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Escherichia coli K-12 substr. MG1655 Transporter: 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

Summary:
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

Gene-Reaction Schematic: ?

GO Terms:

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

Credits:
Curated 18-May-2008 by Nolan L , Macquarie University
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: 3.6.3.14

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

Summary:
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) [Jiang01a]. 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


Subunit of ATP synthase / thiamin triphosphate synthase: ATP synthase F0 complex

Summary:
The F0 complex of ATP synthase functions as the proton channel and consists of three subunits. All are required for a functional F0 complex. The F0 complex is membrane-bound. [Senior90, DeckersHebestre92]


Subunit of ATP synthase F0 complex: ATP synthase F0 complex - subunit c

Synonyms: papH, uncE, dicyclohexylcarbodiimide-binding protein

Gene: atpE Accession Numbers: EG10102 (EcoCyc), b3737, ECK3730

Locations: inner membrane

Subunit composition of ATP synthase F0 complex - subunit c = [AtpE]10

Map Position: [3,918,973 <- 3,919,212] (84.47 centisomes)
Length: 240 bp / 79 aa

Molecular Weight of Polypeptide: 8.256 kD (from nucleotide sequence)

pI: 4.69

GO Terms:

Biological Process: GO:0006754 - ATP biosynthetic process Inferred by computational analysis [UniProtGOA11]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11]
GO:0006811 - ion transport Inferred by computational analysis [UniProtGOA11]
GO:0015986 - ATP synthesis coupled proton transport Inferred by computational analysis [GOA01]
GO:0015991 - ATP hydrolysis coupled proton transport Inferred by computational analysis [GOA01]
GO:0015992 - proton transport Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0046933 - proton-transporting ATP synthase activity, rotational mechanism Inferred from experiment [Aris85]
GO:0046961 - proton-transporting ATPase activity, rotational mechanism Inferred from experiment [Foster82]
GO:0008289 - lipid binding Inferred by computational analysis [UniProtGOA11]
GO:0015078 - hydrogen ion transmembrane transporter activity Inferred by computational analysis [GOA01]
Cellular Component: GO:0016021 - integral component of membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, Aris85]
GO:0045263 - proton-transporting ATP synthase complex, coupling factor F(o) Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA01, Foster82]
GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11a, UniProtGOA11]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11]
GO:0033177 - proton-transporting two-sector ATPase complex, proton-transporting domain Inferred by computational analysis [GOA01]

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

Unification Links: EcoliWiki:b3737 , Mint:MINT-8087956 , ModBase:P68699 , PR:PRO_000022190 , Pride:P68699 , Protein Model Portal:P68699 , RefSeq:NP_418193 , SMR:P68699 , String:511145.b3737 , UniProt:P68699

Relationship Links: InterPro:IN-FAMILY:IPR000454 , InterPro:IN-FAMILY:IPR002379 , InterPro:IN-FAMILY:IPR005953 , InterPro:IN-FAMILY:IPR020537 , PDB:Structure:1A91 , PDB:Structure:1ATY , PDB:Structure:1C0V , PDB:Structure:1C17 , PDB:Structure:1C99 , PDB:Structure:1IJP , PDB:Structure:1J7F , PDB:Structure:1L6T , PDB:Structure:1QO1 , Pfam:IN-FAMILY:PF00137 , Prints:IN-FAMILY:PR00124 , Prosite:IN-FAMILY:PS00605

Summary:
The c subunit of the F0 complex of ATP synthase is absolutely required for proton translocation and is also necessary for binding of the F1 complex. The number of subunit c monomers determines the number of transported ions per revolution. The stoichiometry of the subunits has been obtained within the range of 9 to 18 [DeckersHebestre92, Norwood92, Fillingame91, Senior90, Jones98] however, the preferred number of c subunits is 10 [Jiang01a, Ballhausen09]. Quantitation, cross-linking and reconstitution experiments with wild-type and mutant F0 show that the stoichiometry of subunit-c is independent of its rate of synthesis [Krebstakies08]. This is the subunit affected by the inhibitor dicyclohexylcarbodiimide.

