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3.E.1.6.1
Green-light-absorbing H+ pumping proteorhopdopsin of 249 aas and 8 TMSs. It exhibits variable vectorality: H+ is pumped out at basic pH but not at acidic pH; see Friedrich et al., 2002). It presents a fast proton release and an alkaliphilic photocycle, consistent with its marine origin and the near-surface environment where this bacterium was collected. This proteorhodopsin has been used to measure membrane potentials and electrical spiking in E. coli (Kralj et al., 2011; Ward et al., 2011).  3-d structures of three proteorhodopsins show that they can exist as pentamers or hexamers, depending on the protein (Ran et al. 2013).  Protonation states of several carboxylic acids, the boundaries and distortions of transmembrane α-helices, and secondary structural elements in the loops have been identified (Shi et al. 2009). Proteorhodopsin molecules incorporated into mesostructured silica films exhibit native-like function, as well as enhanced thermal stability compared to surfactant or lipid environments (Jahnke et al. 2018).

Accession Number:Q9F7P4
Protein Name:Green-light absorbing proteorhodopsin [Precursor]
Length:249
Molecular Weight:27251.00
Species:uncultured proteobacterium EBAC31A08 [133804]
Number of TMSs:8
Location1 / Topology2 / Orientation3: Cell membrane1 / Multi-pass membrane protein2
Substrate H+

Cross database links:

Pfam: PF01036   

Gene Ontology

GO:0016021 C:integral to membrane
GO:0005886 C:plasma membrane
GO:0005216 F:ion channel activity
GO:0009881 F:photoreceptor activity
GO:0007602 P:phototransduction
GO:0018298 P:protein-chromophore linkage
GO:0015992 P:proton transport

References (10)

[1] “Bacterial rhodopsin: evidence for a new type of phototrophy in the sea.”  Beja O.et.al.   10988064
[2] “Detection of fast light-activated H+ release and M intermediate formation from proteorhodopsin.”  Krebs R.A.et.al.   11943070
[3] “Proton transfers in the photochemical reaction cycle of proteorhodopsin.”  Dioumaev A.K.et.al.   11969395
[4] “Characterization of the photochemical reaction cycle of proteorhodopsin.”  Varo G.et.al.   12547799
[5] “Spectroscopic and photochemical characterization of a deep ocean proteorhodopsin.”  Wang W.W.et.al.   12821661
[6] “Proteorhodopsin is a light-driven proton pump with variable vectoriality.”  Friedrich T.et.al.   12206764
[7] “The photochemical reaction cycle of proteorhodopsin at low pH.”  Lakatos M.et.al.   12719254
[8] “Proton transport by proteorhodopsin requires that the retinal Schiff base counterion Asp-97 be anionic.”  Dioumaev A.K.et.al.   12767242
[9] “Proteorhodopsin phototrophy in the ocean.”  Beja O.et.al.   11459054
[10] “Diversification and spectral tuning in marine proteorhodopsins.”  Man D.et.al.   12682005
Structure:
2L6X   5ABB     

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FASTA formatted sequence
1:	MKLLLILGSV IALPTFAAGG GDLDASDYTG VSFWLVTAAL LASTVFFFVE RDRVSAKWKT 
61:	SLTVSGLVTG IAFWHYMYMR GVWIETGDSP TVFRYIDWLL TVPLLICEFY LILAAATNVA 
121:	GSLFKKLLVG SLVMLVFGYM GEAGIMAAWP AFIIGCLAWV YMIYELWAGE GKSACNTASP 
181:	AVQSAYNTMM YIIIFGWAIY PVGYFTGYLM GDGGSALNLN LIYNLADFVN KILFGLIIWN 
241:	VAVKESSNA