UniProt ID stringlengths 6 10 | Protein Sequence stringlengths 2 35.2k | Functional Description stringlengths 5 30.7k |
|---|---|---|
P45822 | MDELNIEIVAVDRKIWSGKGTFLFTRTTAGEIGILPRHIPMVAQLVDDNMVRIEREGEKDLRVAVDGGFLSVTEERVSILAESAEFDSEIDENAAKQDAESDDPRIAARGRARLRAVGAID | Produces ATP from ADP in the presence of a proton gradient across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase epsilon chain family. |
B2HQK1 | MAELNVEIVAVDRKIWSGAGTFLFTRTTVGEIGILPNHIPLVAQLVDDAMVRVERDGDKDLRIAVDGGFMSVTDAGVSILAESAEFESEIDEAVARQDSESDDPRTAARGRARLRAVGAID | Produces ATP from ADP in the presence of a proton gradient across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase epsilon chain family. |
Q57HY0 | MAMTYHLDVVSAEQQMFSGLVEKIQVTGSEGELGIYPGHAPLLTAIKPGMIRIVKQHGHEEFIYLSGGILEVQPGSVTVLADTAIRGQDLDEARALEAKRKAEEHIKSSHGDVDYAQASAELAKAIAKLRVIELTKKAM | Produces ATP from ADP in the presence of a proton gradient across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase epsilon chain family. |
B5QUS3 | MAMTYHLDVVSAEQQMFSGLVEKIQVTGSEGELGIYPGHAPLLTAIKPGMIRIVKQHGHEEFIYLSGGILEVQPGSVTVLADTAIRGQDLDEARALEAKRKAEEHIKSSHGDVDYAQASAELAKAIAKLRVIELTKKAM | Produces ATP from ADP in the presence of a proton gradient across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase epsilon chain family. |
B5RFW4 | MAMTYHLDVVSAEQQMFSGLVEKIQVTGSEGELGIYPGHAPLLTAIKPGMIRIVKQHGHEEFIYLSGGILEVQPGSVTVLADTAIRGQDLDEARALEAKRKAEEHIKSSHGDVDYAQASAELAKAIAKLRVIELTKKAM | Produces ATP from ADP in the presence of a proton gradient across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase epsilon chain family. |
B4SYD0 | MAMTYHLDVVSAEQQMFSGLVEKIQVTGSEGELGIYPGHAPLLTAIKPGMIRIVKQHGHEEFIYLSGGILEVQPGSVTVLADTAIRGQDLDEARALEAKRKAEEHIKSSHGDVDYAQASAELAKAIAKLRVIELTKKAM | Produces ATP from ADP in the presence of a proton gradient across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase epsilon chain family. |
Q5PKX3 | MAMTYHLDVVSAEQQMFSGLVEKIQVTGSEGELGIYPGHAPLLTAIKPGMIRIVKQHGHEEFIYLSGGILEVQPGSVTVLADTAIRGQDLDEARALEAKRKAEEHIKSSHGDVDYAQASAELAKAIAKLRVIELTKKAM | Produces ATP from ADP in the presence of a proton gradient across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase epsilon chain family. |
C0Q2N1 | MAMTYHLDVVSAEQQMFSGLVEKIQVTGSEGELGIYPGHAPLLTAIKPGMIRIVKQHGHEEFIYLSGGILEVQPGSVTVLADTAIRGQDLDEARALEAKRKAEEHIKSSHGDVDYAQASAELAKAIAKLRVIELTKKAM | Produces ATP from ADP in the presence of a proton gradient across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase epsilon chain family. |
B5BIN5 | MAMTYHLDVVSAEQQMFSGLVEKIQVTGSEGELGIYPGHAPLLTAIKPGMIRIVKQHGHEEFIYLSGGILEVQPGSVTVLADTAIRGQDLDEARALEAKRKAEEHIKSSHGDVDYAQASAELAKAIAKLRVIELTKKAM | Produces ATP from ADP in the presence of a proton gradient across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase epsilon chain family. |
Q2RZV2 | MADELTVDIVTPDERSFQGPANGVRAPGIEGSFEVREDHAPMIAAFGIGPLIVKTQAAHEYADMHNDRIIFATSGGFLEVIDNKVTVLAETVEPASEIDVERAESAEERAKRRLEEGVQEEERETHEAARDRARNRLRVAMGKVGTRQS | Produces ATP from ADP in the presence of a proton gradient across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase epsilon chain family. |
Q9RFL2 | MAMTYHLDVVSAEQQMFSGLVEKIQVTGSEGELGIYPGHAPLLTAIKPGMIRIVKQHGHEEFIYLSGGILEVQPGSVTVLADTAIRGQDLDEARALEAKRKAEEHIKSSHGDVDYAQASAELAKAIAKLRVIELTKKAM | Produces ATP from ADP in the presence of a proton gradient across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase epsilon chain family. |
A8G7M9 | MAMTYHLDVVSAEKHMFSGLVQKIQVTGSEGELGIFPGHAPLLTAIKPGMVRIVKQHGEEEFIYLSGGILEVQPSVVTVLADTAIRGTDLDEARALEAKRKAEEHISSSHGDVDYAQASAELAKAIAKLRVIELTRRSM | Produces ATP from ADP in the presence of a proton gradient across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase epsilon chain family. |
