bop

Functionⁱ

Light-driven proton pump.3 Publications

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Siteⁱ	98	Primary proton acceptor3 Publications		1

GO - Molecular functionⁱ

ion channel activity Source: InterPro
photoreceptor activity Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

phototransduction Source: UniProtKB-KW
protein-chromophore linkage Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Photoreceptor protein, Receptor, Retinal protein
Biological process	Hydrogen ion transport, Ion transport, Transport
Ligand	Chromophore

Protein family/group databases

TCDBⁱ	3.E.1.1.1 the ion-translocating microbial rhodopsin (mr) family

TCDBⁱ

3.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
Organismⁱ	Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium)
Taxonomic identifierⁱ	64091 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Archaea › Euryarchaeota › Stenosarchaea group › Halobacteria › Halobacteriales › Halobacteriaceae › Halobacterium › Halobacterium salinarum
Proteomesⁱ	UP000000554 Componentⁱ: Chromosome

Subcellular locationⁱ

Cell membrane
1 Publication
Manual assertion based on experiment inⁱ
- Ref.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, SUBCELLULAR LOCATION, TOPOLOGY, RETINAL BINDING.
; Multi-pass membrane protein
12 Publications
Manual assertion based on experiment inⁱ
- Ref.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, SUBCELLULAR LOCATION, TOPOLOGY, RETINAL BINDING.
- Ref.11
  "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, SUBUNIT, TOPOLOGY.
- Ref.17
  "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 14-261 IN COMPLEX WITH ALL-TRANS-RETINAL, SUBUNIT, TOPOLOGY.
- Ref.18
  "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 14-261 IN COMPLEX WITH ALL-TRANS-RETINAL, SUBUNIT, TOPOLOGY.
- Ref.19
  "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 14-261 IN COMPLEX WITH ALL-TRANS-RETINAL, SUBUNIT, TOPOLOGY.
- Ref.20
  "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 IN COMPLEX WITH ALL-TRANS-RETINAL, SUBUNIT, TOPOLOGY.
- Ref.21
  "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 (2.10 ANGSTROMS) OF 14-261 IN COMPLEX WITH ALL-TRANS-RETINAL, TOPOLOGY.
- Ref.22
  "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 IN COMPLEX WITH ALL-TRANS-RETINAL, TOPOLOGY.
- Ref.23
  "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 IN COMPLEX WITH ALL-TRANS-RETINAL, FUNCTION, TOPOLOGY.
- Ref.25
  "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 14-261 IN COMPLEX WITH ALL-TRANS-RETINAL, FUNCTION, TOPOLOGY.
- Ref.26
  "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 IN COMPLEX WITH ALL-TRANS-RETINAL, TOPOLOGY.
- Ref.27
  "A three-dimensional movie of structural changes in bacteriorhodopsin."
  Nango E., Royant A., Kubo M., Nakane T., Wickstrand C., Kimura T., Tanaka T., Tono K., Song C., Tanaka R., Arima T., Yamashita A., Kobayashi J., Hosaka T., Mizohata E., Nogly P., Sugahara M., Nam D.
  Iwata S.
  Science 354:1552-1557(2016) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 14-261 IN COMPLEX WITH ALL-TRANS-RETINAL, TOPOLOGY, FUNCTION.

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	14 – 22	ExtracellularCombined sources2 Publications	9
Transmembraneⁱ	23 – 42	Helical; Name=Helix ACombined sources2 PublicationsAdd BLAST	20
Topological domainⁱ	43 – 56	CytoplasmicCombined sources2 PublicationsAdd BLAST	14
Transmembraneⁱ	57 – 75	Helical; Name=Helix BCombined sources2 PublicationsAdd BLAST	19
Topological domainⁱ	76 – 92	ExtracellularCombined sources2 PublicationsAdd BLAST	17
Transmembraneⁱ	93 – 109	Helical; Name=Helix CCombined sources2 PublicationsAdd BLAST	17
Topological domainⁱ	110 – 120	CytoplasmicCombined sources2 PublicationsAdd BLAST	11
Transmembraneⁱ	121 – 140	Helical; Name=Helix DCombined sources2 PublicationsAdd BLAST	20
Topological domainⁱ	141 – 147	ExtracellularCombined sources2 Publications	7
Transmembraneⁱ	148 – 167	Helical; Name=Helix ECombined sources2 PublicationsAdd BLAST	20
Topological domainⁱ	168 – 185	CytoplasmicCombined sources2 PublicationsAdd BLAST	18
Transmembraneⁱ	186 – 204	Helical; Name=Helix FCombined sources2 PublicationsAdd BLAST	19
Topological domainⁱ	205 – 216	ExtracellularCombined sources2 PublicationsAdd BLAST	12
Transmembraneⁱ	217 – 236	Helical; Name=Helix GCombined sources2 PublicationsAdd BLAST	20
Topological domainⁱ	237 – 262	CytoplasmicCombined sources2 PublicationsAdd BLAST	26

