Escherichia coli K-12 substr. MG1655 Protein: ATP synthase F1 complex - beta subunit

Gene: atpD Accession Numbers: EG10101 (EcoCyc), b3732, ECK3725

Synonyms: papB, uncD

Regulation Summary Diagram: ?

Regulation summary diagram for atpD

Component of:
ATP synthase F1 complex (summary available)
ATP synthase / thiamin triphosphate synthase (extended summary available)

Subunit composition of ATP synthase F1 complex - beta subunit = [AtpD]3
         ATP synthase F1 complex - beta subunit = AtpD

The beta subunit contains the catalytic site. The complex is a homotrimer [Iwamoto91, Senior90]. The role of conserved residues surrounding the catalytic site has been studied [Li09].

Gene Citations: [Nielsen84, Jones83, Kasimoglu96]

Locations: inner membrane

Map Position: [3,914,016 <- 3,915,398] (84.36 centisomes, 304°)
Length: 1383 bp / 460 aa

Molecular Weight of Polypeptide: 50.325 kD (from nucleotide sequence)

pI: 5.1

Unification Links: ASAP:ABE-0012208 , CGSC:30 , DIP:DIP-31846N , EchoBASE:EB0099 , EcoGene:EG10101 , EcoliWiki:b3732 , Mint:MINT-1251407 , OU-Microarray:b3732 , PortEco:atpD , PR:PRO_000022189 , Pride:P0ABB4 , Protein Model Portal:P0ABB4 , RefSeq:NP_418188 , RegulonDB:EG10101 , SMR:P0ABB4 , String:511145.b3732 , Swiss-Model:P0ABB4 , UniProt:P0ABB4

Relationship Links: InterPro:IN-FAMILY:IPR000194 , InterPro:IN-FAMILY:IPR000793 , InterPro:IN-FAMILY:IPR003593 , InterPro:IN-FAMILY:IPR004100 , InterPro:IN-FAMILY:IPR005722 , InterPro:IN-FAMILY:IPR020003 , InterPro:IN-FAMILY:IPR024034 , InterPro:IN-FAMILY:IPR027417 , Panther:IN-FAMILY:PTHR15184:SF8 , PDB:Structure:1D8S , PDB:Structure:3OAA , Pfam:IN-FAMILY:PF00006 , Pfam:IN-FAMILY:PF00306 , Pfam:IN-FAMILY:PF02874 , Prosite:IN-FAMILY:PS00152 , Smart:IN-FAMILY:SM00382

In Paralogous Gene Group: 555 (4 members)

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

GO Terms:

Biological Process: GO:0006754 - ATP biosynthetic process Inferred by computational analysis [UniProtGOA11a]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a]
GO:0006811 - ion transport Inferred by computational analysis [UniProtGOA11a]
GO:0015986 - ATP synthesis coupled proton transport Inferred by computational analysis [GOA01a]
GO:0015991 - ATP hydrolysis coupled proton transport Inferred by computational analysis [GOA01a]
GO:0015992 - proton transport Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0042777 - plasma membrane ATP synthesis coupled proton transport Inferred by computational analysis [GOA06]
GO:0046034 - ATP metabolic process Inferred by computational analysis [GOA01a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Huang06, Lasserre06, Arifuzzaman06, Stenberg05, Butland05]
GO:0046961 - proton-transporting ATPase activity, rotational mechanism Inferred from experiment [Senior79]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016820 - hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances Inferred by computational analysis [GOA01a]
GO:0046933 - proton-transporting ATP synthase activity, rotational mechanism Inferred by computational analysis [GOA06, GOA01a]
Cellular Component: GO:0016020 - membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Lasserre06]
GO:0045261 - proton-transporting ATP synthase complex, catalytic core F(1) Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Senior79]
GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06]
GO:0033178 - proton-transporting two-sector ATPase complex, catalytic domain Inferred by computational analysis [GOA01a]