Mutational and cross-linking studies indicate that transmembrane helices (TMH) 4 and 5 of subunit a pack in close proximity to TMH2 of subunit c. Additional studies suggest that pH-dependent conformational change may be related to the proposed role of TMH5 of subunit-a in gating H(+) access from the periplasm to TMH2 of subunit-c [Moore08].

The initiating methionine is cleaved [Wasinger98].

Chemical modification studies suggest that the ion exit channel lies between the interface of subunit-c and subunit-a. Other models suggest that ions exit through an aqueous channel in subunit-c or a second half channel in subunit-a [Angevine03].

It has been suggested that the structural divergence of the c-subunit ring and the a-subunits between bacterial species may allow development of species specific drugs which target these subunits [Maeda08].

Gene Citations: [Nielsen84, Jones83, Kasimoglu96]

Essentiality data for atpE 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 Indeterminate 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
No [Feist07, Comment 4]

Subunit of ATP synthase F0 complex: ATP synthase F0 complex - b subunit

Synonyms: papF, uncF, B chain

Gene: atpF Accession Numbers: EG10103 (EcoCyc), b3736, ECK3729

Locations [Comment 5]: inner membrane

Subunit composition of ATP synthase F0 complex - b subunit = [AtpF]2
         ATP synthase F0 complex - b subunit = AtpF

Map Position: [3,918,441 <- 3,918,911] (84.46 centisomes)
Length: 471 bp / 156 aa

Molecular Weight of Polypeptide: 17.264 kD (from nucleotide sequence)

pI: 6.26

GO Terms:

Biological Process: GO:0006754 - ATP biosynthetic process Inferred by computational analysis [UniProtGOA11]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11]
GO:0006811 - ion transport Inferred by computational analysis [UniProtGOA11]
GO:0015986 - ATP synthesis coupled proton transport Inferred by computational analysis [GOA01]
GO:0015992 - proton transport Inferred by computational analysis [UniProtGOA11]
GO:0042777 - plasma membrane ATP synthesis coupled proton transport Inferred by computational analysis [GOA06]
Molecular Function: GO:0046933 - proton-transporting ATP synthase activity, rotational mechanism Inferred from experiment Inferred by computational analysis [GOA06, Aris85]
GO:0046961 - proton-transporting ATPase activity, rotational mechanism Inferred from experiment [Foster82]
GO:0015078 - hydrogen ion transmembrane transporter activity Inferred by computational analysis [GOA01]
Cellular Component: GO:0031225 - anchored component of membrane Inferred from experiment [Aris85]
GO:0045263 - proton-transporting ATP synthase complex, coupling factor F(o) Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA01, Foster82]
GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, GOA06]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11]

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

Unification Links: DIP:DIP-35994N , EcoliWiki:b3736 , ModBase:P0ABA0 , PR:PRO_000022191 , Pride:P0ABA0 , Protein Model Portal:P0ABA0 , RefSeq:NP_418192 , SMR:P0ABA0 , String:511145.b3736 , UniProt:P0ABA0

Relationship Links: InterPro:IN-FAMILY:IPR002146 , InterPro:IN-FAMILY:IPR005864 , PDB:Structure:1B9U , PDB:Structure:1L2P , PDB:Structure:2KHK , Pfam:IN-FAMILY:PF00430

Summary:
The b subunit complex is involved in binding the F1 complex to the F0 complex and is necessary for the assembly of the F0 complex. Most of the subunit complex is exposed to the cytoplasm with only the short hydrophobic amino terminus embedded in the membrane [Porter85, DeckersHebestre92]. Results from cross-linking studies [Claggett09] and molecular modeling [Wise08, Hornung08] suggest that this subunit can stably exist as a left-handed coiled coil although results from other studies have not supported this [Zaida08].

A chimera approach has been used to investigate the tolerance of regions of the ATP synthase stator stalk to change, providing insight into the structural and sequential requirements for the function of this subunit [Bi08].

