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Protein

Bacteriorhodopsin

Gene

bop

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

Functioni

Light-driven proton pump.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei98Primary proton acceptor3 Publications1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionPhotoreceptor protein, Receptor, Retinal protein
Biological processHydrogen ion transport, Ion transport, Transport
LigandChromophore

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 – 22ExtracellularCombined sources2 Publications9
Transmembranei23 – 42Helical; Name=Helix ACombined sources2 PublicationsAdd BLAST20
Topological domaini43 – 56CytoplasmicCombined sources2 PublicationsAdd BLAST14
Transmembranei57 – 75Helical; Name=Helix BCombined sources2 PublicationsAdd BLAST19
Topological domaini76 – 92ExtracellularCombined sources2 PublicationsAdd BLAST17
Transmembranei93 – 109Helical; Name=Helix CCombined sources2 PublicationsAdd BLAST17
Topological domaini110 – 120CytoplasmicCombined sources2 PublicationsAdd BLAST11
Transmembranei121 – 140Helical; Name=Helix DCombined sources2 PublicationsAdd BLAST20
Topological domaini141 – 147ExtracellularCombined sources2 Publications7
Transmembranei148 – 167Helical; Name=Helix ECombined sources2 PublicationsAdd BLAST20
Topological domaini168 – 185CytoplasmicCombined sources2 PublicationsAdd BLAST18
Transmembranei186 – 204Helical; Name=Helix FCombined sources2 PublicationsAdd BLAST19
Topological domaini205 – 216ExtracellularCombined sources2 PublicationsAdd BLAST12
Transmembranei217 – 236Helical; Name=Helix GCombined sources2 PublicationsAdd BLAST20
Topological domaini237 – 262CytoplasmicCombined sources2 PublicationsAdd BLAST26

GO - Cellular componenti

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000202461 – 133 PublicationsAdd BLAST13
ChainiPRO_000002024714 – 262Bacteriorhodopsin2 PublicationsAdd BLAST249

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei14Pyrrolidone carboxylic acid1 Publication1
Modified residuei229N6-(retinylidene)lysineCombined sources12 Publications1

Post-translational modificationi

The covalent binding of retinal to the apoprotein, bacterioopsin, generates bacteriorhodopsin.13 Publications

Keywords - PTMi

Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiP02945

Interactioni

Subunit structurei

Homotrimer.5 Publications

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 – 176Combined sources3
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[»]
5B34X-ray2.10A14-262[»]
5B35X-ray2.35A14-262[»]
5B6VX-ray2.00A14-261[»]
5B6WX-ray2.10A14-261[»]
5B6XX-ray2.10A14-261[»]
5B6YX-ray2.10A14-261[»]
5B6ZX-ray2.10A14-261[»]
5BR2X-ray1.80A14-262[»]
5BR5X-ray2.00A14-262[»]
5H2HX-ray2.10A14-261[»]
5H2IX-ray2.10A14-261[»]
5H2JX-ray2.10A14-261[»]
5H2KX-ray2.10A14-261[»]
5H2LX-ray2.10A14-261[»]
5H2MX-ray2.10A14-261[»]
5H2NX-ray2.10A14-261[»]
5H2OX-ray2.10A14-261[»]
5H2PX-ray2.10A14-261[»]
5J7AX-ray2.30A18-244[»]
5VN7X-ray2.70A/B1-262[»]
5VN9X-ray2.59A/B1-262[»]
ProteinModelPortaliP02945
SMRiP02945
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02945

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiarCOG02812 Archaea
COG5524 LUCA
InParanoidiP02945
KOiK04641
OMAiRIFHYIT
OrthoDBiPOG093Z092V
PhylomeDBiP02945

Family and domain databases

InterProiView protein in InterPro
IPR001425 Arc/bac/fun_rhodopsins
IPR018229 Rhodopsin_retinal_BS
PANTHERiPTHR28286 PTHR28286, 1 hit
PfamiView protein in Pfam
PF01036 Bac_rhodopsin, 1 hit
PRINTSiPR00251 BACTRLOPSIN
SMARTiView protein in SMART
SM01021 Bac_rhodopsin, 1 hit
PROSITEiView protein in PROSITE
PS00950 BACTERIAL_OPSIN_1, 1 hit
PS00327 BACTERIAL_OPSIN_RET, 1 hit

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
PATRICifig|64091.14.peg.1122

Similar proteinsi

Entry informationi

Entry nameiBACR_HALSA
AccessioniPrimary (citable) accession number: P02945
Secondary accession number(s): Q9HPU5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1989
Last modified: May 23, 2018
This is version 178 of the entry and version 2 of the sequence. See 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

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