MultiFun Terms: cell structure membrane
metabolism energy metabolism, carbon ATP proton motive force interconversion
transport Channel-type Transporters Pyrophosphate Bond (ATP; GTP; P2) Hydrolysis-driven Active Transporters The H+- or Na+-translocating F-type, V-type and A-type ATPase (F-ATPase) Su

Essentiality data for atpD knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Subunit of: ATP synthase F1 complex

Subunit composition of ATP synthase F1 complex = [AtpC][AtpH][(AtpA)3][AtpG][(AtpD)3]
         ATP synthase F1 complex - epsilon subunit = AtpC (summary available)
         ATP synthase F1 complex - delta subunit = AtpH (summary available)
         ATP synthase F1 complex - alpha subunit = (AtpA)3 (summary available)
                 ATP synthase F1 complex - alpha subunit = AtpA
         ATP synthase F1 complex - gamma subunit = AtpG (summary available)
         ATP synthase F1 complex - beta subunit = (AtpD)3 (summary available)
                 ATP synthase F1 complex - beta subunit = AtpD

Component of: ATP synthase / thiamin triphosphate synthase (extended summary available)

The F1 complex of ATP synthase contains the catalytic sites. The complex consists of five subunits, each of which is required for activity [Senior90, Futai89]. The positive catalytic cooperativity of ATP hydrolysis by the F1 complex has been studied [Bulygin09].

Citations: [Sekiya14]

Last-Curated ? 30-Jun-2009 by Mackie A , Macquarie University

Subunit of: ATP synthase / thiamin triphosphate synthase

Synonyms: ATP synthase F0F1, ATP synthase F1F0

Subunit composition of ATP synthase / thiamin triphosphate synthase = [([AtpE]10)([AtpF]2)(AtpB)][(AtpC)(AtpH)([AtpA]3)(AtpG)([AtpD]3)]
         ATP synthase F0 complex = ([AtpE]10)([AtpF]2)(AtpB) (summary available)
                 ATP synthase F0 complex - subunit c = (AtpE)10
                 ATP synthase F0 complex - b subunit = (AtpF)2 (extended summary available)
                         ATP synthase F0 complex - b subunit = AtpF
                 ATP synthase F0 complex - a subunit = AtpB (extended summary available)
         ATP synthase F1 complex = (AtpC)(AtpH)([AtpA]3)(AtpG)([AtpD]3) (summary available)
                 ATP synthase F1 complex - epsilon subunit = AtpC (summary available)
                 ATP synthase F1 complex - delta subunit = AtpH (summary available)
                 ATP synthase F1 complex - alpha subunit = (AtpA)3 (summary available)
                         ATP synthase F1 complex - alpha subunit = AtpA
                 ATP synthase F1 complex - gamma subunit = AtpG (summary available)
                 ATP synthase F1 complex - beta subunit = (AtpD)3 (summary available)
                         ATP synthase F1 complex - beta subunit = AtpD

ATP synthase (also known as F0F1 synthase) catalyzes the synthesis of ATP from ADP and inorganic phosphate (Pi) under aerobic and anaerobic cell growth. ATP synthase uses the free energy derived from the transmembrane proton gradient to drive ATP synthesis (see review by [Senior88] and references therein). During fermentation ATP synthase functions in the reverse direction and catalyzes the hydrolysis of ATP to generate the electrochemical proton gradient needed for other membrane functions (see review by [Trchounian04] and references therein). ATP synthase is a rotary molecular nanomotor that couples the mechanical force of subunit rotation to the synthesis or hydrolysis of ATP at the enzyme's catalytic sites. Proton movement across the membrane generates subunit rotation which drives ATP synthesis by forcing sequential conformation change at each of the three catalytic sites.

ATP synthase is comprised of two subcomplexes known as F1 and F0 (see review by [Senior90] and references therein). The hydrophilic F1 complex consists of five subunits (α, β, γ, δ and ε) in a stoichiometry of 3:3:1:1:1. The F1 complex contains three catalytic sites located in the three α/β subunit pairs. The F0 complex is membrane-embedded and forms the proton channel through the membrane. This complex consists of three subunits (a, b and c) in a stoichiometry of 1:2:10. Functionally, ATP synthase may be considered tripartite, consisting of a rotor (γεc10), a rotor stalk or stator (b2δ) and three catalytic sites (α3β3) where ATP synthesis or hydrolysis occurs (see review by [Senior02] and comment by [Senior07]).

