Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P02945 (BACR_HALSA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bacteriorhodopsin

Short name=BR
Alternative name(s):
Bacterioopsin
Short name=BO
Gene names
Name:bop
Ordered Locus Names:VNG_1467G
OrganismHalobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium) [Reference proteome] [HAMAP]
Taxonomic identifier64091 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHalobacterium

Protein attributes

Sequence length262 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Light-driven proton pump.

Subunit structure

Homotrimer.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Post-translational modification

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

Sequence similarities

Belongs to the archaeal/bacterial/fungal opsin family.

Mass spectrometry

Molecular mass is 27052.5±2.7 Da from positions 14 - 261. Determined by ESI. Ref.10

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 1313
PRO_0000020246
Chain14 – 262249Bacteriorhodopsin
PRO_0000020247

Regions

Topological domain14 – 2310Extracellular
Transmembrane24 – 4219Helical; Name=Helix A
Topological domain43 – 5614Cytoplasmic
Transmembrane57 – 7519Helical; Name=Helix B
Topological domain76 – 9116Extracellular
Transmembrane92 – 10918Helical; Name=Helix C
Topological domain110 – 12011Cytoplasmic
Transmembrane121 – 14020Helical; Name=Helix D
Topological domain141 – 1477Extracellular
Transmembrane148 – 16720Helical; Name=Helix E
Topological domain168 – 18518Cytoplasmic
Transmembrane186 – 20419Helical; Name=Helix F
Topological domain205 – 21612Extracellular
Transmembrane217 – 23620Helical; Name=Helix G
Topological domain237 – 26226Cytoplasmic

Sites

Site981Primary proton acceptor

Amino acid modifications

Modified residue141Pyrrolidone carboxylic acid
Modified residue2291N6-(retinylidene)lysine

Experimental info

Sequence conflict1181Q → E AA sequence Ref.6
Sequence conflict1241L → I AA sequence Ref.6
Sequence conflict1301I → L AA sequence Ref.6
Sequence conflict1511Missing AA sequence Ref.6
Sequence conflict1591L → S AA sequence Ref.6
Sequence conflict2191L → A AA sequence Ref.6

Secondary structure

............................ 262
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02945 [UniParc].

Last modified July 1, 1989. Version 2.
Checksum: 38AC8A364C8C7F21

FASTA26228,256
        10         20         30         40         50         60 
MLELLPTAVE GVSQAQITGR PEWIWLALGT ALMGLGTLYF LVKGMGVSDP DAKKFYAITT 

        70         80         90        100        110        120 
LVPAIAFTMY LSMLLGYGLT MVPFGGEQNP IYWARYADWL FTTPLLLLDL ALLVDADQGT 

       130        140        150        160        170        180 
ILALVGADGI MIGTGLVGAL TKVYSYRFVW WAISTAAMLY ILYVLFFGFT SKAESMRPEV 

       190        200        210        220        230        240 
ASTFKVLRNV TVVLWSAYPV VWLIGSEGAG IVPLNIETLL FMVLDVSAKV GFGLILLRSR 

       250        260 
AIFGEAEAPE PSAGDGAAAT SD 

« Hide

References

« Hide 'large scale' references
[1]"The bacteriorhodopsin gene."
Dunn R.J., McCoy J., Simsek M., Majumdar A., Chang S.H., RajBhandary U.L., Khorana H.G.
Proc. Natl. Acad. Sci. U.S.A. 78:6744-6748(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 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]"Genome sequence of Halobacterium species NRC-1."
Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D., Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D., Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K. expand/collapse author list , Cruz R., Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P., Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M., Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J., Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L., DasSarma S.
Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000) [PubMed] [Europe PMC] [Abstract]
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]"Amino acid sequence of bacteriorhodopsin."
Khorana H.G., Gerber G.E., Herlihy W.C., Gray C.P., Anderegg R.J., Nihei K., Biemann K.
Proc. Natl. Acad. Sci. U.S.A. 76:5046-5050(1979) [PubMed] [Europe PMC] [Abstract]
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]"Attachment site(s) of retinal in bacteriorhodopsin."
Katre N.V., Wolber P.K., Stoeckenius W., Stroud R.M.
Proc. Natl. Acad. Sci. U.S.A. 78:4068-4072(1981) [PubMed] [Europe PMC] [Abstract]
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]"Structure of bacteriorhodopsin at 1.55-A resolution."
Luecke H., Schobert B., Richter H.-T., Cartailler J.-P., Lanyi J.K.
J. Mol. Biol. 291:899-911(1999) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V00474 Genomic DNA. Translation: CAA23744.1.
M11720 Genomic DNA. Translation: AAA72504.1.
X70293 Genomic DNA. Translation: CAA49774.1.
AE004437 Genomic DNA. Translation: AAG19772.1.
PIRRAHSB. A93898.
H84300.
RefSeqNP_280292.1. NC_002607.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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-ray3.50A15-253[»]
1BRDelectron microscopy-A15-261[»]
1BRRX-ray2.90A/B/C15-253[»]
1BRXX-ray2.30A15-261[»]
1C3WX-ray1.55A18-244[»]
1C8RX-ray1.80A14-262[»]
1C8SX-ray2.00A18-235[»]
1CWQX-ray2.25A/B14-253[»]
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-ray2.00A14-243[»]
1KG9X-ray1.81A14-243[»]
1KGBX-ray1.65A14-243[»]
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[»]
2AT9X-ray3.00A15-253[»]
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[»]
ProteinModelPortalP02945.
SMRP02945. Positions 15-252.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-59007N.
STRING64091.VNG1467G.

Protein family/group databases

TCDB3.E.1.1.1. the ion-translocating microbial rhodopsin (mr) family.

Proteomic databases

PaxDbP02945.
PRIDEP02945.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG19772; AAG19772; VNG_1467G.
GeneID1448071.
KEGGhal:VNG1467G.

Phylogenomic databases

eggNOGCOG5524.
KOK04641.
OMALWHAPRA.
PhylomeDBP02945.
ProtClustDBCLSK511428.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR017452. GPCR_Rhodpsn_7TM.
IPR001425. Rhodopsin_arc/bac/fun.
IPR018229. Rhodopsin_retinal_BS.
[Graphical view]
PfamPF01036. Bac_rhodopsin. 1 hit.
[Graphical view]
PRINTSPR00251. BACTRLOPSIN.
SMARTSM01021. Bac_rhodopsin. 1 hit.
[Graphical view]
PROSITEPS00950. BACTERIAL_OPSIN_1. 1 hit.
PS00327. BACTERIAL_OPSIN_RET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP02945.

Entry information

Entry nameBACR_HALSA
AccessionPrimary (citable) accession number: P02945
Secondary accession number(s): Q9HPU5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1989
Last modified: April 16, 2014
This is version 153 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries