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P02945

- BACR_HALSA

UniProt

P02945 - BACR_HALSA

Protein

Bacteriorhodopsin

Gene

bop

Organism
Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 2 (01 Jul 1989)
      Previous versions | rss
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    Functioni

    Light-driven proton pump.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei98 – 981Primary proton acceptor

    GO - Molecular functioni

    1. ion channel activity Source: InterPro
    2. photoreceptor activity Source: UniProtKB-KW

    GO - Biological processi

    1. phototransduction Source: UniProtKB-KW
    2. protein-chromophore linkage Source: UniProtKB-KW
    3. proton transport Source: UniProtKB-KW

    Keywords - Molecular functioni

    Photoreceptor protein, Receptor, Retinal protein

    Keywords - Biological processi

    Hydrogen ion transport, Ion transport, Transport

    Keywords - Ligandi

    Chromophore

    Protein family/group databases

    TCDBi3.E.1.1.1. the ion-translocating microbial rhodopsin (mr) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bacteriorhodopsin
    Short name:
    BR
    Alternative name(s):
    Bacterioopsin
    Short name:
    BO
    Gene namesi
    Name:bop
    Ordered Locus Names:VNG_1467G
    OrganismiHalobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium)
    Taxonomic identifieri64091 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHalobacterium
    ProteomesiUP000000554: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 13133 PublicationsPRO_0000020246Add
    BLAST
    Chaini14 – 262249BacteriorhodopsinPRO_0000020247Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei14 – 141Pyrrolidone carboxylic acid1 Publication
    Modified residuei229 – 2291N6-(retinylidene)lysine

    Post-translational modificationi

    The covalent binding of retinal to the apoprotein, bacterioopsin, generates bacteriorhodopsin.

    Keywords - PTMi

    Pyrrolidone carboxylic acid

    Proteomic databases

    PaxDbiP02945.
    PRIDEiP02945.

    Interactioni

    Subunit structurei

    Homotrimer.

    Protein-protein interaction databases

    DIPiDIP-59007N.
    STRINGi64091.VNG1467G.

    Structurei

    Secondary structure

    1
    262
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni19 – 224
    Helixi23 – 4321
    Turni44 – 463
    Helixi50 – 7425
    Turni75 – 784
    Beta strandi80 – 845
    Beta strandi87 – 915
    Helixi94 – 11320
    Helixi118 – 14023
    Helixi144 – 16724
    Helixi168 – 1736
    Beta strandi174 – 1774
    Helixi178 – 20427
    Turni206 – 2094
    Beta strandi210 – 2123
    Helixi214 – 23825
    Helixi240 – 2423