Small-angle X-ray scattering (SAXS) has determined the structure of the soluble domain of this subunit (b22-156) to low resolution [Priya08]. Fluorescence correlation spectroscopy (FCS) titration experiments have allowed assignment of the segments involved in δ-b assembly [Priya08].

Gene Citations: [Nielsen84, Jones83, Kasimoglu96]

Essentiality data for atpF knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol No 37 Aerobic 7.2 0.35 No [Joyce06]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 6]

Subunit of ATP synthase F0 complex: ATP synthase F0 complex - a subunit

Synonyms: UncB, PapD, AtpB, protein 6, chain A

Gene: atpB Accession Numbers: EG10099 (EcoCyc), b3738, ECK3731

Locations: inner membrane

Sequence Length: 271 AAs

Molecular Weight: 30.303 kD (from nucleotide sequence)

pI: 6.8

GO Terms:

Biological Process: GO:0042777 - plasma membrane ATP synthesis coupled proton transport Inferred from experiment Inferred by computational analysis [GOA06, Aris85, Cain89]
GO:0006754 - ATP biosynthetic process Inferred by computational analysis [UniProtGOA11]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11]
GO:0006811 - ion transport Inferred by computational analysis [UniProtGOA11]
GO:0015986 - ATP synthesis coupled proton transport Inferred by computational analysis [GOA01]
GO:0015992 - proton transport Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0046933 - proton-transporting ATP synthase activity, rotational mechanism Inferred from experiment Inferred by computational analysis [GOA06, Cain89, Aris85]
GO:0015078 - hydrogen ion transmembrane transporter activity Inferred by computational analysis [GOA01]
Cellular Component: GO:0005887 - integral component of plasma membrane Inferred from experiment [Valiyaveetil98, Long98, Wada99]
GO:0016021 - integral component of membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, Aris85]
GO:0045263 - proton-transporting ATP synthase complex, coupling factor F(o) Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA01, Aris85, Foster82]
GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, GOA06]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11]

MultiFun Terms: cell structure membrane
information transfer protein related chaperoning, repair (refolding)
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

Unification Links: DIP:DIP-47956N , EcoliWiki:b3738 , Mint:MINT-1300501 , ModBase:P0AB98 , PR:PRO_000022187 , Protein Model Portal:P0AB98 , RefSeq:NP_418194 , SMR:P0AB98 , String:511145.b3738 , UniProt:P0AB98

Relationship Links: InterPro:IN-FAMILY:IPR000568 , InterPro:IN-FAMILY:IPR023011 , Panther:IN-FAMILY:PTHR11410 , PDB:Structure:1C17 , Pfam:IN-FAMILY:PF00119 , Prints:IN-FAMILY:PR00123 , Prosite:IN-FAMILY:PS00449

Summary:
Subunit-a of the F0 complex is an integral membrane protein that plays a critical role in the proton translocation mechanism. Subunit-a is thought to provide aqueous access channels to and from the H+ binding site that is located in the decameric c-ring [Aris85, Cain89, Fillingame03, Angevine03, Steed08].

Subunit-a contains 5 transmembrane helices (TMH); the amino terminus is located in the periplasm and the carboxy terminus is located in the cytoplasm [Valiyaveetil98, Long98, Wada99]. Mutational and cross-linking studies indicate that transmembrane helices 2,3,4 and 5 form a four helix bundle that interacts with subunit c. pH-dependent conformational change of helices 4 and 5 has been implicated in the gating of H+ [Schwem06, Moore08, Moore08a, Moore13].

Structural divergence of the c-subunit ring and the a-subunits between bacterial species may allow development of species specific drugs which target these subunits [Maeda08].

Reviews: [DeckersHebestre92, Vik00, Vik05]

Citations: [Duser08, Lightowlers87, Hartzog93, Cain88, Paule89, Aksimentiev04, Long02, DeLeonRangel03, Zhang03d, Zhang03e, Vik94, Vik90, Vik98, Angevine07, Dong10]

Essentiality data for atpB 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 No 37 Aerobic 7.2 0.35 No [Joyce06]
MOPS medium with 0.4% glucose Indeterminate 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
No [Feist07, Comment 4]

Subunit of ATP synthase / thiamin triphosphate synthase: ATP synthase F1 complex

Summary:
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].