B8EDU9 | MAAMTVHLDIVSAESKIFSGRVASLQVTGSEGELGIMHGHAPLLSYIKPGMARIVKQDGSEEVFYLSGGILEVQPSTVSVLADVVMRAKDIDEQAALEAKRRAEAHMANAGADFNYDAAMVELAKAMAQLRVVETIKKNIAR | Produces ATP from ADP in the presence of a proton gradient across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase epsilon chain family. |
A3DAR3 | MAAMTVHLDIVSAESKIFSGRVVSLQVTGSEGELGIMHGHAPLLSYIKPGMARIVKQDGSEEVFYLSGGILEVQPSTVSVLADVVMRAKDIDEQAALEAKRRAEAHMANAGADFNYDAAMVELAKAMAQLRVVETIKKNIAR | Produces ATP from ADP in the presence of a proton gradient across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase epsilon chain family. |
A6WUI9 | MAAMTVHLDIVSAESKIFSGRVASLQVTGSEGELGIMHGHAPLLSYIKPGMARIVKQDGSEEVFYLSGGILEVQPSTVSVLADVVMRAKDIDEQAALEAKRRAEAHMANAGADFNYDAAMVELAKAMAQLRVVETIKKNIAR | Produces ATP from ADP in the presence of a proton gradient across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase epsilon chain family. |
A9KX05 | MAAMTVHLDIVSAESKIFSGRVASLQVTGSEGELGIMHGHAPLLSYIKPGMARIVKQDGSEEVFYLSGGILEVQPSTVSVLADVVMRAKDIDEQAALEAKRRAEAHMANAGADFNYDAAMVELAKAMAQLRVVETIKKNIAR | Produces ATP from ADP in the presence of a proton gradient across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase epsilon chain family. |
Q12HQ2 | MAAMTVQLDIVSAEGGIYSGRVSHLQVTGSEGELGIMHGHAPLISKIKPGMARVTKQDGSEEVFYLSGGILEVQPASTSILADVVLRADDIDEKAAIEAKNRAEAHMVDAGSDFDYQAALIEIAKATAQLRVLETIKKNIAR | Produces ATP from ADP in the presence of a proton gradient across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase epsilon chain family. |
Q07VU5 | MAAKTVQLDIVSAENSIFHGQVSFLEVNGAEGELGIMPNHVALLTKIKPGMARFIKQDGSEEVLYLSGGLLEVQPTAISVLADVALRADDIDEKAALEAKERAEQAIANAGTDFNYEAATIELAKSLAQLRVVECIKKNITR | Produces ATP from ADP in the presence of a proton gradient across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase epsilon chain family. |
B0TQF3 | MAAMTVQLDMVSAESNIFSGRVAQLQVSGTEGELGIMPGHAALLTSIKPGMARIVKQDGSEEVFYLSGGILEVQPSSISVLADVVLRAEEIDEQAAVEAKRRAEAHMANAGADFNYAAAAIELAQAIAQLRVVETIKKNISR | Produces ATP from ADP in the presence of a proton gradient across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase epsilon chain family. |
A3QJQ9 | MAAMTVQLDIVSAESSIFSGLVAHLQVSGAEGDLGVMPGHAPLLTHIKPGMARIVKQDGKEEVFYLSGGILEVQPFSVSVLADVVLRAEEIDEQAAVEAKRRAEAHMANAGADFNYAAAAIELAQAIAQLRVVETIKKNIAR | Produces ATP from ADP in the presence of a proton gradient across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase epsilon chain family. |
Q8E8C1 | MAAMTVQLDIVSAESSIFSGRVASLQVTGSEGELGIMHGHAPLLSYIKPGMARIVKQDGNEEVFYLSGGLLEVQPSSVSVLADVVMRAKDIDEQAALEAKRRAEAHMATAGADFNYDAAMVELAKAMAQLRVVETIKKNIAR | Produces ATP from ADP in the presence of a proton gradient across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Belongs to the ATPase epsilon chain family. |
Q2IRA3 | MAIFAEAETWVAIAFVILMGIFAYLGVHRTVLKALDNRRDRIKAELDEARKLKDEAAKLLADYRARRAQAEREAEAIVASAKADAERIAAESKAKLEDFVVRRTKTAESKIALAEAQALADVRAAAAEAAVSAAAIVLSQSVKGQVADDLLGKGIQEVRSKLN | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
Q07H89 | MIELLSAAETWVAVGFAILMVVFVYFGVHRTVLNALDNRRDRIKAELDEASRLKEEAAKLLADYKARAASAEREAEAIIASAKDEAERIAAEAKAKLEDFVARRTKTAEGKIAMAEAQAIADVRAAAANAAVAAASSILSQSVKGSVADELIGKGIAEVRSKLN | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
Q6NBI5 | MAIFGEAETWVAIAFVILLGVFAYLGVHRTVLQALDKRRDRIKAELDEARKLKDEAAKLLADYRARRASAEREAQAIVDSAKADAERIAAEAKAKLEDFVARRTKTAESKIALAEAQALADVRAAAAEAAVAAASRILSESVKGNLADELLSKGIQEVRGKLN | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
Q20X01 | MTGILAEPETWVAVAFVILMGVFAYFGVHRTVLKSLDNRRDRIKAELDEAARLKEEAAALLAEYKARRASAEREAQEIIAGAKDEAERIAAEAKAKLEDFVARRTKTAEGKIALAEAQAVADVRSAAANAAVAAASTILSQSVKGQVAEGLLQRGIEEVRSKLN | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