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AP9X-ray2.35A14-261[»]
    1AT9X-ray3.00A15-261[»]
    1BACmodel-A14-261[»]
    1BADmodel-A14-261[»]
    1BCTNMR-A176-244[»]
    1BHANMR-A14-84[»]
    1BHBNMR-A14-84[»]
    1BM1X-ray3.50A15-261[»]
    1BRDelectron microscopy-A15-261[»]
    1BRRX-ray2.90A/B/C15-261[»]
    1BRXX-ray2.30A15-261[»]
    1C3WX-ray1.55A18-244[»]
    1C8RX-ray1.80A14-262[»]
    1C8SX-ray2.00A18-235[»]
    1CWQX-ray2.25A/B14-261[»]
    1DZEX-ray2.50A14-261[»]
    1E0PX-ray2.10A18-245[»]
    1F4ZX-ray1.80A18-244[»]
    1F50X-ray1.70A18-244[»]
    1FBBX-ray3.20A14-261[»]
    1FBKX-ray3.20A14-261[»]
    1IW6X-ray2.30A14-261[»]
    1IW9X-ray2.50A14-261[»]
    1IXFX-ray2.60A14-261[»]
    1JV6X-ray2.00A14-262[»]
    1JV7X-ray2.25A14-262[»]
    1KG8X-ray2.00A14-244[»]
    1KG9X-ray1.81A14-244[»]
    1KGBX-ray1.65A14-244[»]
    1KMEX-ray2.00A/B14-244[»]
    1L0MNMR-A20-231[»]
    1M0KX-ray1.43A1-262[»]
    1M0LX-ray1.47A1-262[»]
    1M0MX-ray1.43A1-262[»]
    1MGYX-ray2.00A14-262[»]
    1O0AX-ray1.62A14-262[»]
    1P8HX-ray1.52A14-262[»]
    1P8IX-ray1.86A14-262[»]
    1P8UX-ray1.62A14-262[»]
    1PXRX-ray1.70A/B14-262[»]
    1PXSX-ray2.20A/B14-262[»]
    1PY6X-ray1.80A/B14-262[»]
    1Q5IX-ray2.30A/B14-262[»]
    1Q5JX-ray2.10A/B14-262[»]
    1QHJX-ray1.90A14-261[»]
    1QKOX-ray2.10A14-261[»]
    1QKPX-ray2.10A14-261[»]
    1QM8X-ray2.50A14-261[»]
    1R2NNMR-A14-262[»]
    1R84NMR-A14-245[»]
    1S51X-ray2.00A/B18-244[»]
    1S52X-ray2.30A/B18-244[»]
    1S53X-ray2.00A/B18-244[»]
    1S54X-ray2.20A/B18-244[»]
    1S8JX-ray2.30A14-262[»]
    1S8LX-ray2.30A14-262[»]
    1TN0X-ray2.50A/B14-262[»]
    1TN5X-ray2.20A/B14-262[»]
    1UCQX-ray2.40A14-262[»]
    1VJMX-ray2.30A14-262[»]
    1X0IX-ray2.30114-261[»]
    1X0KX-ray2.60114-261[»]
    1X0SX-ray2.50A14-261[»]
    1XJIX-ray2.20A15-261[»]
    2AT9electron microscopy3.00A15-261[»]
    2BRDX-ray3.50A15-261[»]
    2I1XX-ray2.00A14-262[»]
    2I20X-ray2.08A14-262[»]
    2I21X-ray1.84A14-262[»]
    2NTUX-ray1.53A14-262[»]
    2NTWX-ray1.53A14-262[»]
    2WJKX-ray2.30A14-262[»]
    2WJLX-ray2.15A14-262[»]
    2ZFEX-ray2.50A1-262[»]
    2ZZLX-ray2.03A1-262[»]
    3COCX-ray2.31A/B14-262[»]
    3CODX-ray2.70A/B14-262[»]
    3HANX-ray2.75A14-262[»]
    3HAOX-ray2.49A/B14-262[»]
    3HAPX-ray1.60A14-262[»]
    3HAQX-ray2.30A14-262[»]
    3HARX-ray1.70A14-262[»]
    3HASX-ray1.90A14-262[»]
    3MBVX-ray2.00A14-261[»]
    3NS0X-ray1.78A14-261[»]
    3NSBX-ray1.78A14-261[»]
    3T45X-ray3.01A/B/C20-244[»]
    3UTVX-ray2.06A14-262[»]
    3UTWX-ray2.40A14-262[»]
    3UTXX-ray2.47A/B14-262[»]
    3UTYX-ray2.37A/B14-262[»]
    3VHZX-ray2.30A1-262[»]
    3VI0X-ray2.30A1-262[»]
    4FPDX-ray2.65A1-262[»]
    4HWLX-ray2.00A/B1-262[»]
    4HYXX-ray1.99A/B1-262[»]
    ProteinModelPortaliP02945.
    SMRiP02945. Positions 15-252.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02945.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini14 – 2310Extracellular
    Topological domaini43 – 5614CytoplasmicAdd
    BLAST
    Topological domaini76 – 9116ExtracellularAdd
    BLAST
    Topological domaini110 – 12011CytoplasmicAdd
    BLAST
    Topological domaini141 – 1477Extracellular
    Topological domaini168 – 18518CytoplasmicAdd
    BLAST
    Topological domaini205 – 21612ExtracellularAdd
    BLAST
    Topological domaini237 – 26226CytoplasmicAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei24 – 4219Helical; Name=Helix AAdd
    BLAST
    Transmembranei57 – 7519Helical; Name=Helix BAdd
    BLAST
    Transmembranei92 – 10918Helical; Name=Helix CAdd
    BLAST
    Transmembranei121 – 14020Helical; Name=Helix DAdd
    BLAST
    Transmembranei148 – 16720Helical; Name=Helix EAdd
    BLAST
    Transmembranei186 – 20419Helical; Name=Helix FAdd
    BLAST
    Transmembranei217 – 23620Helical; Name=Helix GAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5524.
    KOiK04641.
    OMAiQTHRLFH.
    PhylomeDBiP02945.