'Tri-site' and 'bi-site' modes of enzyme catalysis have been proposed [Cross81, Weber01, Boyer01]. Tri-site catalysis requires that all three catalytic sites are occupied and interact with each other; in bi-site catalysis the enzyme functions with two substrate filled catalytic sites.

Additional reviews: [Senior92, Weber03, Boyer93, Weber, Senior12]

Citations: [Wachter11, Wiedenmann09, BekeSomfai11, DAlessandro08, Kasimoglu96, Kol08, Cain89, Vik91]

Locations: membrane

GO Terms:

Cellular Component: GO:0045259 - proton-transporting ATP synthase complex

Last-Curated ? 16-Jan-2014 by Mackie A , Macquarie University

Enzymatic reaction of: ATP synthase

Synonyms: F-1F-0-type ATPase, ATP phosphohydrolase (H+-transporting), H+-transporting ATP synthase, F0F1-type ATP synthase, adenosinetriphosphatase, H+-transporting ATPase, proton translocating ATP synthase, F-type ATP synthase

EC Number:

Transport reaction diagram for ATP synthase

Alternative Substrates for ADP: GDP , IDP

Alternative Substrates for ATP: GTP , ITP

In Pathways: superpathway of histidine, purine, and pyrimidine biosynthesis , superpathway of purine nucleotides de novo biosynthesis II , superpathway of adenosine nucleotides de novo biosynthesis II , adenosine ribonucleotides de novo biosynthesis

The H+/ATP ratio reflects the number of protons transported for every molecule of ATP synthesized. Based on a model of rotational catalysis for ATP synthase the H+/ATP ratio is equal to the c/β subunit stoichiometric ratio which for E. coli K-12 is 3.3 (c103) [Jiang01]. A thermodynamic H+/ATP ratio of 4 for E. coli ATP synthase has been experimentally determined [Steigmiller08] and this value is used in the above equation. Dihydrogen phosphate is likely to be the phosphate donor during ATP synthesis [alShawi92].

Cofactors or Prosthetic Groups: Mg2+

Inhibitors (Unknown Mechanism): citreoviridin [Senior90] , aurovertin [Senior90] , quercetin [Dadi09] , trans-resveratrol [Dadi09] , fluoroaluminate [Senior90] , 4-chloro-7-nitrobenzo-2-oxa-1,3-diazole [Senior90] , dicyclohexylcarbodiimide [Senior90] , efrapeptin [Senior90]

Enzymatic reaction of: thiamin triphosphate synthase

Transport reaction diagram for thiamin triphosphate synthase

Sequence Features

Protein sequence of ATP synthase F1 complex - beta subunit with features indicated

Feature Class Location Citations Comment
Cleavage-of-Initial-Methionine 1
[Frutiger96, Link97, UniProt12b]
UniProt: Removed.
Chain 2 -> 460
UniProt: ATP synthase subunit beta;
Acetylation-Modification 70
Nucleotide-Phosphate-Binding-Region 150 -> 157
UniProt: ATP; Non-Experimental Qualifier: by similarity;
Mutagenesis-Variant 157
[Iwamoto91, UniProt15]
T → A or C: Impairs ATPase activity.

