1UAZ,1E0P,3VHZ,4FBZ


Conserved Protein Domain Family
7tm_bacteriorhodopsin

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cd15244: 7tm_bacteriorhodopsin 
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light-driven outward proton pump bacteriorhodopsin, member of the seven-transmembrane GPCR superfamily
Bacteriorhosopsin (BR) serves as a light-driven retinal-binding outward proton pump, generating an outside positive membrane potential and thus creating an inwardly directed proton motive force (PMF) necessary for ATP synthesis. BR belongs to the microbial rhodopsin family, also known as type I rhodopsins, comprising light-driven inward chloride pump halorhodopsin (HR), light-gated cation channel channelrhodopsin (ChR), light-sensor activating transmembrane transducer protein sensory rhodopsin II (SRII), light-sensor activating soluble transducer protein Anabaena sensory rhodopsin (ASR), and other light-driven proton pumps such as blue-light absorbing and green-light absorbing proteorhodopsins, among others. They have been found in various single-celled microorganisms from all three domains of life, including halophile archaea, gamma-proteobacteria, cyanobacteria, fungi, and green algae. While microbial (type 1) and animal (type 2) rhodopsins have no sequence similarity with each other, they share a common architecture consisting of seven-transmembrane alpha-helices (TM) connected by extracellular loops and intracellular loops. Both types of rhodopsins consist of opsin and a covalently attached retinal (the aldehyde of vitamin A), a photoreactive chromophore, via a protonated Schiff base linkage to an amino group of lysine in the middle of the seventh transmembrane helix (TM7). Upon the absorption of light, microbial rhodopsins undergo light-induced photoisomerization of all-trans retinal into the 13-cis isomer, whereas the photoisomerization of 11-cis retinal to all-trans isomer occurs in the animal rhodopsins. While animal visual rhodopsins are activated by light to catalyze GDP/GTP exchange in the alpha subunit of the retinal G protein transducin (Gt), microbial rhodopsins do not activate G proteins, but instead can function as light-dependent ion pumps, cation channels, and sensors.
Statistics
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PSSM-Id: 320372
View PSSM: cd15244
Aligned: 9 rows
Threshold Bit Score: 236.13
Threshold Setting Gi: 108766100
Created: 16-Feb-2014
Updated: 26-Jul-2017
Structure
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Program:
Drawing:
Aligned Rows:
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Conserved site includes 16 residues -Click on image for an interactive view with Cn3D
Feature 1:ligand binding site [chemical binding site]
Evidence:
  • Structure:1UAZ: Halorubrum chaoviator archaerhodopsin binds retinal, contacts at 4A.
    View structure with Cn3D
  • Structure:1E0P: Halobacterium salinarum bacteriorhodopsin binds retinal, contacts at 4A.
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                                                        
