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Accession Number: | P02945 |
Protein Name: | BACR aka BOP aka VNG1467G |
Length: | 262 |
Molecular Weight: | 28256.00 |
Species: | Halobacterium halobium [2242] |
Number of TMSs: | 7 |
Location1 / Topology2 / Orientation3: | Cell membrane1 / Multi-pass membrane protein2 |
Substrate | H+ |
Cross database links:
HEGENOM: | HBG498017 |
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RefSeq: | NP_280292.1 |
Entrez Gene ID: | 1448071 |
Pfam: | PF01036 |
BioCyc: | HSP64091:VNG1467G-MONOMER |
KEGG: | hal:VNG1467G |
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
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References (25)[1] “The bacteriorhodopsin gene.” Dunn R.J.et.al. 12049093 [2] “Studies on the light-transducing pigment bacteriorhodopsin.” Dunn R.J.et.al. 6327180 [3] “Bacterioopsin, haloopsin, and sensory opsin I of the halobacterial isolate Halobacterium sp. strain SG1: three new members of a growing family.” Soppa J.et.al. 8478333 [4] “Bacteriorhodopsin precursor. Characterization and its integration into the purple membrane.” Seehra J.S.et.al. 6706999 [5] “Genome sequence of Halobacterium species NRC-1.” Ng W.V.et.al. 11016950 [6] “Amino acid sequence of bacteriorhodopsin.” Khorana H.G.et.al. 291920 [7] “Mass spectrometric analysis of integral membrane proteins: application to complete mapping of bacteriorhodopsins and rhodopsin.” Ball L.E.et.al. 9541408 [8] “Attachment site(s) of retinal in bacteriorhodopsin.” Katre N.V.et.al. 6794028 [9] “Electrospray-ionization mass spectrometry of intact intrinsic membrane proteins.” Whitelegge J.P.et.al. 9655347 [10] “Bicelle crystallization: a new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure.” Faham S.et.al. 11829498 [11] “Tertiary structure of bacteriorhodopsin. Positions and orientations of helices A and B in the structural map determined by neutron diffraction.” Popot J.-L.et.al. 2614846 [12] “Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy.” Henderson R.et.al. 2359127 [13] “Electron-crystallographic refinement of the structure of bacteriorhodopsin.” Grigorieff N.et.al. 8676377 [14] “Three-dimensional structure of proteolytic fragment 163-231 of bacterioopsin determined from nuclear magnetic resonance data in solution.” Barsukov I.L.et.al. 1606953 [15] “1H-15N-NMR studies of bacteriorhodopsin Halobacterium halobium. Conformational dynamics of the four-helical bundle.” Orekhov V.Y.et.al. 1332860 [16] “Surface of bacteriorhodopsin revealed by high-resolution electron crystallography.” Kimura Y.et.al. 9296502 [17] “X-ray structure of bacteriorhodopsin at 2.5-A from microcrystals grown in lipidic cubic phases.” Pebay-Peyroula E.et.al. 9287223 [18] “Lipid patches in membrane protein oligomers: crystal structure of the bacteriorhodopsin-lipid complex.” Essen L.-O.et.al. 9751724 [19] “Proton transfer pathways in bacteriorhodopsin at 2.3 Angstrom resolution.” Luecke H.et.al. 9632391 [20] “Structure of bacteriorhodopsin at 1.55-A resolution.” Luecke H.et.al. 10452895 [21] “High-resolution X-ray structure of an early intermediate in the bacteriorhodopsin photocycle.” Edman K.et.al. 10548112 | |
Structure: | |
[...more] |
External Searches:
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Analyze:
Predict TMSs (Predict number of transmembrane segments) | ||||
FASTA formatted sequence |
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1: MLELLPTAVE GVSQAQITGR PEWIWLALGT ALMGLGTLYF LVKGMGVSDP DAKKFYAITT 61: LVPAIAFTMY LSMLLGYGLT MVPFGGEQNP IYWARYADWL FTTPLLLLDL ALLVDADQGT 121: ILALVGADGI MIGTGLVGAL TKVYSYRFVW WAISTAAMLY ILYVLFFGFT SKAESMRPEV 181: ASTFKVLRNV TVVLWSAYPV VWLIGSEGAG IVPLNIETLL FMVLDVSAKV GFGLILLRSR 241: AIFGEAEAPE PSAGDGAAAT SD