GO - Cellular componentⁱ

integral component of membrane Source: UniProtKB-KW
plasma membrane Source: UniProtKB-SubCell

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cell membrane, Membrane

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
PropeptideⁱPRO_0000020246	1 – 13	3 PublicationsAdd BLAST		13
ChainⁱPRO_0000020247	14 – 262	Bacteriorhodopsin2 PublicationsAdd BLAST		249

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Modified residueⁱ	14	Pyrrolidone carboxylic acid1 Publication		1
Modified residueⁱ	229	N6-(retinylidene)lysineCombined sources12 Publications		1

Post-translational modificationⁱ

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

Keywords - PTMⁱ

Pyrrolidone carboxylic acid

Proteomic databases

PaxDbⁱ	P02945

PaxDbⁱ

P02945

Interactionⁱ

Subunit structureⁱ

Homotrimer.5 Publications

Protein-protein interaction databases

Database of interacting proteins More...DIPⁱ	DIP-59007N
STRINGⁱ	64091.VNG1467G

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Turnⁱ	19 – 22	Combined sources	4
Helixⁱ	23 – 43	Combined sources	21
Turnⁱ	44 – 46	Combined sources	3
Helixⁱ	50 – 74	Combined sources	25
Turnⁱ	75 – 78	Combined sources	4
Beta strandⁱ	80 – 84	Combined sources	5
Beta strandⁱ	87 – 91	Combined sources	5
Helixⁱ	94 – 113	Combined sources	20
Helixⁱ	118 – 140	Combined sources	23
Helixⁱ	144 – 167	Combined sources	24
Helixⁱ	168 – 173	Combined sources	6
Beta strandⁱ	174 – 176	Combined sources	3
Helixⁱ	178 – 204	Combined sources	27
Turnⁱ	206 – 209	Combined sources	4
Beta strandⁱ	210 – 212	Combined sources	3
Helixⁱ	214 – 238	Combined sources	25
Helixⁱ	240 – 242	Combined sources	3

Show more details

3D structure databases

ProteinModelPortalⁱ	P02945
SMRⁱ	P02945
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P02945

EvolutionaryTraceⁱ

P02945

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the archaeal/bacterial/fungal opsin family.Curated

Keywords - Domainⁱ

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	arCOG02812 Archaea COG5524 LUCA
InParanoidⁱ	P02945
KEGG Orthology (KO) More...KOⁱ	K04641
OMAⁱ	RIFHYIT
Database of Orthologous Groups More...OrthoDBⁱ	POG093Z092V
PhylomeDBⁱ	P02945

Family and domain databases

InterProⁱ	View protein in InterPro IPR001425 Arc/bac/fun_rhodopsins IPR018229 Rhodopsin_retinal_BS
PANTHERⁱ	PTHR28286 PTHR28286, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01036 Bac_rhodopsin, 1 hit
PRINTSⁱ	PR00251 BACTRLOPSIN
SMARTⁱ	View protein in SMART SM01021 Bac_rhodopsin, 1 hit
PROSITEⁱ	View 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]FASTA Add 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 key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	118	Q → E AA sequence (Ref. 6) Curated	1
Sequence conflictⁱ	124	L → I AA sequence (Ref. 6) Curated	1
Sequence conflictⁱ	130	I → L AA sequence (Ref. 6) Curated	1
Sequence conflictⁱ	151	Missing AA sequence (Ref. 6) Curated	1
Sequence conflictⁱ	159	L → S AA sequence (Ref. 6) Curated	1
Sequence conflictⁱ	219	L → A AA sequence (Ref. 6) Curated	1

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
PIRⁱ	A93898 RAHSB H84300

Genome annotation databases

EnsemblBacteriaⁱ	AAG19772; AAG19772; VNG_1467G
KEGGⁱ	hal:VNG_1467G
PATRICⁱ	fig\|64091.14.peg.1122

Protein	Similar proteins		Species	Score	Length	Source
P02945	Bacteriorhodopsin	)	HALS3		262	UniRef100_P02945

Protein	Similar proteins		Species	Score	Length	Source
P02945	Bacteriorhodopsin	)	HALS3		262	UniRef90_P02945
UPI0002662AB1		HALSA		262
UPI00001115B5		HALSI		248
UPI0002B7BDCE		HALSA		262
UPI0000112067		HALSI		249
+48

