Summary: Bacteriorhodopsin-like protein
This is the Wikipedia entry entitled "Bacterial rhodopsins". More...
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Bacterial rhodopsins Edit Wikipedia article
||This article needs attention from an expert in archaea. The specific problem is: historical bacteria->archaea classification change.|
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 and other bacteria. They are integral membrane proteins with seven transmembrane helices, the last of which contains the attachment point for retinal (a conserved lysine).
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.
- Oesterhelt D, Tittor J (1989). "Two pumps, one principle: light-driven ion transport in halobacteria". Trends Biochem. Sci. 14 (2): 57–61. doi:10.1016/0968-0004(89)90044-3. PMID 2468194.
- Lottspeich F, Oesterhelt D, Blanck A, Ferrando E, Schegk ES (1989). "Primary structure of sensory rhodopsin I, a prokaryotic photoreceptor". EMBO J. 8 (13): 3963–3971. PMC 401571. PMID 2591367.
|This membrane protein–related article is a stub. You can help Wikipedia by expanding it.|
Bacteriorhodopsin-like protein Provide feedback
The bacterial opsins are retinal-binding proteins that provide light- dependent ion transport and sensory functions to a family of halophilic bacteria [2,3]. 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). 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.
Internal database links
External database links
This tab holds annotation information from the InterPro database.
InterPro entry 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: SWISSPROT, SWISSPROT, SWISSPROT, SWISSPROT.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||membrane (GO:0016020)|
|Molecular function||ion channel activity (GO:0005216)|
|Biological process||ion transport (GO:0006811)|
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
- the number of residues in the sequence
- the Pfam graphic itself.
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This clan contains various seven-transmembrane receptors and related proteins. A major member is Pfam:PF00001, members of which have been considered to be typical members of the rhodopsin superfamily. Many members of this clan are Caenorhabditis proteins, suggesting great expansion of the relevant families in these nematode worms.
The clan contains the following 35 members:7TM-7TMR_HD 7tm_1 7tm_2 7tm_4 7TM_GPCR_Sra 7TM_GPCR_Srab 7TM_GPCR_Srb 7TM_GPCR_Srbc 7TM_GPCR_Srd 7TM_GPCR_Srh 7TM_GPCR_Sri 7TM_GPCR_Srj 7TM_GPCR_Srsx 7TM_GPCR_Srt 7TM_GPCR_Sru 7TM_GPCR_Srv 7TM_GPCR_Srw 7TM_GPCR_Srx 7TM_GPCR_Srz 7TM_GPCR_Str Bac_rhodopsin Dicty_CAR DUF1182 DUF621 Frizzled Git3 Git3_C GpcrRhopsn4 Lung_7-TM_R Ocular_alb Serpentine_r_xa Sre Srg TAS2R V1R
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
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- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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Curation and family details
|Seed source:||Pfam-B_1412 (release 3.0)|
|Author:||Finn RD, Bateman A|
|Number in seed:||17|
|Number in full:||3174|
|Average length of the domain:||141.90 aa|
|Average identity of full alignment:||35 %|
|Average coverage of the sequence by the domain:||89.93 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||13|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Bac_rhodopsin domain has been found. There are 161 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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