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Units:

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram


10/20/97 Gene b3732 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10101; confirmed by SwissProt match.


alShawi92: al-Shawi MK, Senior AE (1992). "Catalytic sites of Escherichia coli F1-ATPase. Characterization of unisite catalysis at varied pH." Biochemistry 31(3);878-85. PMID: 1531027

Arifuzzaman06: Arifuzzaman M, Maeda M, Itoh A, Nishikata K, Takita C, Saito R, Ara T, Nakahigashi K, Huang HC, Hirai A, Tsuzuki K, Nakamura S, Altaf-Ul-Amin M, Oshima T, Baba T, Yamamoto N, Kawamura T, Ioka-Nakamichi T, Kitagawa M, Tomita M, Kanaya S, Wada C, Mori H (2006). "Large-scale identification of protein-protein interaction of Escherichia coli K-12." Genome Res 16(5);686-91. PMID: 16606699

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

BekeSomfai11: Beke-Somfai T, Lincoln P, Norden B (2011). "Double-lock ratchet mechanism revealing the role of alphaSER-344 in FoF1 ATP synthase." Proc Natl Acad Sci U S A 108(12);4828-33. PMID: 21383131

Boyer01: Boyer PD (2001). "Toward an adequate scheme for the ATP synthase catalysis." Biochemistry (Mosc) 66(10);1058-66. PMID: 11736627

Boyer93: Boyer PD (1993). "The binding change mechanism for ATP synthase--some probabilities and possibilities." Biochim Biophys Acta 1140(3);215-50. PMID: 8417777

Bulygin09: Bulygin VV, Milgrom YM (2009). "A bi-site mechanism for Escherichia coli F(1)-ATPase accounts for the observed positive catalytic cooperativity." Biochim Biophys Acta 1787(8);1016-23. PMID: 19269272

Butland05: Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, Canadien V, Starostine A, Richards D, Beattie B, Krogan N, Davey M, Parkinson J, Greenblatt J, Emili A (2005). "Interaction network containing conserved and essential protein complexes in Escherichia coli." Nature 433(7025);531-7. PMID: 15690043

Cain89: Cain BD, Simoni RD (1989). "Proton translocation by the F1F0ATPase of Escherichia coli. Mutagenic analysis of the a subunit." J Biol Chem 264(6);3292-300. PMID: 2536742

Cross81: Cross RL (1981). "The mechanism and regulation of ATP synthesis by F1-ATPases." Annu Rev Biochem 50;681-714. PMID: 6455964

Dadi09: Dadi PK, Ahmad M, Ahmad Z (2009). "Inhibition of ATPase activity of Escherichia coli ATP synthase by polyphenols." Int J Biol Macromol 45(1);72-9. PMID: 19375450

DAlessandro08: D'Alessandro M, Turina P, Melandri BA (2008). "Intrinsic uncoupling in the ATP synthase of Escherichia coli." Biochim Biophys Acta 1777(12);1518-1527. PMID: 18952048

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Frutiger96: Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F. (1996). Data submission to UniProtKB on 1996-02.

Futai89: Futai M, Noumi T, Maeda M (1989). "ATP synthase (H+-ATPase): results by combined biochemical and molecular biological approaches." Annu Rev Biochem 58;111-36. PMID: 2528322

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

Gigliobianco13: Gigliobianco T, Gangolf M, Lakaye B, Pirson B, von Ballmoos C, Wins P, Bettendorff L (2013). "An alternative role of F(o)F(1)-ATP synthase in Escherichia coli: synthesis of thiamine triphosphate." Sci Rep 3;1071. PMID: 23323214

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Huang06: Huang CZ, Lin XM, Wu LN, Zhang DF, Liu D, Wang SY, Peng XX (2006). "Systematic identification of the subproteome of Escherichia coli cell envelope reveals the interaction network of membrane proteins and membrane-associated peripheral proteins." J Proteome Res 5(12);3268-76. PMID: 17137328

Iwamoto91: Iwamoto A, Omote H, Hanada H, Tomioka N, Itai A, Maeda M, Futai M (1991). "Mutations in Ser174 and the glycine-rich sequence (Gly149, Gly150, and Thr156) in the beta subunit of Escherichia coli H(+)-ATPase." J Biol Chem 266(25);16350-5. PMID: 1832155

Jiang01: Jiang W, Hermolin J, Fillingame RH (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(9);4966-71. PMID: 11320246

