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Protein

Bacteriorhodopsin

Gene

bop

Organism
Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium)
Status
Reviewed-Annotation score: 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

GO - Biological processi

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
Proteomesi
  • UP000000554 Componenti: 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

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[»]
4X31X-ray2.40A18-246[»]
4X32X-ray1.90A18-245[»]
4XXJX-ray1.90A/B/C14-262[»]
5A44X-ray2.29A14-261[»]
5A45X-ray2.57A14-261[»]
ProteinModelPortaliP02945.
SMRiP02945. Positions 15-252.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02945.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiarCOG02812. Archaea.
COG5524. LUCA.
InParanoidiP02945.
KOiK04641.
OMAiHASVPFI.
PhylomeDBiP02945.

Family and domain databases

InterProiIPR001425. Arc/bac/fun_rhodopsins.
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 (Ref. 6) Curated
Sequence conflicti124 – 1241L → I AA sequence (Ref. 6) Curated
Sequence conflicti130 – 1301I → L AA sequence (Ref. 6) Curated
Sequence conflicti151 – 1511Missing AA sequence (Ref. 6) Curated
Sequence conflicti159 – 1591L → S AA sequence (Ref. 6) Curated
Sequence conflicti219 – 2191L → A AA sequence (Ref. 6) Curated

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.

Genome annotation databases

EnsemblBacteriaiAAG19772; AAG19772; VNG_1467G.
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.
PIRiA93898. RAHSB.
H84300.

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[»]
4X31X-ray2.40A18-246[»]
4X32X-ray1.90A18-245[»]
4XXJX-ray1.90A/B/C14-262[»]
5A44X-ray2.29A14-261[»]
5A45X-ray2.57A14-261[»]
ProteinModelPortaliP02945.
SMRiP02945. Positions 15-252.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59007N.
STRINGi64091.VNG1467G.

Protein family/group databases

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

Proteomic databases

PaxDbiP02945.
PRIDEiP02945.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG19772; AAG19772; VNG_1467G.
KEGGihal:VNG1467G.

Phylogenomic databases

eggNOGiarCOG02812. Archaea.
COG5524. LUCA.
InParanoidiP02945.
KOiK04641.
OMAiHASVPFI.
PhylomeDBiP02945.

Miscellaneous databases

EvolutionaryTraceiP02945.

Family and domain databases

InterProiIPR001425. Arc/bac/fun_rhodopsins.
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]
ProtoNetiSearch...

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: June 8, 2016
This is version 168 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.