Protein	Similar proteins		Species	Score	Length	Source
P02945	Bacteriorhodopsin	)	HALS3		262	UniRef50_P02945
Bacteriorhodopsin		uncultured archaeon		259
UPI0002B7BDCE		HALSA		262
UPI00001115B5		HALSI		248
Putative opsin (Fragment)		uncultured archaeon		130
+50

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

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB 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	[»]
4X31	X-ray	2.40	A	18-246	[»]
4X32	X-ray	1.90	A	18-245	[»]
4XXJ	X-ray	1.90	A/B/C	14-262	[»]
5A44	X-ray	2.29	A	14-261	[»]
5A45	X-ray	2.57	A	14-261	[»]
5B34	X-ray	2.10	A	14-262	[»]
5B35	X-ray	2.35	A	14-262	[»]
5B6V	X-ray	2.00	A	14-261	[»]
5B6W	X-ray	2.10	A	14-261	[»]
5B6X	X-ray	2.10	A	14-261	[»]
5B6Y	X-ray	2.10	A	14-261	[»]
5B6Z	X-ray	2.10	A	14-261	[»]
5BR2	X-ray	1.80	A	14-262	[»]
5BR5	X-ray	2.00	A	14-262	[»]
5H2H	X-ray	2.10	A	14-261	[»]
5H2I	X-ray	2.10	A	14-261	[»]
5H2J	X-ray	2.10	A	14-261	[»]
5H2K	X-ray	2.10	A	14-261	[»]
5H2L	X-ray	2.10	A	14-261	[»]
5H2M	X-ray	2.10	A	14-261	[»]
5H2N	X-ray	2.10	A	14-261	[»]
5H2O	X-ray	2.10	A	14-261	[»]
5H2P	X-ray	2.10	A	14-261	[»]
5J7A	X-ray	2.30	A	18-244	[»]
5VN7	X-ray	2.70	A/B	1-262	[»]
5VN9	X-ray	2.59	A/B	1-262	[»]
6G7H	X-ray	1.50	A	14-261	[»]
6G7I	X-ray	1.90	A	1-262	[»]
6G7J	X-ray	1.90	A	1-262	[»]
6G7K	X-ray	1.90	A	1-262	[»]
6G7L	X-ray	1.90	A	1-262	[»]
ProteinModelPortalⁱ	P02945
SMRⁱ	P02945
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

TCDBⁱ

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

Proteomic databases

PaxDbⁱ	P02945

PaxDbⁱ

P02945

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAG19772; AAG19772; VNG_1467G
KEGGⁱ	hal:VNG_1467G
PATRICⁱ	fig\|64091.14.peg.1122

Phylogenomic databases

eggNOGⁱ	arCOG02812 Archaea COG5524 LUCA
InParanoidⁱ	P02945
KOⁱ	K04641
OMAⁱ	RIFHYIT
OrthoDBⁱ	POG093Z092V
PhylomeDBⁱ	P02945

Miscellaneous databases

EvolutionaryTraceⁱ	P02945

EvolutionaryTraceⁱ

P02945

Family and domain databases

InterProⁱ	View protein in InterPro IPR001425 Arc/bac/fun_rhodopsins IPR018229 Rhodopsin_retinal_BS
PANTHERⁱ	PTHR28286 PTHR28286, 1 hit
Pfamⁱ	View protein in Pfam PF01036 Bac_rhodopsin, 1 hit
PRINTSⁱ	PR00251 BACTRLOPSIN
SMARTⁱ	View protein in SMART SM01021 Bac_rhodopsin, 1 hit
PROSITEⁱ	View protein in PROSITE PS00950 BACTERIAL_OPSIN_1, 1 hit PS00327 BACTERIAL_OPSIN_RET, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	BACR_HALSA
Accessionⁱ	P02945Primary (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:	October 10, 2018
	This is version 180 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

7-transmembrane G-linked receptors
List of 7-transmembrane G-linked receptor entries
SIMILARITY comments
Index of protein domains and families
PDB cross-references
Index of Protein Data Bank (PDB) cross-references

UniProtKB

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Supporting data

UniProtKB - P02945 (BACR_HALSA)

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Bacteriorhodopsin

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sites

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GO - Biological processi

Protein family/group databases

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Topology

GO - Cellular componenti

Keywords - Cellular componenti

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Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

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Protein-protein interaction databases

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Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Sequence databases

Genome annotation databases

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Sequence databases

3D structure databases

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Proteomic databases

Protocols and materials databases

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Mass spectrometryⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