Gene Ontology annotation through association of InterPro records with GO terms
-
IPR018229 (rhodopsin retinal-binding site) is mapped to monoatomic ion channel activity and ion transport. For bacteriorhodopsin, and for the halorhodopsins, sensory rhodopsin II and proteorhodopsin checked in QuickGO, the channel mapping is wrong because these proteins are pumps or sensors, not channels.
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Combined Automated Annotation using Multiple IEA Methods
Functions of a new photoreceptor membrane.
-
Light-exposed starved or anaerobic cells with purple membrane build a proton gradient without another energy source.
"generate and maintain a proton gradient across the cell membrane as long as they are exposed to light"
Bacteriorhodopsin precursor. Characterization and its integration into the purple membrane.
-
The precursor integrates into the purple membrane, correctly folded and with retinal attached.
"it integrates into the purple membrane in the correctly folded conformation"
Photophosphorylation in Halobacterium halobium.
-
The purple membrane acts as a light-driven proton pump whose gradient drives ATP synthesis in vivo.
"the purple membrane functions as a lightdriven proton pump and the cells use the resulting chemiosmotic gradient for ATP synthesis"
Reconstitution of purple membrane vesicles catalyzing light-driven proton uptake and adenosine triphosphate formation.
Aspartic acid substitutions affect proton translocation by bacteriorhodopsin.
Attachment site(s) of retinal in bacteriorhodopsin.
Structure of bacteriorhodopsin at 1.55 A resolution.
Molecular mechanism of vectorial proton translocation by bacteriorhodopsin.
-
Light isomerises retinal; the Schiff base releases a proton outward and is reprotonated from the cytoplasm.
"The Schiff base then releases a proton to the extracellular medium, and is subsequently reprotonated from the cytoplasm."
Bacteriorhodopsin.
-
Review of the step-by-step mechanism of the bacteriorhodopsin proton transport cycle.
"the proton transport cycle of the light-driven pump, bacteriorhodopsin"
Rhodopsin-like protein from the purple membrane of Halobacterium halobium.
Bacteriorhodopsin is involved in halobacterial photoreception.
-
Bacteriorhodopsin-mediated photoreception works through the light-dependent proton motive force.
"We conclude that the BR-mediated photoreception is due to the light-dependent generation of delta mu H+."
Expression of the bop gene cluster of Halobacterium halobium is induced by low oxygen tension and by light.
Genomic and genetic dissection of an archaeal regulon.
Two photosystems controlling behavioural responses of Halobacterium halobium.