protein

Recombinant Alkaliphilus oremlandii ATP synthase subunit c (atpE)

MBS1000434

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Recombinant Protein

Recombinant Alkaliphilus oremlandii ATP synthase subunit c (atpE)

ATP synthase subunit c (atpE)

Recombinant ATP synthase subunit c (atpE); ATP synthase subunit c; ATP synthase F(0) sector subunit c F-type ATPase subunit c; F-ATPase subunit c Lipid-binding protein

F0F1 ATP synthase subunit C; ATP synthase subunit c; F0F1 ATP synthase subunit C; ATP synthase F(0) sector subunit c; F-type ATPase subunit c; F-ATPase subunit c; Lipid-binding protein

atpE

Clos_2565; atpE; F-ATPase subunit c

ATPL_ALKOO

E Coli or Yeast or Baculovirus or Mammalian Cell

Jan-88

88

MEGITGKELILAASAIGAGLAMIAGLGPGIGQGIAAGKG
AEAVGRQPEAQGDILRTMLLGQAVAETTGIYSLVIALIL
LFANPLIRLL

>90%(SDS-PAGE)

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degree C. For extended storage, store at -20 or -80 degree C. Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4 degree C for up to one week.

Species: Alkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii (strain OhILAs))

F1F0 ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F1 containing the extramembraneous catalytic core and F0 containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation.Key component of the F0 channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F1 delta and epsilon subunits .

158321585

YP_001514092.1

NC_009922.1

A8MJW4

35kD

F-type ATPase, Prokaryotes And Chloroplasts Pathway (381517); Metabolic Pathways (132595); Oxidative Phosphorylation Pathway (59587); Oxidative Phosphorylation Pathway (303)

Function: F1F0 ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F1 containing the extramembraneous catalytic core and F0 containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation . By similarity. HAMAP-Rule MF_01396Key component of the F0 channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F1 delta and epsilon subunits . By similarity. HAMAP-Rule MF_01396. Subunit structure: F-type ATPases have 2 components, F1 - the catalytic core - and F0 - the membrane proton channel. F1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. F0 has three main subunits: a1, b2 and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F1 is attached to F0 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. Subcellular location: Cell membrane; Multi-pass membrane protein . By similarity HAMAP-Rule MF_01396. Sequence similarities: Belongs to the ATPase C chain family.

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