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P02945

- BACR_HALSA

UniProt

P02945 - BACR_HALSA

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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

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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini14 – 2310Extracellular
Transmembranei24 – 4219Helical; Name=Helix AAdd
BLAST
Topological domaini43 – 5614CytoplasmicAdd
BLAST
Transmembranei57 – 7519Helical; Name=Helix BAdd
BLAST
Topological domaini76 – 9116ExtracellularAdd
BLAST
Transmembranei92 – 10918Helical; Name=Helix CAdd
BLAST
Topological domaini110 – 12011CytoplasmicAdd
BLAST
Transmembranei121 – 14020Helical; Name=Helix DAdd
BLAST
Topological domaini141 – 1477Extracellular
Transmembranei148 – 16720Helical; Name=Helix EAdd
BLAST
Topological domaini168 – 18518CytoplasmicAdd
BLAST
Transmembranei186 – 20419Helical; Name=Helix FAdd
BLAST
Topological domaini205 – 21612ExtracellularAdd
BLAST
Transmembranei217 – 23620Helical; Name=Helix GAdd
BLAST
Topological domaini237 – 26226CytoplasmicAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

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 – 224Combined sources
Helixi23 – 4321Combined sources
Turni44 – 463Combined sources
Helixi50 – 7425Combined sources
Turni75 – 784Combined sources
Beta strandi80 – 845Combined sources
Beta strandi87 – 915Combined sources
Helixi94 – 11320Combined sources
Helixi118 – 14023Combined sources
Helixi144 – 16724Combined sources
Helixi168 – 1736Combined sources
Beta strandi174 – 1774Combined sources
Helixi178 – 20427Combined sources
Turni206 – 2094Combined sources
Beta strandi210 – 2123Combined sources
Helixi214 – 23825Combined sources
Helixi240 – 2423Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4MD1X-ray1.73A14-261[»]
4MD2X-ray1.73A14-261[»]
4OV0X-ray2.00A14-262[»]
ProteinModelPortaliP02945.
SMRiP02945. Positions 15-252.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02945.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5524.
InParanoidiP02945.
KOiK04641.
OMAiQTHRLFH.
PhylomeDBiP02945.

Family and domain databases

Gene3Di1.20.1070.10. 1 hit.
InterProiIPR001425. Arc/bac/fun_rhod.
IPR029730. Arc/bac/fun_rhod-like.
IPR017452. GPCR_Rhodpsn_7TM.
IPR018229. Rhodopsin_retinal_BS.
[Graphical view]
PfamiPF01036. Bac_rhodopsin. 1 hit.
[Graphical view]
PRINTSiPR00251. BACTRLOPSIN.
SMARTiSM01021. Bac_rhodopsin. 1 hit.
[Graphical view]
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

        10         20         30         40         50
MLELLPTAVE GVSQAQITGR PEWIWLALGT ALMGLGTLYF LVKGMGVSDP
60 70 80 90 100
DAKKFYAITT LVPAIAFTMY LSMLLGYGLT MVPFGGEQNP IYWARYADWL
110 120 130 140 150
FTTPLLLLDL ALLVDADQGT ILALVGADGI MIGTGLVGAL TKVYSYRFVW
160 170 180 190 200
WAISTAAMLY ILYVLFFGFT SKAESMRPEV ASTFKVLRNV TVVLWSAYPV
210 220 230 240 250
VWLIGSEGAG IVPLNIETLL FMVLDVSAKV GFGLILLRSR AIFGEAEAPE
260
PSAGDGAAAT SD
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 [» ]
4MD1 X-ray 1.73 A 14-261 [» ]
4MD2 X-ray 1.73 A 14-261 [» ]
4OV0 X-ray 2.00 A 14-262 [» ]
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.
InParanoidi P02945.
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.
IPR029730. Arc/bac/fun_rhod-like.
IPR017452. GPCR_Rhodpsn_7TM.
IPR018229. Rhodopsin_retinal_BS.
[Graphical view ]
Pfami PF01036. Bac_rhodopsin. 1 hit.
[Graphical view ]
PRINTSi PR00251. BACTRLOPSIN.
SMARTi SM01021. Bac_rhodopsin. 1 hit.
[Graphical view ]
PROSITEi PS00950. BACTERIAL_OPSIN_1. 1 hit.
PS00327. BACTERIAL_OPSIN_RET. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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: November 26, 2014
This is version 159 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