    Family and domain databases

    Gene3Di1.20.1070.10. 1 hit.
    InterProiIPR001425. Arc/bac/fun_rhod.
    IPR017452. GPCR_Rhodpsn_7TM.
    IPR018229. Rhodopsin_retinal_BS.
    [Graphical view]
    PRINTSiPR00251. BACTRLOPSIN.
    PROSITEiPS00950. BACTERIAL_OPSIN_1. 1 hit.
    PS00327. BACTERIAL_OPSIN_RET. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P02945-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLELLPTAVE GVSQAQITGR PEWIWLALGT ALMGLGTLYF LVKGMGVSDP    50
    DAKKFYAITT LVPAIAFTMY LSMLLGYGLT MVPFGGEQNP IYWARYADWL 100
    FTTPLLLLDL ALLVDADQGT ILALVGADGI MIGTGLVGAL TKVYSYRFVW 150
    WAISTAAMLY ILYVLFFGFT SKAESMRPEV ASTFKVLRNV TVVLWSAYPV 200
    VWLIGSEGAG IVPLNIETLL FMVLDVSAKV GFGLILLRSR AIFGEAEAPE 250
    PSAGDGAAAT SD 262
    Length:262
    Mass (Da):28,256
    Last modified:July 1, 1989 - v2
    Checksum:i38AC8A364C8C7F21
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti118 – 1181Q → E AA sequence 1 PublicationCurated
    Sequence conflicti124 – 1241L → I AA sequence 1 PublicationCurated
    Sequence conflicti130 – 1301I → L AA sequence 1 PublicationCurated
    Sequence conflicti151 – 1511Missing AA sequence 1 PublicationCurated
    Sequence conflicti159 – 1591L → S AA sequence 1 PublicationCurated
    Sequence conflicti219 – 2191L → A AA sequence 1 PublicationCurated

    Mass spectrometryi

    Molecular mass is 27052.5±2.7 Da from positions 14 - 261. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00474 Genomic DNA. Translation: CAA23744.1.
    M11720 Genomic DNA. Translation: AAA72504.1.
    X70293 Genomic DNA. Translation: CAA49774.1.
    AE004437 Genomic DNA. Translation: AAG19772.1.
    PIRiA93898. RAHSB.
    H84300.
    RefSeqiNP_280292.1. NC_002607.1.
    WP_010903069.1. NC_002607.1.