1UAZ_A        13 RPETLWLGIGTLLMLIGTFYFIVKGWGVTDkeaREYYSITILVPGIASAAYLSMFFgigltevqv-gsemldiyYARYAD 91
1E0P_A         3 RPEWIWLALGTALMGLGTLYFLVKGMGVSDpdaKKFYAITTLVPAIAFTMYLSMLLgygltmvpf-ggeqnpiyWARYAD 81
3VHZ_A        20 RPEWIWLALGTALMGLGTLYFLVKGMGVSDpdaKKFYAITTLVPAIAFTMYLSMLLgygltmvpf-ggeqnpiyWARYAD 98
4FBZ_A         6 GPESIWLWIGTIGMTLGTLYFVGRGRGVRDrkmQEFYIITTFITTIAAAMYFAMATgfgvtevvv-gdealtiyWARYAD 84
gi 2499387    12 GGESIFLWVGTAGMFLGMLYFIARGWSVSDqrrQKFYIATIMIAAIAFVNYLSMALgfgvttiel-ggeeraiyWARYTD 90
gi 110666993   5 GSEATWLWIGTIGMVLGTVYFAVRGRGSTDpeqQTYYIITTLIPAIAAAAYLAMATglgvismpirgtevidiyWARYAD 84
gi 55231469   12 EGEGIWLALGTVGMLLGMVYFMAKGWDVQDpeqEEFYVITILIAGIAASSYLSMFFgfgltevelvngrvidvyWARYAD 91
gi 108766100   2 EALWLWIGFVGMLLGTLYFAFLLTNAPEGT---RYFFVITATITGIAAIAYLVMATgsgstvl----pdgrefyWARYID 74
gi 297548767   3 SATVTVLWVTSLLMILCTLVFTYRSFRARTe-iKHFYYLTALITLIAATLYMTMASgyggigq-----ngrvilFGRYID 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1        #  ##                                #   #                     #  ##  #         
1UAZ_A        92 WLFTTPLLLLDLALLAKvd-----rVSIGTLVGVDALMIVTGLVGAlsht------plaRYTWWLFSTICMIVVLYFLAT 160
1E0P_A        82 WLFTTPLLLLDLALLVDad-----qGTILALVGADGIMIGTGLVGAltkv------ysyRFVWWAISTAAMLYILYVLFF 150
3VHZ_A        99 WLFTTPLALLDLALLVDad-----qGTILALVGADGIMIGTGLVGAltkv------ysyRFVWWAISTAAMLYILYVLFF 167
4FBZ_A        85 WLFTTPLLLLDLGLLAGan-----rNTIATLIGLDVFMIGTGMIAAfaat------pgtRIAWWGISTGALLALLYVLVG 153
gi 2499387    91 WLFTTPLLLYDLALLAGad-----rNTIYSLVGLDVLMIGTGALATlsagsgvlpagaeRLVWWGISTGFLLVLLYFLFS 165
gi 110666993  85 WLLTTPLLIIDLALVAGar-----kQTLYKLIIIDAIMILGGLAGSmmqq-----gaviRIVWWAVSTAAFIILLYYLLG 154
gi 55231469   92 WLFTTPLLLLDIGLLAGas-----nRDMASLITIDAFMIVTGLAATlmkv------pvaRYAFWTISTIAMLFVLYYLVV 160
gi 108766100  75 WVITTPLLLLDLCLLALadpr-rnvTFIASLIALDVVMILTGLWAGatvn------vagRAILFIISTAAFIGVLYLLVS 147
gi 297548767  77 WVITTPLLLMNLALIALprnfpsrfAVIGTMIAADVYMIVSGLGASlir-------snfRWAFFAVSCAGFLAVLYFIVV 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
Feature 1                                   #  ##  #                       #  ##           
1UAZ_A       161 SLRAaakergPEVASTFNTLTALVLVLWTAYPILWIIGtegag-vvglGIETLLFMVLDVTAKVGFGFILLRSR 233
1E0P_A       151 GFTSkaesmrPEVASTFKVLRNVTVVLWSAYPVVWLIGsegag-ivplNIETLLFMVLDVSAKVGFGLILLRSR 223
3VHZ_A       168 GFTSkaesmrPEVASTFKVLRNVTVVLWSAYPVVWLIGsegag-ivplNIETLLFMVLDVSAKVGFGLILLRSR 240
4FBZ_A       154 TLSKdargqsPEVASLFGRLRNLVIVLWLLYPVVWILGtegtfgilplYWETAAFMVLDLSAKVGFGVVLLRSR 227
gi 2499387   166 NLTDraselsGDLQSKFSTLRNLVLVLWLVYPVLWLVGteglg-lvglPIETAAFMVLDLTAKIGFGIILLQSH 238
gi 110666993 155 ELSErarsrsAETGIVFNRLRNITLGLWALYPIVWILGtgggfgiiavTTEIMLYVMLDIGTKIGFGAVLLESQ 228
gi 55231469  161 VVGEaasdasEEAQSTFNVLRNIILVAWAIYPVAWLVGteglg-lvglFGETLLFMILDLTAKIGFGFILLRSR 233
gi 108766100 148 RLFAeasrrtPAVAQIFRTLAVLTIVLWICYPIVWLIGtegfg-avslSVEVFLFMVLDLLAKVGFGLLLLSSR 220
gi 297548767 150 KLTPeanvrsEPVQRHYSTLSIMLIALWVCYPIVWILGtegfg-vislLPEVVLYAVLDILAKGAFGFVLLSKP 222

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