Q13CX4 | MGIFAEAETWVAVAFVILMALFAYLGVHRTVLQALDNRRARIKAELDEARKLKDEAAKLLADYRARRAQAEREAEAIISSAKADAERIAAESKAKLEDFVARRTKTAESKIALAEAQAVADVRAAAAEAAVSAAATILSQSVKGQVADDLLGKGIQEVRSKLN | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
B3QF34 | MAIFGEAETWVAIAFVILLGVFAYLGVHRTVLQALDKRRDRIKAELDEARKLKDEAAKLLADYRARRASAEREAQAIVDSAKADAERIAAEAKAKLEDFVARRTKTAESKIALAEAQALADVRAAAAEAAVAAASRILSESVKGNLADELLSKGIQEVRGKLN | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
Q2RPA7 | MISLALAAETAEHGGEAASHGGLFADPAFWVSIAFLMVVGFVYIKAKNKILGALDGRGAAVKAKLDEARKLRDDAQALLAEYQRRQRDAMKEADEIIRHAKDEAARLRAKAEADLEASIRRREQQAVDRIAQAEAQALAQVRNEAVDVAVSAARSLMAGSLAKADQNRLIDAAIADLPGKLH | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
Q16AM5 | MRNLSRLSVLALAMLAANPAFAAGGGISLKNTDFVVLLGLLVFIGILVYFKVPGMIGKMLDSRAEGIEAELNEARALREEAQSLLASYERKQREVQEQADRIVEAAKEEATIAAEQARADLEVSLARRMAAAEDQIASAQAAAIKEVRDQSVSIAIAAAQDVIAKQLTAADANALIDGAITEVEAKLH | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
Q1GDE3 | MRATLAIALTLATTSPAFAAGGGWNLGNTDFVVILAFLLFIGILLAAKVPSLIGKQLDNRADSIKSELEEARALREEAQTLLASYERKQQDVQAQAERIVANARDEAAAAAEQAKADLAASIARRLTAAEEQIASAEASAVKEVRDRAITIAVEVADQVISKQMTAADANKLIDAAIQDVEAKLH | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
A6U6M7 | MALDATFYALVGLILFFVLIAYLKVPGMVGKALDARADKISNELAEAKRLREEAQSLVAEYQRKRKDAEAEAASIVAAAQREAEMLTAEAKQKTEEFVARRTALSEQKIKQAESDAINAVRAAAVDLAISAAEKVIASKADASAQETLFQKALGEVKSRLN | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
Q2LQZ9 | MKKSVWHHSLKGYCGRIAAVLCFSVLVPLVAMAAEGGGHGEEGTDWVNFGWRVLDFIILVGLFYWLLASKVKSFFSGRREEIKTTLEEARLAKEAAEHKFKEYSEKLDKASKEIEGVYEMIRAQGQAEKEKILEDARKAAAKMKEDTQARIEQELKKASQQLRMEAVQLSVHVAEDILKRNITPEDHQSMVKDYLDKVVRKH | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
Q39ZT7 | MSRHSRRMRILCLCATTLLMAGSALASEAGGHADGQLKDFLYRLLDFGITFGALYFLLRGPLKRALSARRQRVAEALEQARQMQASAERRFAACRQQLADADAQIAQLTADLKAESALQCQRIEEQARKMADDIRSEATRSAAREIEAARKQLHQEAVRLAMELAEQRLKQQIAPQDQARLVDEYLRKTGE | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
B1XHZ0 | MGIISYLATASEGGFHLNFDILETNIINLAIIIGVLYVYGSKFIGNILETRKSKIVADLEDAENRAKKAQEALTKAQKDLEQAQAQAAKIREDAKVAAEKTKQDILAKGRDEVEKLKASAVKELSTEQAKVITELKRRVAELALAKVEAQLRSDLDESAQAKLVDRSIAQLGGGA | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has four main subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta, b and b' chains. Belongs to the ATPase B chain family. |
A7N0Y5 | MNINATLLGQAISFALFVWFCMKYVWPPLMQAIEERQKKIADGLQAAERAAKDLDLAQANASDQMKEAKRTATEIIDQANKRKSQIIDEAREEAQAERQKILAQAEAELEAERNRARDELRKQVATLAVAGAEKILERTIDKDAQKDILDNITAKL | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
A7IGS7 | MNEMSLAELWVAVAFLLFVGILIYVGAHRAIGSALDSRGQRIAAELEEARRLKEEAQKLVAEFKRKQREAEAEAESIVTAAKAEAERLASEAKAKLEDFVTRRTKMAEDKIAQAELQAVADVKAIAADAAAKAAEVLLGSAARGDVGDRLISNAIGEVKTKLN | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
Q66JD1 | MAAAVVQMSMGYRGLLAVRNRGTGPLALGVVSSQLRAFSVRKEPELDENPYYGKYRDKIQQLRRTNPSAFDARLDKRKELKQQPLGYSKQAEFAKTVEEKVGTASGKGFSKNKTLDSILNIELIKDKDADEIREIWKQYFSLRNSVYAVIPGESFELIWRRAKTCPSFLYALPRKEGYEFFVGQWSGSELHFTALINIQTAGDAAPSQLILYHYPEFQKDKGIVLMTSEIDTKFLNVQDAQCLANQVQLFYGSDGAETFGLVEKFNHKSDEFKYMAVVSFLEQSGLGKSFLNEQGHNKEDKLE | May play an essential role for the assembly of the mitochondrial F1-F0 complex. Belongs to the ATP11 family. |
B0BZK9 | MFDFNGTLPLMMFQFFLLVAVLNAVFFKPLTQAIDERDGFIRTNNTEARERLAKAKSLTEQYEQELAGTRKQSQQVLADAQAEAQKIAQTQITEAQKQVQAEVMKAQAELESQKQSAFSELEKQVDTLSQQILNKLLGSTLA | 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). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has four main subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta, b and b' chains. Belongs to the ATPase B chain family. |