    Genome annotation databases

    EnsemblBacteriaiAAG19772; AAG19772; VNG_1467G.
    GeneIDi1448071.
    KEGGihal:VNG1467G.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00474 Genomic DNA. Translation: CAA23744.1 .
    M11720 Genomic DNA. Translation: AAA72504.1 .
    X70293 Genomic DNA. Translation: CAA49774.1 .
    AE004437 Genomic DNA. Translation: AAG19772.1 .
    PIRi A93898. RAHSB.
    H84300.
    RefSeqi NP_280292.1. NC_002607.1.
    WP_010903069.1. NC_002607.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AP9 X-ray 2.35 A 14-261 [» ]
    1AT9 X-ray 3.00 A 15-261 [» ]
    1BAC model - A 14-261 [» ]
    1BAD model - A 14-261 [» ]
    1BCT NMR - A 176-244 [» ]
    1BHA NMR - A 14-84 [» ]
    1BHB NMR - A 14-84 [» ]
    1BM1 X-ray 3.50 A 15-261 [» ]
    1BRD electron microscopy - A 15-261 [» ]
    1BRR X-ray 2.90 A/B/C 15-261 [» ]
    1BRX X-ray 2.30 A 15-261 [» ]
    1C3W X-ray 1.55 A 18-244 [» ]
    1C8R X-ray 1.80 A 14-262 [» ]
    1C8S X-ray 2.00 A 18-235 [» ]
    1CWQ X-ray 2.25 A/B 14-261 [» ]
    1DZE X-ray 2.50 A 14-261 [» ]
    1E0P X-ray 2.10 A 18-245 [» ]
    1F4Z X-ray 1.80 A 18-244 [» ]
    1F50 X-ray 1.70 A 18-244 [» ]
    1FBB X-ray 3.20 A 14-261 [» ]
    1FBK X-ray 3.20 A 14-261 [» ]
    1IW6 X-ray 2.30 A 14-261 [» ]
    1IW9 X-ray 2.50 A 14-261 [» ]
    1IXF X-ray 2.60 A 14-261 [» ]
    1JV6 X-ray 2.00 A 14-262 [» ]
    1JV7 X-ray 2.25 A 14-262 [» ]
    1KG8 X-ray 2.00 A 14-244 [» ]
    1KG9 X-ray 1.81 A 14-244 [» ]
    1KGB X-ray 1.65 A 14-244 [» ]
    1KME X-ray 2.00 A/B 14-244 [» ]
    1L0M NMR - A 20-231 [» ]
    1M0K X-ray 1.43 A 1-262 [» ]
    1M0L X-ray 1.47 A 1-262 [» ]
    1M0M X-ray 1.43 A 1-262 [» ]
    1MGY X-ray 2.00 A 14-262 [» ]
    1O0A X-ray 1.62 A 14-262 [» ]
    1P8H X-ray 1.52 A 14-262 [» ]
    1P8I X-ray 1.86 A 14-262 [» ]
    1P8U X-ray 1.62 A 14-262 [» ]
    1PXR X-ray 1.70 A/B 14-262 [» ]
    1PXS X-ray 2.20 A/B 14-262 [» ]
    1PY6 X-ray 1.80 A/B 14-262 [» ]
    1Q5I X-ray 2.30 A/B 14-262 [» ]
    1Q5J X-ray 2.10 A/B 14-262 [» ]
    1QHJ X-ray 1.90 A 14-261 [» ]
    1QKO X-ray 2.10 A 14-261 [» ]
    1QKP X-ray 2.10 A 14-261 [» ]
    1QM8 X-ray 2.50 A 14-261 [» ]
    1R2N NMR - A 14-262 [» ]
    1R84 NMR - A 14-245 [» ]
    1S51 X-ray 2.00 A/B 18-244 [» ]
    1S52 X-ray 2.30 A/B 18-244 [» ]
    1S53 X-ray 2.00 A/B 18-244 [» ]
    1S54 X-ray 2.20 A/B 18-244 [» ]
    1S8J X-ray 2.30 A 14-262 [» ]
    1S8L X-ray 2.30 A 14-262 [» ]
    1TN0 X-ray 2.50 A/B 14-262 [» ]
    1TN5 X-ray 2.20 A/B 14-262 [» ]
    1UCQ X-ray 2.40 A 14-262 [» ]
    1VJM X-ray 2.30 A 14-262 [» ]
    1X0I X-ray 2.30 1 14-261 [» ]
    1X0K X-ray 2.60 1 14-261 [» ]
    1X0S X-ray 2.50 A 14-261 [» ]
    1XJI X-ray 2.20 A 15-261 [» ]
    2AT9 electron microscopy 3.00 A 15-261 [» ]
    2BRD X-ray 3.50 A 15-261 [» ]
    2I1X X-ray 2.00 A 14-262 [» ]
    2I20 X-ray 2.08 A 14-262 [» ]
    2I21 X-ray 1.84 A 14-262 [» ]
    2NTU X-ray 1.53 A 14-262 [» ]
    2NTW X-ray 1.53 A 14-262 [» ]
    2WJK X-ray 2.30 A 14-262 [» ]
    2WJL X-ray 2.15 A 14-262 [» ]
    2ZFE X-ray 2.50 A 1-262 [» ]
    2ZZL X-ray 2.03 A 1-262 [» ]
    3COC X-ray 2.31 A/B 14-262 [» ]
    3COD X-ray 2.70 A/B 14-262 [» ]
    3HAN X-ray 2.75 A 14-262 [» ]
    3HAO X-ray 2.49 A/B 14-262 [» ]
    3HAP X-ray 1.60 A 14-262 [» ]
    3HAQ X-ray 2.30 A 14-262 [» ]
    3HAR X-ray 1.70 A 14-262 [» ]
    3HAS X-ray 1.90 A 14-262 [» ]
    3MBV X-ray 2.00 A 14-261 [» ]
    3NS0 X-ray 1.78 A 14-261 [» ]
    3NSB X-ray 1.78 A 14-261 [» ]
    3T45 X-ray 3.01 A/B/C 20-244 [» ]
    3UTV X-ray 2.06 A 14-262 [» ]
    3UTW X-ray 2.40 A 14-262 [» ]
    3UTX X-ray 2.47 A/B 14-262 [» ]
    3UTY X-ray 2.37 A/B 14-262 [» ]
    3VHZ X-ray 2.30 A 1-262 [» ]
    3VI0 X-ray 2.30 A 1-262 [» ]
    4FPD X-ray 2.65 A 1-262 [» ]
    4HWL X-ray 2.00 A/B 1-262 [» ]
    4HYX X-ray 1.99 A/B 1-262 [» ]
    ProteinModelPortali P02945.
    SMRi P02945. Positions 15-252.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-59007N.
    STRINGi 64091.VNG1467G.

    Protein family/group databases

    TCDBi 3.E.1.1.1. the ion-translocating microbial rhodopsin (mr) family.

    Proteomic databases

    PaxDbi P02945.
    PRIDEi P02945.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAG19772 ; AAG19772 ; VNG_1467G .
    GeneIDi 1448071.
    KEGGi hal:VNG1467G.

    Phylogenomic databases

    eggNOGi COG5524.
    KOi K04641.
    OMAi QTHRLFH.
    PhylomeDBi P02945.

    Miscellaneous databases

    EvolutionaryTracei P02945.

    Family and domain databases

    Gene3Di 1.20.1070.10. 1 hit.
    InterProi IPR001425. Arc/bac/fun_rhod.
    IPR017452. GPCR_Rhodpsn_7TM.
    IPR018229. Rhodopsin_retinal_BS.
    [Graphical view ]
    PRINTSi PR00251. BACTRLOPSIN.
    PROSITEi PS00950. BACTERIAL_OPSIN_1. 1 hit.
    PS00327. BACTERIAL_OPSIN_RET. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: R1 / S9.
    2. "Studies on the light-transducing pigment bacteriorhodopsin."
      Dunn R.J., Hackett N.R., Huang K.-S., Jones S., Khorana H.G., Lee D.-S., Liao M.-J., Lo K.-M., McCoy J., Noguchi S., Radhakrishnan R., RajBhandary U.L.
      Cold Spring Harb. Symp. Quant. Biol. 48:853-862(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Bacterioopsin, haloopsin, and sensory opsin I of the halobacterial isolate Halobacterium sp. strain SG1: three new members of a growing family."
      Soppa J., Duschl J., Oesterhelt D.
      J. Bacteriol. 175:2720-2726(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: SG1.
    4. "Bacteriorhodopsin precursor. Characterization and its integration into the purple membrane."
      Seehra J.S., Khorana H.G.
      J. Biol. Chem. 259:4187-4193(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700922 / JCM 11081 / NRC-1.
    6. "The amino acid sequence of bacteriorhodopsin."
      Ovchinnikov Y.A., Abdulaev N.G., Feigina M.Y., Kiselev A.V., Lobanov N.A., Nasimov I.V.
      Bioorg. Khim. 4:1573-1574(1978)
      Cited for: PROTEIN SEQUENCE OF 14-261.
    7. Cited for: PROTEIN SEQUENCE OF 14-261.
    8. "Mass spectrometric analysis of integral membrane proteins: application to complete mapping of bacteriorhodopsins and rhodopsin."
      Ball L.E., Oatis J.E. Jr., Dharmasiri K., Busman M., Wang J., Cowden L.B., Galijatovic A., Chen N., Crouch R.K., Knapp D.R.
      Protein Sci. 7:758-764(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 14-248, PYROGLUTAMATE FORMATION AT GLN-14.
    9. Cited for: RETINAL-BINDING SITE.
    10. "Electrospray-ionization mass spectrometry of intact intrinsic membrane proteins."
      Whitelegge J.P., Gundersen C.B., Faull K.F.
      Protein Sci. 7:1423-1430(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: MASS SPECTROMETRY.
    11. "Bicelle crystallization: a new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure."
      Faham S., Bowie J.U.
      J. Mol. Biol. 316:1-6(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 14-244.
    12. "Tertiary structure of bacteriorhodopsin. Positions and orientations of helices A and B in the structural map determined by neutron diffraction."
      Popot J.-L., Engleman D.M., Gurel O., Zaccai G.
      J. Mol. Biol. 210:829-847(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NEUTRON DIFFRACTION.
    13. "Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy."
      Henderson R., Baldwin J.M., Ceska T.A., Zemlin F., Beckmann E., Downing K.H.
      J. Mol. Biol. 213:899-929(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.5 ANGSTROMS) OF 15-261.
    14. "Electron-crystallographic refinement of the structure of bacteriorhodopsin."
      Grigorieff N., Ceska T.A., Downing K.H., Baldwin J.M., Henderson R.