Subunit of ATP synthase F1 complex: ATP synthase F1 complex - epsilon subunit

Synonyms: UncC, PapG, AtpC

Gene: atpC Accession Numbers: EG10100 (EcoCyc), b3731, ECK3724

Locations: cytosol, inner membrane

Sequence Length: 139 AAs

Molecular Weight: 15.068 kD (from nucleotide sequence)

pI: 5.73

GO Terms:

Biological Process: GO:0006754 - ATP biosynthetic process Inferred by computational analysis [UniProtGOA11]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11]
GO:0006811 - ion transport Inferred by computational analysis [UniProtGOA11]
GO:0015986 - ATP synthesis coupled proton transport Inferred by computational analysis [GOA01]
GO:0015992 - proton transport Inferred by computational analysis [UniProtGOA11]
GO:0042777 - plasma membrane ATP synthesis coupled proton transport Inferred by computational analysis [GOA06]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Hauser14, Rajagopala14, Butland05]
GO:0046933 - proton-transporting ATP synthase activity, rotational mechanism Inferred from experiment Inferred by computational analysis [GOA06, GOA01, Klionsky84]
GO:0005524 - ATP binding Inferred by computational analysis [GOA06]
GO:0046961 - proton-transporting ATPase activity, rotational mechanism Inferred by computational analysis [GOA01]
Cellular Component: GO:0045261 - proton-transporting ATP synthase complex, catalytic core F(1) Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA01, Klionsky84]
GO:0005829 - cytosol
GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, GOA06]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11]

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

Unification Links: DIP:DIP-47828N , EcoliWiki:b3731 , PR:PRO_000022188 , Pride:P0A6E6 , Protein Model Portal:P0A6E6 , RefSeq:NP_418187 , SMR:P0A6E6 , String:511145.b3731 , UniProt:P0A6E6

Relationship Links: InterPro:IN-FAMILY:IPR001469 , InterPro:IN-FAMILY:IPR020546 , InterPro:IN-FAMILY:IPR020547 , Panther:IN-FAMILY:PTHR13822 , PDB:Structure:1AQT , PDB:Structure:1BSH , PDB:Structure:1BSN , PDB:Structure:1FS0 , PDB:Structure:1QO1 , PDB:Structure:3OAA , Pfam:IN-FAMILY:PF00401 , Pfam:IN-FAMILY:PF02823 , ProDom:IN-FAMILY:PD000944

Summary:
The epsilon subunit appears to play an important role in coupling the catalytic site events with proton translocation in association with the gamma subunit. The coupling involves conformational changes and probable translocations of one or both subunits. This subunit is also required for binding of the F1 complex to the F0 complex. [Tang96, Senior90]

Citations: [Iino09]

Essentiality data for atpC knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol No 37 Aerobic 7.2 0.35 No [Joyce06]
MOPS medium with 0.4% glucose Indeterminate 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
No [Feist07, Comment 4]

Subunit of ATP synthase F1 complex: ATP synthase F1 complex - delta subunit

Synonyms: UncH, PapE, AtpH

Gene: atpH Accession Numbers: EG10105 (EcoCyc), b3735, ECK3728

Locations: cytosol, inner membrane

Sequence Length: 177 AAs

Molecular Weight: 19.332 kD (from nucleotide sequence)

pI: 5.11

GO Terms:

Biological Process: GO:0006754 - ATP biosynthetic process Inferred by computational analysis [UniProtGOA11]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11]
GO:0006811 - ion transport Inferred by computational analysis [UniProtGOA11]
GO:0015986 - ATP synthesis coupled proton transport Inferred by computational analysis [GOA01]
GO:0015992 - proton transport Inferred by computational analysis [UniProtGOA11]
GO:0042777 - plasma membrane ATP synthesis coupled proton transport Inferred by computational analysis [GOA06]
Molecular Function: GO:0046933 - proton-transporting ATP synthase activity, rotational mechanism Inferred from experiment Inferred by computational analysis [GOA06, GOA01, Humbert83]
GO:0046961 - proton-transporting ATPase activity, rotational mechanism Inferred from experiment [Humbert83]
Cellular Component: GO:0045261 - proton-transporting ATP synthase complex, catalytic core F(1) Inferred from experiment Inferred by computational analysis [UniProtGOA11, Humbert83]
GO:0005829 - cytosol
GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, GOA06]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11, GOA01]

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

Unification Links: DIP:DIP-47921N , EcoliWiki:b3735 , ModBase:P0ABA4 , PR:PRO_000022193 , Pride:P0ABA4 , Protein Model Portal:P0ABA4 , RefSeq:NP_418191 , SMR:P0ABA4 , String:511145.b3735 , UniProt:P0ABA4

Relationship Links: InterPro:IN-FAMILY:IPR000711 , InterPro:IN-FAMILY:IPR020781 , InterPro:IN-FAMILY:IPR026015 , Panther:IN-FAMILY:PTHR11910 , PDB:Structure:1ABV , PDB:Structure:2A7U , Pfam:IN-FAMILY:PF00213 , Prints:IN-FAMILY:PR00125 , Prosite:IN-FAMILY:PS00389

Summary:
The delta subunit is required for binding the F1 complex to the F0 complex. It may also block proton conduction through the F0 complex. [Engelbrecht90, Xiao94]

Essentiality data for atpH knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol No 37 Aerobic 7.2 0.35 No [Joyce06]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 6]

Subunit of ATP synthase F1 complex: ATP synthase F1 complex - alpha subunit

Synonyms: papA, uncA

Gene: atpA Accession Numbers: EG10098 (EcoCyc), b3734, ECK3727

Locations: cytosol, inner membrane

Subunit composition of ATP synthase F1 complex - alpha subunit = [AtpA]3
         ATP synthase F1 complex - alpha subunit = AtpA

Map Position: [3,916,339 <- 3,917,880] (84.41 centisomes)
Length: 1542 bp / 513 aa

Molecular Weight of Polypeptide: 55.222 kD (from nucleotide sequence)

pI: 6.16

GO Terms:

Biological Process: GO:0015986 - ATP synthesis coupled proton transport Inferred from experiment Inferred by computational analysis [GOA01, Butlin71]
GO:0006754 - ATP biosynthetic process Inferred by computational analysis [UniProtGOA11]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11]
GO:0006811 - ion transport Inferred by computational analysis [UniProtGOA11]
GO:0015991 - ATP hydrolysis coupled proton transport Inferred by computational analysis [GOA01]
GO:0015992 - proton transport Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0042777 - plasma membrane ATP synthesis coupled proton transport Inferred by computational analysis [GOA06]
GO:0046034 - ATP metabolic process Inferred by computational analysis [GOA01]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Huang06, Lasserre06, Arifuzzaman06, Stenberg05, Butland05]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11, GOA06, GOA01]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11]
GO:0016820 - hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances Inferred by computational analysis [GOA01]
GO:0046933 - proton-transporting ATP synthase activity, rotational mechanism Inferred by computational analysis [GOA06, GOA01]
GO:0046961 - proton-transporting ATPase activity, rotational mechanism Inferred by computational analysis [GOA01]
Cellular Component: GO:0016020 - membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, Lasserre06]
GO:0045261 - proton-transporting ATP synthase complex, catalytic core F(1) Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA01, Kanazawa78]
GO:0005829 - cytosol
GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, GOA06]
GO:0033178 - proton-transporting two-sector ATPase complex, catalytic domain Inferred by computational analysis [GOA01]