A5FVI8 | MRRTTILLAATALGLTPAIAMAEGKMPQMDFSNPLTGAQVVWMAVIMVVLYFVLARWALPRIGGVIENRHNRIATDLETARRAKAEAEHAVRELNLAIQNARESSQGAIAEAVNAAKERARAQTAALNDRLSAQIASAEAEIDSARRTAVGALAPIARDVASSLLQRLIGEAVEPGRIEQAVSALSTQG | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
F8BSK0 | MAESHATGTTTHTEVPHGKPEFPPFNKDTFASQLVSFAIAFALLYVIVSRFALPRVGGVIKTREGTIEKDLAEAQAFRDESDLALKAYETELAAARTRAQAIGSETRDTLAAQSDAERKAVELSLSAKLAEAEKTISDMRTKAMGNVKAIAADATSAIVQQLSGTAPDAQLIDRAVDASLKGGRDAA | 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 (By similarity). Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria (By similarity). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains (By similarity). Belongs to the ATPase B chain family. |
Q7D0U9 | MFVTEAYAQSAPTVGETHTETPAVGQPQPEATHTETGVAHGAEHGASGVFPPFDQSTYASQVLWLAITFGLFYLLMQKVIVPRVGGILENRHGRIAQDLDEAARLKAEADTAVETYEKELAAARAKASSIGASARDAAKAKADADRAAIEAGLAEKLAAAEKRIAGIRDHAFADVGAIAEETATAIVDQLVGAKVKDTDVKAAIAAASAVKGA | 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 (By similarity). Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria (By similarity). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains (By similarity). Belongs to the ATPase B chain family. |
A0PUK3 | MSTFIGQLVGFAAIVFLVWRYVVPPVRRMMAARQDTVRQQLADAATAAVRLTESTTAHSKAVEAAKAEAEQVVAEAKEEAKRITAQMQTQAGVEAERIKVQGSRQVELLRTQLTRQLRLELGHESVRQASELVRNHVSDPGQQAATVDRFLDELDAMAPAAAEVERPVAAKMRSASRRALGSLVDKFAGLAKGLDNAALSALASGLVSVAQLLQREVIVTRYLTVPAEDAAPRIRLLERLISGQVGNPALDILRAAVTERWSASSDLIDAIEHVSRQALLEVAQRDGQVDEVEDQLFRFSRILDAQPRLSILLGDYVVPAEGRVGLLRKVLDSAGSVNPIAVALLSQTVELLRGQPAEEAALLLAEVAVARRGEVVAQVSAAAELSDAQRTRVTEVLSRIYGHPVTVQLQTDPTLLGGLSIAVGDEVIDGTLSSRLTAAEAQLPD | 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 (By similarity). This fusion protein includes a component of the F(0) channel (subunit b) and of the F(1) subunit (subunit delta). Two copies of subunit b and one of delta together form the peripheral 'stator' stalk which links F(1) to F(0) (By similarity). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains (By similarity). In the N-terminal section; belongs to the ATPase B chain family. In the C-terminal section; belongs to the ATPase delta chain family. |
A1TD58 | MSIFIGQLIGFAVIVFILVKWVVPPIKGLMQKQQEAVRVALAESAEAGKKLADADAMHAKAVEDAKAAGAKVTEEAQQDSQRITAQLAEQADAEAERIKAQGAQQVQLMRQQLIRQLRSGLGSESVQKAEEIVRNYVSDPAAQASTVDRFLDELDAMAPSSAVLEAGASLNLRAASREALAELVKKFESVAESADTAALATLADNLSAVARLLLTSATLDKHLAEPTGDSAAKVRLLERLFGGKVDDNTMDLLKTAVAQRWSTEGNLIDAVEHVARLALLVRAEREGQSEEVEDQLFRFGRVLDAQSQLSRLLADPVIPADKRVALLKKVLDSGGGVNPIAEALLTQTVELIRGASADDAVNDLAELAVARRGEAVAQVTAAADLSDAQRTRLTEVLSRIYGTPVSIQLEVDPEVLGGLLITVGDEVIDGSISSRLAAARTGLPD | 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 (By similarity). This fusion protein includes a component of the F(0) channel (subunit b) and of the F(1) subunit (subunit delta). Two copies of subunit b and one of delta together form the peripheral 'stator' stalk which links F(1) to F(0) (By similarity). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains (By similarity). In the N-terminal section; belongs to the ATPase B chain family. In the C-terminal section; belongs to the ATPase delta chain family. |
A3DIM5 | MLQENFVSCSKEREVQLAVLSEFIHIPTFIYTALNLVILYFILKRLLFKPVWEFMENRKNSIAESMEKAEKGKAEALELKNKYESELNEAYAKAQKILKEAEEKAKQEYERIIRDAKNEAEALKLKAKEEIEREKNEALKEIRNEVVSLALEAASKVLEANMDTEENRKLVNRFIDEQGVA | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
A9NGW6 | MDIFKEISDAIQEGLNSIFERWDLVLWQIAATVILIIVVRIFLWKPITRYLEQRQEALSKELHEAAHERERVAQIRYELQTEYEVMRKEARQMKDTLMSEAQLEKERIISDARNEAKRRIQQVDRDVQQELRLQSEKIRENIKNIAFDVAEKIVSHQVTDENIDEVIDEMLDEKL | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