Jones83: Jones HM, Brajkovich CM, Gunsalus RP (1983). "In vivo 5' terminus and length of the mRNA for the proton-translocating ATPase (unc) operon of Escherichia coli." J Bacteriol 155(3);1279-87. PMID: 6193097

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Kasimoglu96: Kasimoglu E, Park SJ, Malek J, Tseng CP, Gunsalus RP (1996). "Transcriptional regulation of the proton-translocating ATPase (atpIBEFHAGDC) operon of Escherichia coli: control by cell growth rate." J Bacteriol 178(19);5563-7. PMID: 8824597

Kol08: Kol S, Nouwen N, Driessen AJ (2008). "The charge distribution in the cytoplasmic loop of subunit C of the F1F0 ATPase is a determinant for YidC targeting." J Biol Chem 283(15);9871-7. PMID: 18276587

Lasserre06: Lasserre JP, Beyne E, Pyndiah S, Lapaillerie D, Claverol S, Bonneu M (2006). "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis." Electrophoresis 27(16);3306-21. PMID: 16858726

Li09: Li W, Brudecki LE, Senior AE, Ahmad Z (2009). "Role of alpha -subunit VISIT-DG sequence residues Ser-347 and Gly-351 in the catalytic sites of Escherichia coli ATP synthase." J Biol Chem. PMID: 19240022

Link97: Link AJ, Robison K, Church GM (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18(8);1259-313. PMID: 9298646

Nielsen84: Nielsen J, Jorgensen BB, van Meyenburg KV, Hansen FG (1984). "The promoters of the atp operon of Escherichia coli K12." Mol Gen Genet 1984;193(1);64-71. PMID: 6318052

Pati89: Pati S, Brusilow WS (1989). "The roles of the alpha and gamma subunits in proton conduction through the Fo sector of the proton-translocating ATPase of Escherichia coli." J Biol Chem 264(5);2640-4. PMID: 2536718

Rajagopala14: Rajagopala SV, Sikorski P, Kumar A, Mosca R, Vlasblom J, Arnold R, Franca-Koh J, Pakala SB, Phanse S, Ceol A, Hauser R, Siszler G, Wuchty S, Emili A, Babu M, Aloy P, Pieper R, Uetz P (2014). "The binary protein-protein interaction landscape of Escherichia coli." Nat Biotechnol 32(3);285-90. PMID: 24561554

Sekiya14: Sekiya M, Hisasaka R, Iwamoto-Kihara A, Futai M, Nakanishi-Matsui M (2014). "A unique mechanism of curcumin inhibition on F1 ATPase." Biochem Biophys Res Commun 452(4);940-4. PMID: 25230139

Senior02: Senior AE, Nadanaciva S, Weber J (2002). "The molecular mechanism of ATP synthesis by F1F0-ATP synthase." Biochim Biophys Acta 1553(3);188-211. PMID: 11997128

Senior07: Senior AE (2007). "ATP synthase: motoring to the finish line." Cell 130(2);220-1. PMID: 17662937

Senior12: Senior AE (2012). "Two ATPases." J Biol Chem 287(36);30049-62. PMID: 22822068

Senior79: Senior AE, Fayle DR, Downie JA, Gibson F, Cox GB (1979). "Properties of membranes from mutant strains of Escherichia coli in which the beta-subunit of the adenosine triphosphatase is abnormal." Biochem J 180(1);111-8. PMID: 158358

Senior88: Senior AE (1988). "ATP synthesis by oxidative phosphorylation." Physiol Rev 68(1);177-231. PMID: 2892214

Senior90: Senior AE (1990). "The proton-translocating ATPase of Escherichia coli." Annu Rev Biophys Biophys Chem 19;7-41. PMID: 2141983

Senior92: Senior AE (1992). "Catalytic sites of Escherichia coli F1-ATPase." J Bioenerg Biomembr 24(5);479-84. PMID: 1429542