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

Unification Links: DIP:DIP-31845N , EcoliWiki:b3734 , Mint:MINT-1251537 , ModBase:P0ABB0 , PR:PRO_000022186 , Pride:P0ABB0 , Protein Model Portal:P0ABB0 , RefSeq:NP_418190 , SMR:P0ABB0 , String:511145.b3734 , Swiss-Model:P0ABB0 , UniProt:P0ABB0

Relationship Links: InterPro:IN-FAMILY:IPR000194 , InterPro:IN-FAMILY:IPR000793 , InterPro:IN-FAMILY:IPR004100 , InterPro:IN-FAMILY:IPR005294 , InterPro:IN-FAMILY:IPR018538 , InterPro:IN-FAMILY:IPR020003 , InterPro:IN-FAMILY:IPR023366 , InterPro:IN-FAMILY:IPR027417 , Panther:IN-FAMILY:PTHR15184:SF3 , PDB:Structure:1D8S , PDB:Structure:3OAA , Pfam:IN-FAMILY:PF00006 , Pfam:IN-FAMILY:PF00306 , Pfam:IN-FAMILY:PF09378 , Prosite:IN-FAMILY:PS00152

Summary:
The α-subunit plays an essential role in the catalytic mechanism of the enzyme and in the binding and coupling between the F1 and F0 complexes. The α-subunit also contains an adenine-specific binding site which is noncatalytic, nonregulatory and not essential for enzyme assembly in vitro. Its function has not yet been determined. The α-subunit complex is a homotrimer [Rao88].

A hydrogen-bonding network is formed at the closed α/β-subunit interface of F1 [Abrahams94]. Elimination of this network results in a severely impaired enzyme. A possible role for the hydrogen-bonding network in coupling of ATP synthesis/hydrolysis and rotation has been proposed [Mao08]. The role of conserved residues surrounding the catalytic site has been studied [Li09a].

Citations: [Salcedo14]

Gene Citations: [Nielsen84, Jones83, Kasimoglu96]

Essentiality data for atpA 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 No 37 Aerobic 7.2 0.35 No [Joyce06]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 6]

Subunit of ATP synthase F1 complex: ATP synthase F1 complex - gamma subunit

Synonyms: UncG, PapC, AtpG

Gene: atpG Accession Numbers: EG10104 (EcoCyc), b3733, ECK3726

Locations: cytosol, inner membrane

Sequence Length: 287 AAs

Molecular Weight: 31.577 kD (from nucleotide sequence)

pI: 8.96

GO Terms:

Biological Process: GO:0006754 - ATP biosynthetic process Inferred by computational analysis [UniProtGOA11]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11]
GO:0006811 - ion transport Inferred by computational analysis [UniProtGOA11]
GO:0015986 - ATP synthesis coupled proton transport Inferred by computational analysis [GOA01]
GO:0015992 - proton transport Inferred by computational analysis [UniProtGOA11]
GO:0042777 - plasma membrane ATP synthesis coupled proton transport Inferred by computational analysis [GOA06]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Hauser14, Rajagopala14, Butland05]
GO:0046933 - proton-transporting ATP synthase activity, rotational mechanism Inferred from experiment Inferred by computational analysis [GOA06, GOA01, Futai77]
GO:0046961 - proton-transporting ATPase activity, rotational mechanism Inferred from experiment Inferred by computational analysis [GOA01, Futai77]
GO:0005524 - ATP binding Inferred by computational analysis [GOA06]
Cellular Component: GO:0016020 - membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, Lasserre06]
GO:0045261 - proton-transporting ATP synthase complex, catalytic core F(1) Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA01, Klionsky85]
GO:0005829 - cytosol
GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, GOA06]

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

Unification Links: DIP:DIP-35938N , EcoliWiki:b3733 , ModBase:P0ABA6 , PR:PRO_000022192 , Pride:P0ABA6 , Protein Model Portal:P0ABA6 , RefSeq:NP_418189 , SMR:P0ABA6 , String:511145.b3733 , UniProt:P0ABA6

Relationship Links: InterPro:IN-FAMILY:IPR000131 , InterPro:IN-FAMILY:IPR023632 , InterPro:IN-FAMILY:IPR023633 , Panther:IN-FAMILY:PTHR11693 , PDB:Structure:1D8S , PDB:Structure:1FS0 , PDB:Structure:3OAA , Pfam:IN-FAMILY:PF00231 , Prints:IN-FAMILY:PR00126 , Prosite:IN-FAMILY:PS00153

Summary:
The gamma subunit appears to play an important role in coupling the catalytic site events with proton translocation in association with the epsilon subunit. The coupling involves conformational changes and probable translocations of one or both subunits [Tang96].