A1TJ37 | MSINATLFVQAIVFLILVLFTMKFVWPPIAKALDERAQKIAEGLAAADRAKSELVAVNQRVETELAQTRNETASRLADAERRAQAIIEEAKARATEEGNKIVAAARAEAEQQTIQAREALREQVAALAVKGAEQILRKEVNAGVHADLLNRLKTEL | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
Q6FFK4 | MNINLTLIGQAIAFAIFVAFCMKFVWPPLINAISERQRKIADGLNAAEKAKADLADAQAQVKQELDAAKAQAAQLIEQANRRAAQLIEEARTQATAEGERIRQQSKETVDQEINAAREELRQQVAALAVDGAEKILNQQVDQQAHAAMLEQLAAKL | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
B7H298 | MNINLTLIGQAIAFAFFVAFCMKFVWPPLINAISERQRKIADGLNAAEKAKADLADAQAQVKQELDAAKAQAAQLIEQANRRAAQLIEEARTQAAAEGERIRQQAKEAVDQEINSAREELRQQVAALAVTGAEKILNQQVDAEAHNAMLSQLAAKL | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
B7I1W0 | MNINLTLIGQAIAFAFFVAFCMKFVWPPLINAISERQRKIADGLNAAEKAKADLADAQAQVKQELDAAKAQAAQLIEQANRRAAQLIEEARTQAAAEGERIRQQAKEAVDQEINSAREELRQQVAALAVTGAEKILNQQVDAEAHNAMLSQLAAKL | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
B2I0Z8 | MNINLTLIGQAIAFAFFVAFCMKFVWPPLINAISERQRKIADGLNAAEKAKADLADAQAQVKQELDAAKAQAAQLIEQANRRAAQLIEEARTQAAAEGERIRQQAKEAVDQEINSAREELRQQVAALAVTGAEKILNQQVDAEAHNAMLSQLAAKL | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
B0VNK0 | MNINLTLIGQAIAFAFFVAFCMKFVWPPLINAISERQRKIADGLNAAEKAKADLADAQAQVKQELDAAKAQAAQLIEQANRRAAQLIEEARTQAAAEGERIRQQAKEAVDQEINSAREELRQQVAALVVTGAEKILNQQVDAEAHNAMLSQLAAKL | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
A3M140 | MNINLTLIGQAIAFAFFVAFCMKFVWPPLINAISERQRKIADGLNAAEKAKADLADAQAQVKQELDAAKAQAAQLIEQANRRAAQLIEEARTQAAAEGERIRQQAKEAVDQEINSAREELRQQVAALAVTGAEKILNQQVDAEAHNAMLSQLAAKL | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
B0VBP7 | MNINLTLIGQAIAFAFFVAFCMKFVWPPLINAISERQRKIADGLNAAEKAKADLADAQAQVKQELDAAKAQAAQLIEQANRRAAQLIEEARTQAAAEGERIRQQAKEAVDQEINSAREELRQQVAALAVTGAEKILNQQVDAEAHNAMLSQLAAKL | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
A0LSL2 | MPPRTLADNFLVPGPTAIAELIVFLLILFIFGKYIVPFVNQKLAERQELIRSQFEEAKRARDEAEAAAAEYRAQLQEIRAEATRVRERAHEEGQQIIAEMKEQARREADRIVRAAEEQIQAERARAVAAVRAEVGSLAVELASRIVGESLADVERQHRIVERFLAELEERAQRQPAASDVVGGQQREEVHR | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
B7JB88 | MNPVGINGTLIVQLVTFVILVALLYKYMYGPLRKVMDDRRAKIADGLAAAERGKEEMALAQKRATELLREAKDKAAEIIANAERRGVELREEAQGKAREEADRIIASARAEIDVETNRAREVLRGQVVELVVNGTQRILHREIDDQTHRDIIDRMVGQL | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
B5ER46 | MNPVGINGTLIVQLVTFVILVALLYKYMYGPLRKVMDDRRAKIADGLAAAERGKEEMALAQKRATELLREAKDKAAEIIANAERRGVELREEAQGKAREEADRIIASARAEIDVETNRAREVLRGQVVELVVNGTQRILHREIDDQTHRDIIDRMVGQL | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
P41172 | MNPVGINGTLIVQLVTFVILVALLYKYMYGPLRKVMDDRRAKIADGLAAAERGKEEMALAQKRATELVREAKDKAAEIIANAERRGVELREEAQGKAREEADRIIASARAEIDVETNRAREVLRGQVVELVVNGTQRILHREIDDQTHRDIIDRMVGQL | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
A1W2T3 | MSINATLFVQAIVFLILVLFTMKFVWPPITKALDERAQKIADGLAAADRAKTELAAADQRVKQELAAASNEIATRLADAERRAQAIIEEAKARANDEGNKIVAAARAEAEQQAIQAREALREQVAALAVKGAEQILRKEVNAGVHADLLNRLKTEL | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
Q3V548 | MKNITDSFVSLGHWPFAGSFGFNTDILATNLINLSVVLGVLIFFGKGVLSDLLDNRRQRILSTIRNSEELRRGALEQLEKARARLRKVEMEADEYRVNGYSEIEREKMNLINATYENLERLENYKNETLHFEQQRAINQVRQRVFQQALQGALGTLNNCLNSELHFRTISANIGMLGAMKEITD | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has four main subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta, b and b' chains. In plastids the F-type ATPase is also known as CF(1)CF(0). Belongs to the ATPase B chain family. |
A3N2U8 | MNLNATLIGQLIAFALFVAFCMKFVWPPLIKAIEERQANIANALASAEKAKQEQADSKAAADQEILKAKEEAQKIIDLATKRRNEILETVQAEAEIERQRIIEQGHAEVESERKRVQEELRQKVAALAVAGAEKIVGCSVDQAANNDIIDKLVAEL | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
