dec 15;224(3):799-815. [Article]
  2. Gay NJ, Walker JE: 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. 1981 Aug 25;9(16):3919-26. [Article]
  3. Kanazawa H, Mabuchi K, Kayano T, Noumi T, Sekiya T, Futai M: Nucleotide sequence of the genes for F0 components of the proton-translocating ATPase from Escherichia coli: prediction of the primary structure of F0 subunits. Biochem Biophys Res Commun. 1981 Nov 30;103(2):613-20. [Article]
  4. Nielsen J, Hansen FG, Hoppe J, Friedl P, von Meyenburg K: 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. 1981;184(1):33-9. [Article]
  5. Kanazawa H, Futai M: Structure and function of H+-ATPase: what we have learned from Escherichia coli H+-ATPase. Ann N Y Acad Sci. 1982;402:45-64. [Article]
  6. Porter AC, Kumamoto C, Aldape K, Simoni RD: Role of the b subunit of the Escherichia coli proton-translocating ATPase. A mutagenic analysis. J Biol Chem. 1985 Jul 5;260(13):8182-7. [Article]
  7. Burland V, Plunkett G 3rd, Daniels DL, Blattner FR: DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication. Genomics. 1993 Jun;16(3):551-61. [Article]
  8. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  9. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  10. Mabuchi K, Kanazawa H, Kayano T, Futai M: Nucleotide sequence of the gene coding for the delta subunit of proton translocating ATPase of Escherichia coli. Biochem Biophys Res Commun. 1981 Sep 16;102(1):172-9. [Article]
  11. McCormick KA, Cain BD: Targeted mutagenesis of the b subunit of F1F0 ATP synthase in Escherichia coli: Glu-77 through Gln-85. J Bacteriol. 1991 Nov;173(22):7240-8. [Article]
  12. Stenberg F, Chovanec P, Maslen SL, Robinson CV, Ilag LL, von Heijne G, Daley DO: Protein complexes of the Escherichia coli cell envelope. J Biol Chem. 2005 Oct 14;280(41):34409-19. Epub 2005 Aug 3. [Article]
  13. Dmitriev O, Jones PC, Jiang W, Fillingame RH: Structure of the membrane domain of subunit b of the Escherichia coli F0F1 ATP synthase. J Biol Chem. 1999 May 28;274(22):15598-604. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03091IsoglutamineexperimentalunknownDetails