|SMART accession number:||SM01021|
|Description:||The bacterial opsins are retinal-binding proteins that provide light- dependent ion transport and sensory functions to a family of halophilic bacteria (PUBMED:2468194), (PUBMED:2591367). They are integral membrane proteins believed to contain seven transmembrane (TM) domains, the last of which contains the attachment point for retinal (a conserved lysine).|
|Interpro abstract (IPR001425):|
Bacterial rhodopsins are a family of bacterial opsins. They are retinal-binding proteins that provide light-dependent ion transport and sensory functions to a family of halophilic bacteria [(PUBMED:2468194), (PUBMED:2591367)]. They are integral membrane proteins believed to contain seven transmembrane (TM) domains, the last of which contains the attachment point for retinal binding (a conserved lysine).
The archaeal/bacterial/fungal rhodopsin family includes 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 UV) responses. This family also includes distantly related proteins that do not contain the retinal binding lysine and so cannot function as opsins. Some fungal examples are: O74870, P25619, P38079, Q12117.
|GO process:||ion transport (GO:0006811)|
|GO component:||membrane (GO:0016020)|
|GO function:||ion channel activity (GO:0005216)|
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- Evolution (species in which this domain is found)
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