B3H2P7 | MNLNATLIGQLIAFALFVAFCMKFVWPPLIKAIEERQANIANALASAEKAKQEQADSKAAADQEILKAKEEAQKIIDLATKRRNEILESVQAEAEIERQRIIEQGHAEVESERKRVQEELRQKVAALAVAGAEKIVGRSVDQAANNDIIDKLVAEL | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
B2XWN5 | MKNVTDSFVSLGHWRSAGSFGFNTDIFATNPINLSVVIGVLIFFGKGVFSDLLDNRKLRIVNTIRNSEELCGRAVEQLEKARARLRKVEMEADQFRMNGYSEIERDKLNLINSIYKTLEQLENYKNETIHFEQQRVINQVRLRVFQQALQGALGTLNSCLSNELHLRTINANIGMFGAMKEITD | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has four main subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta, b and b' chains. In plastids the F-type ATPase is also known as CF(1)CF(0). Belongs to the ATPase B chain family. |
A7HJW1 | MDFFEINLTAVVQLLNFLFLLWILNKLLYKPFLGMMEKRKEKIEGEIVEAEKLRKQAEEIKKNAEEELKNARIRAEQIIASANSESEKIVEEAKQKAQKEAEKILQNAYLEIEKQKQEALAQVQTIATELAINLAMKVLKGTLDEKAKREYLAKVIKEYEK | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
A5FL32 | MDKLINDFSFGLFFWQALILVILILLLVKFAWKPIMESITAREEGIKNALLSAENAKREMENLQADNQRILNEARAERDAMLKEAREMKEKMIADSKNEAQEAGQKMIEQAKAAIESEKNAAMAELKSQVSTLSLSIAEKLLKEELSNKESQTKLVEKMLGDVKLN | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
A6H2D9 | MEQLLGQFSLGLFILQIILFVGLILLLKKFAWKPILDAVNEREDGIKNALLSAENARTEMQNLQADNQRILQEARLERDNMLKDAREIKEKMIADSKTEAQAQGIKMIEQAKAAIESEKNAAMAELKSQVSNLSIEIAEKLLKDELSNKDAQTKLVEKMLGDVKLN | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
Q0RDB0 | MSASAAILLAASESGHSDENVLIPPLSELLIGTLAFGLLVAFFFWKIRPQIARTYAQRTERIEGGIARAEAAQREAQALLEQYRAQLTEARAEAARIRDDAHTEGRQIVEELRASAQREIAEIKERADAQLAADRAQIVAQVRREVGVIAIDLASKIVGYQVESTATQARLVDDFIAALDNSAEGAGSSTPAPVGSGG | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
Q2J6M9 | MSATSILIAAAESGHSDENVLIPPLSELLIGTLSFALLVAFFFWKIRPQIARTYAQRTERIEGGLARAEAAQREAQALLEQYRAQLAEARTEAARIREEAHSEGRQITEELRAAAQREIAEIKARADAQLAADRAQIVAQVRREVGEIAVDLASKIVGFQLESSATQNRLIDDFIAALDNSAEGVGTVAAPVRPGG | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
B0TWS3 | MDINITLIGQMITFAIFVGFTMKFVWPPLRKALDERREKIAEGLASADRASRELEVAKRQSAEILREAKAKATEIVENAYVRAHKVDEQAKEEAIAAADKIKSMAMAEIEQEKVKAKEELKHEVVSLAMAAASKIISANVDEQSSKKILKDFVEKV | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
A8L3W1 | MLQNLVLAAAEEGAEHEDSVLVPPLAELIVGLLAFGLLVGFFFWKIYPQIRKTYAERAERIEGGLNRAERAEREAQALLEQYRSQLAEARSEAARIREDAQAQGRQIVEELRTQVQQEVAEIRERADAALVAERAQVVASVRREIGEIALELATRIVGRELENDTRQRQLVDDFIAGLDEAPQPDAVPAGPGV | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
Q14K10 | MDINITLIGQMITFAIFVGFTMKFVWPPLRKALEERREKIAEGLASADRASRELEVAKRQSAEILREAKAKATEIVENAYVRAHKVDEQAKEEAIAAADKIKSMAIAEIEQEKVKAKEQLKQELVNLAMAAASKIIAASVDEKASKKVLEDFVEKV | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
A7NEH8 | MDINITLIGQMITFAIFIGFTMKFVWPPLRKALEERREKIAEGLASADRASRELEVAKRQSAEILREAKAKATEIVENAYVRAHKVDEQAKEEAIAAADKIKSMAIAEIEQEKVKAKEQLKQELVNLAMAAASKIIAASVDEKASKKVLEDFVEKV | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
Q2A1H8 | MDINITLIGQMITFAIFIGFTMKFVWPPLRKALEERREKIAEGLASADRASRELEVAKRQSAEILREAKAKATEIVENAYVRAHKVDEQAKEEAIAAADKIKSMAIAEIEQEKVKAKEQLKQELVNLAMAAASKIIAASVDEKASKKVLEDFVEKV | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
B2SEX7 | MDINITLIGQMITFAIFVGFTMKFVWPPLRKALEERREKIAEGLASADRASRELEVAKRQSAEILREAKAKATEIVENAYVRAHKVDEQAKEEAIAAADKIKSMAIAEIEQEKVKAKEQLKQELVNLAMAAASKIIAASVDEKASKKVLEDFVEKV | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
A0Q8E3 | MDINITLIGQMITFAIFVGFTMKFVWPPLRKALEERREKIAEGLASADRASRELEVAKRQSAEILREAKAKATEIVENAYVRAHKVDEQAKEEAIAAADKIKSMAIAEIEQEKVKAKEQLKQELVNLAMAAASKIIAASVDEKASKKVLEDFVEKV | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
Q0BK80 | MDINITLIGQMITFAIFIGFTMKFVWPPLRKALEERREKIAEGLASADRASRELEVAKRQSAEILREAKAKATEIVENAYVRAHKVDEQAKEEAIAAADKIKSMAIAEIEQEKVKAKEQLKQELVNLAMAAASKIIAASVDEKASKKVLEDFVEKV | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
