Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Sitei98Primary proton acceptor1

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)DescriptionActionsGraphical viewLength
Topological domaini14 – 23Extracellular10
Transmembranei24 – 42Helical; Name=Helix AAdd BLAST19
Topological domaini43 – 56CytoplasmicAdd BLAST14
Transmembranei57 – 75Helical; Name=Helix BAdd BLAST19
Topological domaini76 – 91ExtracellularAdd BLAST16
Transmembranei92 – 109Helical; Name=Helix CAdd BLAST18
Topological domaini110 – 120CytoplasmicAdd BLAST11
Transmembranei121 – 140Helical; Name=Helix DAdd BLAST20
Topological domaini141 – 147Extracellular7
Transmembranei148 – 167Helical; Name=Helix EAdd BLAST20
Topological domaini168 – 185CytoplasmicAdd BLAST18
Transmembranei186 – 204Helical; Name=Helix FAdd BLAST19
Topological domaini205 – 216ExtracellularAdd BLAST12
Transmembranei217 – 236Helical; Name=Helix GAdd BLAST20
Topological domaini237 – 262CytoplasmicAdd BLAST26

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000202461 – 133 PublicationsAdd BLAST13
ChainiPRO_000002024714 – 262BacteriorhodopsinAdd BLAST249

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei14Pyrrolidone carboxylic acid1 Publication1
Modified residuei229N6-(retinylidene)lysine1

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

1262
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni19 – 22Combined sources4
Helixi23 – 43Combined sources21
Turni44 – 46Combined sources3
Helixi50 – 74Combined sources25
Turni75 – 78Combined sources4
Beta strandi80 – 84Combined sources5
Beta strandi87 – 91Combined sources5
Helixi94 – 113Combined sources20
Helixi118 – 140Combined sources23
Helixi144 – 167Combined sources24
Helixi168 – 173Combined sources6
Beta strandi174 – 177Combined sources4
Helixi178 – 204Combined sources27
Turni206 – 209Combined sources4
Beta strandi210 – 212Combined sources3
Helixi214 – 238Combined sources25
Helixi240 – 242Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5BR2X-ray1.80A14-262[»]
5BR5X-ray2.00A14-262[»]
5J7AX-ray2.30A18-244[»]
ProteinModelPortaliP02945.
SMRiP02945.
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)DescriptionActionsGraphical viewLength
Sequence conflicti118Q → E AA sequence (Ref. 6) Curated1
Sequence conflicti124L → I AA sequence (Ref. 6) Curated1
Sequence conflicti130I → L AA sequence (Ref. 6) Curated1
Sequence conflicti151Missing AA sequence (Ref. 6) Curated1
Sequence conflicti159L → S AA sequence (Ref. 6) Curated1
Sequence conflicti219L → A AA sequence (Ref. 6) Curated1

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:VNG_1467G.

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
PDB 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[»]
5BR2X-ray1.80A14-262[»]
5BR5X-ray2.00A14-262[»]
5J7AX-ray2.30A18-244[»]
ProteinModelPortaliP02945.
SMRiP02945.
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:VNG_1467G.

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: November 30, 2016
This is version 171 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.