Steigmiller08: Steigmiller S, Turina P, Graber P (2008). "The thermodynamic H+/ATP ratios of the H+-ATPsynthases from chloroplasts and Escherichia coli." Proc Natl Acad Sci U S A 105(10);3745-50. PMID: 18316723

Stenberg05: Stenberg F, Chovanec P, Maslen SL, Robinson CV, Ilag LL, von Heijne G, Daley DO (2005). "Protein complexes of the Escherichia coli cell envelope." J Biol Chem 280(41);34409-19. PMID: 16079137

Trchounian04: Trchounian A (2004). "Escherichia coli proton-translocating F0F1-ATP synthase and its association with solute secondary transporters and/or enzymes of anaerobic oxidation-reduction under fermentation." Biochem Biophys Res Commun 315(4);1051-7. PMID: 14985119

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt12b: UniProt Consortium (2012). "UniProt version 2012-02 released on 2012-02-29 00:00:00." Database.

UniProt15: UniProt Consortium (2015). "UniProt version 2015-01 released on 2015-01-16 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Vik91: Vik SB, Lee D, Marshall PA (1991). "Temperature-sensitive mutations at the carboxy terminus of the alpha subunit of the Escherichia coli F1F0 ATP synthase." J Bacteriol 173(14);4544-8. PMID: 1829729

Wachter11: Wachter A, Bi Y, Dunn SD, Cain BD, Sielaff H, Wintermann F, Engelbrecht S, Junge W (2011). "Two rotary motors in F-ATP synthase are elastically coupled by a flexible rotor and a stiff stator stalk." Proc Natl Acad Sci U S A 108(10);3924-9. PMID: 21368147

Weber: Weber J "ATP synthase: subunit-subunit interactions in the stator stalk." Biochim Biophys Acta 1757(9-10);1162-70. PMID: 16730323

Weber01: Weber J, Senior AE (2001). "Bi-site catalysis in F1-ATPase: does it exist?." J Biol Chem 276(38);35422-8. PMID: 11451960

Weber03: Weber J, Senior AE (2003). "ATP synthesis driven by proton transport in F1F0-ATP synthase." FEBS Lett 545(1);61-70. PMID: 12788493

Wiedenmann09: Wiedenmann A, Dimroth P, von Ballmoos C (2009). "Functional asymmetry of the F(0) motor in bacterial ATP synthases." Mol Microbiol 72(2);479-90. PMID: 19317834

Yu08: Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG (2008). "The diversity of lysine-acetylated proteins in Escherichia coli." J Microbiol Biotechnol 18(9);1529-36. PMID: 18852508

Other References Related to Gene Regulation

Arechaga03: Arechaga I, Miroux B, Runswick MJ, Walker JE (2003). "Over-expression of Escherichia coli F1F(o)-ATPase subunit a is inhibited by instability of the uncB gene transcript." FEBS Lett 547(1-3);97-100. PMID: 12860393

Kumar11: Kumar R, Shimizu K (2011). "Transcriptional regulation of main metabolic pathways of cyoA, cydB, fnr, and fur gene knockout Escherichia coli in C-limited and N-limited aerobic continuous cultures." Microb Cell Fact 10;3. PMID: 21272324

Lin12b: Lin X, Wang C, Guo C, Tian Y, Li H, Peng X (2012). "Differential regulation of OmpC and OmpF by AtpB in Escherichia coli exposed to nalidixic acid and chlortetracycline." J Proteomics 75(18);5898-910. PMID: 22960566

Marzan13: Marzan LW, Hasan CM, Shimizu K (2013). "Effect of acidic condition on the metabolic regulation of Escherichia coli and its phoB mutant." Arch Microbiol 195(3);161-71. PMID: 23274360

Salmon03: Salmon K, Hung SP, Mekjian K, Baldi P, Hatfield GW, Gunsalus RP (2003). "Global gene expression profiling in Escherichia coli K12. The effects of oxygen availability and FNR." J Biol Chem 278(32);29837-55. PMID: 12754220

Walker84: Walker JE, Gay NJ, Saraste M, Eberle AN (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(3);799-815. PMID: 6395859

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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