Q5NIK7 | MDINITLIGQMITFAIFVGFTMKFVWPPLRKALEERREKIAEGLASADRASRELEVAKRQSAEILREAKAKATEIVENAYVRAHKVDEQAKEEAIAAADKIKSMAIAEIEQEKVKAKEQLKQELVNLAMAAASKIIAASVDEKASKKVLEDFVEKV | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
A4IW20 | MDINITLIGQMITFAIFVGFTMKFVWPPLRKALEERREKIAEGLASADRASRELEVAKRQSAEILREAKAKATEIIENAYVRAHKVDEQAKEEAIAAADKIKSMAIAEIEQEKVKAKEQLKQELVNLAMAAASKIIAASVDEKASKKVLEDFVEKV | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
Q8RGD8 | MPIISIDYTFFWQIINFFLLLFIVKKYFKEPISKIINERKQKIEAELVEATKNKKEAEQLLKDAEAQINASRKEATEIVKAAQRKAEEEAHNLIREARENRENILKTTELEITKIKNDAKEELGREVKNLAAELAEKIIKEKVDDAQEISLIDKFIAEVGEDK | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
P35011 | MFFDVLGYENSQSSIKINLDLLETNIINIFILIIILIYLGRKFLGNILINRQNRVITSIRESEERLEKSTIRLNEAKNQLSSAQIIINQIKQEAKNTAANVKESILKQGKTDIERLLLNTKNYIYNTELQIKKQIKQQIAALALQKVQSKLKDELDNNIQQKIIDQSLAMLTIRNK | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has four main subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta, b and b' chains. In plastids the F-type ATPase is also known as CF(1)CF(0). Belongs to the ATPase B chain family. |
Q5KUI9 | MWKANVWVLGEAAHGISGGTIIYQLLMFIILLALLRKFAWQPLMNIMKQREEHIANEIDQAEKRRQEAEKLLEEQRELMKQSRQEAQALIENARKLAEEQKEQIVASARAEAERVKEVAKKEIEREKEQAMAALREQVASLSVLIASKVIEKELTEQDQRKLIEAYIKDVQEAGGAR | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
Q39Q52 | MANACKKKRLLKSVMMPAAVCAAVIGLSALGFAAEGGEGAHHVDTGKQMKDFMWRVIDFAALLGVIIWALKKANAKGALADRTANIEKALREAEEARAAAEKKFAEYSGKLEKANLEIDDIYAAIRKEAELEKERIIAEAKLTADKIREQAAATASQEVLKAKAELRGEAARLAVQMAEQSLRENIKKDDQDRLVNDYLTKVENLH | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
Q65Q03 | MNLNATLIGQLIAFALFTWFCVKFVWPPIIKAIEERQSSIANALASAEKAKQDQADSQAAVEQEILAAKEEAQKIIDLANKRRNDILEEVKTEAENLKATIIAQGHAEVEAERKRVQEELRVKVASLAIAGAEKIVGRTVDEAANNDIIDKLVAEL | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
A1U7H8 | MNINLTLIGQSIAFAIFVWFCVKYVWPPITAAMEARQKKIADGLSAADRASLDLELAQEKATKELQKAKEEAAALIDQANKRAAQIVEASKEDARKEGEKLIEQARAEIQQERVQARDALRAEVATLAVAGAEKILETSVDAKAHSEMLEKLAAEL | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
P06291 | MENGTYFIISSNFWTIAGSFGLNTNLLETNLINLGVVLGLLVYFGKGVLSNLLNNRKLTILNTIQDAEERYKEATDKLNQARTRLQQAKQKADDIRINGLSQMEKEKQDLINAADEDSKRLEDSKNATIRFEKQRAIEQVRQQVSRLALERALETLKSRLNSELHLRMIDYHIGLLRAMESTIE | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has four main subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta, b and b' chains. In plastids the F-type ATPase is also known as CF(1)CF(0). Belongs to the ATPase B chain family. |
Q6F206 | MIFFAETQTAGVPEIITSLFPNLPNFIAHVIATIVLVVILSKLMYKPFRKTIKDRRNKINELLSEAVQKQTEANIGVRKAEALLQDAKTESSLIIQTSKVDADIQKTHIISEAHKYADIIKNQAEKDIAQERSKIEAEIKTTIVNVAFDAAEQILQTEINKTKNKKIVDEFIENLDK | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
Q601Z9 | MVNLNQSLGDLFKGIIPNVYVLGATIVSFLILFLFITYFVYRPLKKYIKKRKDFLQSHIDLTIKSNVEAEKLEKKSQQKLLETKEFCTDLKEKSQIEANKFLEDAKKTAIDNARQLINEGQKVLLEYENEIKSKYYMNVINVAVEICQKYLEKQDKNNKILQQSLIADLEKELKKRENSSKKKDNFGK | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
Q4A8W3 | MVNLNQSLGDLFKGIIPNVYVLGATIVSFLVLFLFITYFVYRPLKKYIKKRKDFLQNHIDLTIKSNVEAEKLEKKSQQKLLETKEFCIELKEKSQIEANKFLEDAKKTAIDNARQLINEGQKVLLEYENEIKSKYYMNVINVAVEICQKYLEKQDKNNKILQQSLIADLEKELRKRENSSKKKDNFGK | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
Q4AAW1 | MVNLNQSLGDLFKGIIPNVYVLGATIVSFLILFLFITYFVYRPLKKYIKKRKDFLQNHIDLTIKSNVEAEKLEKKSQQKLLETKEFCIELKEKSQIEANEFLEDAKKTAIDNARQLINEGQKVLLEYENEIKSKYYMNVINVAVEICQKYLEKQDKNNKILQQSLIADLEKELKKRENSSKKKDNFGK | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