The rate limiting rotation step carried out by this subunit has been investigated and residues involved in this rotation process have been identified [Scanlon08].

ArcA appears to repress atpG gene expression under anaerobiosis. Two putative ArcA binding sites were identified upstream of this gene [Salmon05], but no promoter upstream of it has been identified. Instead, atpG is transcribed from three promoters: one of them is located usptream of atpI gene and the others are located upstream of atpB gene.

Essentiality data for atpG 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 No 37 Aerobic 7.2 0.35 No [Joyce06]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 6]

Subunit of ATP synthase F1 complex: ATP synthase F1 complex - beta subunit

Synonyms: papB, uncD

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

Locations: cytosol, inner membrane

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

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

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

pI: 5.1

GO Terms:

Biological Process: GO:0006754 - ATP biosynthetic process Inferred by computational analysis [UniProtGOA11]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11]
GO:0006811 - ion transport Inferred by computational analysis [UniProtGOA11]
GO:0015986 - ATP synthesis coupled proton transport Inferred by computational analysis [GOA01]
GO:0015991 - ATP hydrolysis coupled proton transport Inferred by computational analysis [GOA01]
GO:0015992 - proton transport Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0042777 - plasma membrane ATP synthesis coupled proton transport Inferred by computational analysis [GOA06]
GO:0046034 - ATP metabolic process Inferred by computational analysis [GOA01]
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 [UniProtGOA11]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11, GOA06, GOA01]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11]
GO:0016820 - hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances Inferred by computational analysis [GOA01]
GO:0046933 - proton-transporting ATP synthase activity, rotational mechanism Inferred by computational analysis [GOA06, GOA01]
Cellular Component: GO:0016020 - membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, Lasserre06]
GO:0045261 - proton-transporting ATP synthase complex, catalytic core F(1) Inferred from experiment Inferred by computational analysis [UniProtGOA11, Senior79]
GO:0005829 - cytosol
GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, GOA06]
GO:0033178 - proton-transporting two-sector ATPase complex, catalytic domain Inferred by computational analysis [GOA01]

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

Unification Links: DIP:DIP-31846N , EcoliWiki:b3732 , Mint:MINT-1251407 , PR:PRO_000022189 , Pride:P0ABB4 , Protein Model Portal:P0ABB4 , RefSeq:NP_418188 , 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

Summary:
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 [Li09a].

Gene Citations: [Nielsen84, Jones83, Kasimoglu96]

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 6]

References

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Mao08: Mao HZ, Abraham CG, Krishnakumar AM, Weber J (2008). "A functionally important hydrogen-bonding network at the betaDP/alphaDP interface of ATP synthase." J Biol Chem 283(36);24781-8. PMID: 18579516

Moore08: Moore KJ, Fillingame RH (2008). "Structural interactions between transmembrane helices 4 and 5 of subunit a and the subunit c ring of Escherichia coli ATP synthase." J Biol Chem 283(46);31726-35. PMID: 18786930

Moore08a: Moore KJ, Angevine CM, Vincent OD, Schwem BE, Fillingame RH (2008). "The cytoplasmic loops of subunit a of Escherichia coli ATP synthase may participate in the proton translocating mechanism." J Biol Chem 283(19);13044-52. PMID: 18337242

Moore13: Moore KJ, Fillingame RH (2013). "Obstruction of transmembrane helical movements in subunit a blocks proton pumping by F1Fo ATP synthase." J Biol Chem 288(35);25535-41. PMID: 23864659

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

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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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