Microbial rhodopsin

http://dbpedia.org/resource/Microbial_rhodopsin an entity of type: Thing

Microbial rhodopsins, also known as bacterial rhodopsins are retinal-binding proteins that provide light-dependent ion transport and sensory functions in halophilic and other bacteria. They are integral membrane proteins with seven transmembrane helices, the last of which contains the attachment point (a conserved lysine) for retinal. Contrary to their name, microbial rhodopsins are found not only in Archaea and Bacteria, but also in Eukaryota (such as algae) and viruses; although they are rare in complex multicellular organisms. rdf:langString
rdf:langString Microbial rhodopsin
rdf:langString Bacteriorhodopsin-like protein
xsd:integer 48050134
xsd:integer 1109327245
xsd:integer 3
rdf:langString PDOC00291
xsd:integer 2
rdf:langString Bacteriorhodopsin trimer
rdf:langString IPR001425
rdf:langString PF01036
rdf:langString Bac_rhodopsin
xsd:integer 200
rdf:langString Microbial rhodopsins, also known as bacterial rhodopsins are retinal-binding proteins that provide light-dependent ion transport and sensory functions in halophilic and other bacteria. They are integral membrane proteins with seven transmembrane helices, the last of which contains the attachment point (a conserved lysine) for retinal. This protein family includes light-driven proton pumps, ion pumps and ion channels, as well as light sensors. For example, the proteins from halobacteria include bacteriorhodopsin and archaerhodopsin, which are light-driven proton pumps; halorhodopsin, a light-driven chloride pump; and sensory rhodopsin, which mediates both photoattractant (in the red) and photophobic (in the ultra-violet) responses. Proteins from other bacteria include proteorhodopsin. Contrary to their name, microbial rhodopsins are found not only in Archaea and Bacteria, but also in Eukaryota (such as algae) and viruses; although they are rare in complex multicellular organisms.
xsd:integer 6
xsd:integer 1
xsd:nonNegativeInteger 32292
xsd:string Bac_rhodopsin

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