Q9MUT1 | MTDILTNIFTILSRMSLAEGFGFNTDIFETNILNLAVVLGILLTSGREFFVSLLQNRQQNILQSINDADERYKEAAEKLQQAQNEFEQAKLEADQILAQSKKTASEIEVGLMNLIKEDTKKLLDMKQATISFEEEKAISEIRRQVIRLALQRALEQSKSRLNRRLQKRVTRLNIGLLGRLVTPNDV | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has four main subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta, b and b' chains. In plastids the F-type ATPase is also known as CF(1)CF(0). Belongs to the ATPase B chain family. |
B3PLV4 | MNFNINQSSISDAITKTFGNLTINWPFFVFSFLTLILVVTIVTLLVYKPLKKMLKNRQNFIQNNIDESIKAKEAALKVQEEIDEKIIESSKHANQIIEQAKLERERIINNGIEVSNKKAEIIIEQANILVTKSQAEFENKQRKIIVENAVEIAKKIIGREIRDKDNLKMIEEMLES | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
Q1GXM6 | MNINLTLIAQAISFAILIWFTTKFVWPYLLNAIETRQKTIADGLAAAERGKQELDMATQRSAEVVNDAKQKATSIIAQAEKRASEIVEEAKANAKAEGDRIIAGAKAEIDQEVNRAKEGLRQQVSALAVAGAEKILRKEIDAKAHADLLNAIANEL | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
B3E0Z6 | MHQLGIEWNKLIAQIINFVIVLWVLNRFAFKPVLKILEERRKKIAESLQNAEKIKQELAEAEEARKEILRKANEQASFIVAEAQKVASYQGEKKIQEAVEEAKRVLKKAEESAKLEREKAKEEMRREILNLVIEITSKVVGKTLTLDDQERLKNEVLSKLPQKEGHEAYSRN | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
A2SC66 | MSLNATLFAQLVVFFILAWFTMKFVWPPITKALDERASKIADGLAAADRAKTELASANKRVEEQLASVRDENARRLADAEKRALAIVEDAKKRATEEGSKIVAAAKSEAEQQLVQARESLREQVAALAVKGAEQILKREVNAGVHADLLSRLKTEL | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has four main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains (By similarity). Belongs to the ATPase B chain family. |
B0JWU9 | MIIDTILLLATEAKEAAAEGFGINTDILGTNLFNLSILLGLIIFYGRKVLGQILGERQSKIAEALAEAENRKNIAATALAEEQKKLALAKQEAEKIIDNSRSRAKAVTADIAAQAELDIQRMRESAAKDLSAEQDRVLVELRQRITALALANVESQLSTGLEESVQQTLIDRSLANLGGK | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has four main subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta, b and b' chains. Belongs to the ATPase B chain family. |
C5CA74 | MISNGLILAAAEGANPLIPNPWEILVVVVGFALLMFIVIKFIVPTLEKSYQDRVEAIEGGLAKAEKAQAEANAMMADYESQLADARTEANRIREDARTEAAEIVAEARERATAEATRVFEQAQAQIAAERQQAAAQLKREVGSLATTLAGKIVGESLEDDARSQRVVDRFLADLDRHQSAGVAE | 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 (By similarity). Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains (By similarity). Belongs to the ATPase B chain family. |
O05429 | MQAIFQALNFNPWTFLFQTLNLLVVMGLLYVFLYKPLGKVLADREARIEGNLNDAAAAREKAENILAEYRQQLQGARQEAQAILDRATKMAEETRAEIINRAREEAERTLAQARREIEGEKSKALAAIRSEAASLAILAAGKVLERSLTPDDQERLAREAIAEVERLQ | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
Q09X31 | MKNVTDPFLSLSYWPSAGSFGFNTDILATNPINLSVVLGVLIFFGKGVLSDLLDNRKQRILKTIRNSEELREGALEQLEKARSRLRKVEKEADQFRVNGYSEIEREKLNLINSTSKTLEQLENYKNETIHFEQQRAINEVRQRVFQQALEGALGTLNSCLNNELHLRTISTNIGMFGTMKEITD | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has four main subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta, b and b' chains. In plastids the F-type ATPase is also known as CF(1)CF(0). Belongs to the ATPase B chain family. |
A0QCX4 | MMGDASLSVLASSQVVAEGGNNFLVPNGTFFFVLAIFLIVLAVIGTFVVPPVMKVLRERDAMVAKTAADNRKAAEQFEAAQADYEEAMTEARVQASSLRDNARAEGRKVVEDARAKAEQEVLSTLQLAARQLKRERDAVELDLRANVASMSATLASRILGVDVAPAAATTSATKTSGR | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
B1MLV8 | MGELHSVASAVTAVAAEAAEEGGKQNNFLIPNGTFFVVLAIFLIVLAVIGTFVVPPIQKVLKAREDMVTKTAEDNRNAAEQFTAAEADYKDELAKARGAATAVRDEARAEGRGILEDMRQRANAEATAVTETAAAELARQGEVTAGELATNVDSLSRTLAERVLGVSLSEPANAGRG | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
A5IYE1 | MNLFYNLSLKANTLLSAQSGGIKDELKDKFKTLFPTWPMFLATLIAFILVVLILWFLLHKPIKKAMKARQDYIQKNIDEAKLTNDISKQKLNEANKRLAEAYSEADELIKNAKIHGESVIDEYTHKAKNKSKRIIEKAHMEIESERQKMVDDSKSNIAKAAIEISKKIMQKEVTKESQDEVIKNFLKDK | 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). F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Belongs to the ATPase B chain family. |
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