      J. Mol. Biol. 259:393-421(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.5 ANGSTROMS) OF 14-260.
    15. "Three-dimensional structure of proteolytic fragment 163-231 of bacterioopsin determined from nuclear magnetic resonance data in solution."
      Barsukov I.L., Nolde D.E., Lomize A.L., Arseniev A.S.
      Eur. J. Biochem. 206:665-672(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 176-244.
    16. "1H-15N-NMR studies of bacteriorhodopsin Halobacterium halobium. Conformational dynamics of the four-helical bundle."
      Orekhov V.Y., Abdulaeva G.V., Musina L.Y., Arseniev A.S.
      Eur. J. Biochem. 210:223-229(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-231.
    17. "Surface of bacteriorhodopsin revealed by high-resolution electron crystallography."
      Kimura Y., Vassylyev D.G., Miyazawa A., Kidera A., Matsushima M., Mitsuoka K., Murata K., Hirai T., Fujiyoshi Y.
      Nature 389:206-211(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) OF 15-244.
    18. "X-ray structure of bacteriorhodopsin at 2.5-A from microcrystals grown in lipidic cubic phases."
      Pebay-Peyroula E., Rummel G., Rosenbusch J.P., Landau E.M.
      Science 277:1676-1681(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 20-238.
    19. "Lipid patches in membrane protein oligomers: crystal structure of the bacteriorhodopsin-lipid complex."
      Essen L.-O., Siegert R., Lehmann W.D., Oesterhelt D.
      Proc. Natl. Acad. Sci. U.S.A. 95:11673-11678(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 15-245.
    20. "Proton transfer pathways in bacteriorhodopsin at 2.3 Angstrom resolution."
      Luecke H., Richter H.-T., Lanyi J.K.
      Science 280:1934-1937(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 19-165.
    21. Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 18-244.
    22. "High-resolution X-ray structure of an early intermediate in the bacteriorhodopsin photocycle."
      Edman K., Nollert P., Royant A., Belrhali H., Pebay-Peyroula E., Hajdu J., Neutze R., Landau E.M.
      Nature 401:822-826(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 18-245.
    23. "Protein, lipid and water organization in bacteriorhodopsin crystals: a molecular view of the purple membrane at 1.9 A resolution."
      Belrhali H., Nollert P., Royant A., Menzel C., Rosenbusch J.P., Landau E.M., Pebay-Peyroula E.
      Structure 7:909-917(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 14-261.
    24. "Coupling photoisomerization of retinal to directional transport in bacteriorhodopsin."
      Luecke H., Schobert B., Cartailler J.-P., Richter H.T., Rosengarth A., Needleman R., Lanyi J.K.
      J. Mol. Biol. 300:1237-1255(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 18-245.
    25. "Helix deformation is coupled to vectorial proton transport in the photocycle of bacteriorhodopsin."
      Royant A., Edman K., Ursby T., Pebay-Peyroula E., Landau E.M., Neutze R.
      Nature 406:645-648(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 18-245.
    26. "Molecular mechanism of vectorial proton translocation by bacteriorhodopsin."
      Subramaniam S., Henderson R.
      Nature 406:653-657(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 14-262.

    Entry informationi

    Entry nameiBACR_HALSA
    AccessioniPrimary (citable) accession number: P02945
    Secondary accession number(s): Q9HPU5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 157 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. 7-transmembrane G-linked receptors
      List of 7-transmembrane G-linked receptor entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3