P02945 · BACR_HALSA
- ProteinBacteriorhodopsin
- Genebop
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids262 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Light-driven proton pump.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 98 | Primary proton acceptor | ||||
Sequence: D |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | light-driven active monoatomic ion transmembrane transporter activity | |
Molecular Function | monoatomic ion channel activity | |
Molecular Function | photoreceptor activity | |
Biological Process | phototransduction | |
Biological Process | proton transmembrane transport |
Keywords
- Molecular function
- Biological process
- Ligand
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameBacteriorhodopsin
- Short namesBR
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageArchaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Halobacteriaceae > Halobacterium > Halobacterium salinarum NRC-34001
Accessions
- Primary accessionP02945
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 14-22 | Extracellular | ||||
Sequence: QAQITGRPE | ||||||
Transmembrane | 23-42 | Helical; Name=Helix A | ||||
Sequence: WIWLALGTALMGLGTLYFLV | ||||||
Topological domain | 43-56 | Cytoplasmic | ||||
Sequence: KGMGVSDPDAKKFY | ||||||
Transmembrane | 57-75 | Helical; Name=Helix B | ||||
Sequence: AITTLVPAIAFTMYLSMLL | ||||||
Topological domain | 76-92 | Extracellular | ||||
Sequence: GYGLTMVPFGGEQNPIY | ||||||
Transmembrane | 93-109 | Helical; Name=Helix C | ||||
Sequence: WARYADWLFTTPLLLLD | ||||||
Topological domain | 110-120 | Cytoplasmic | ||||
Sequence: LALLVDADQGT | ||||||
Transmembrane | 121-140 | Helical; Name=Helix D | ||||
Sequence: ILALVGADGIMIGTGLVGAL | ||||||
Topological domain | 141-147 | Extracellular | ||||
Sequence: TKVYSYR | ||||||
Transmembrane | 148-167 | Helical; Name=Helix E | ||||
Sequence: FVWWAISTAAMLYILYVLFF | ||||||
Topological domain | 168-185 | Cytoplasmic | ||||
Sequence: GFTSKAESMRPEVASTFK | ||||||
Transmembrane | 186-204 | Helical; Name=Helix F | ||||
Sequence: VLRNVTVVLWSAYPVVWLI | ||||||
Topological domain | 205-216 | Extracellular | ||||
Sequence: GSEGAGIVPLNI | ||||||
Transmembrane | 217-236 | Helical; Name=Helix G | ||||
Sequence: ETLLFMVLDVSAKVGFGLIL | ||||||
Topological domain | 237-262 | Cytoplasmic | ||||
Sequence: LRSRAIFGEAEAPEPSAGDGAAATSD |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for propeptide, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Propeptide | PRO_0000020246 | 1-13 | ||||
Sequence: MLELLPTAVEGVS | ||||||
Modified residue | 14 | Pyrrolidone carboxylic acid | ||||
Sequence: Q | ||||||
Chain | PRO_0000020247 | 14-262 | Bacteriorhodopsin | |||
Sequence: QAQITGRPEWIWLALGTALMGLGTLYFLVKGMGVSDPDAKKFYAITTLVPAIAFTMYLSMLLGYGLTMVPFGGEQNPIYWARYADWLFTTPLLLLDLALLVDADQGTILALVGADGIMIGTGLVGALTKVYSYRFVWWAISTAAMLYILYVLFFGFTSKAESMRPEVASTFKVLRNVTVVLWSAYPVVWLIGSEGAGIVPLNIETLLFMVLDVSAKVGFGLILLRSRAIFGEAEAPEPSAGDGAAATSD | ||||||
Modified residue | 229 | N6-(retinylidene)lysine | ||||
Sequence: K |
Post-translational modification
The covalent binding of retinal to the apoprotein, bacterioopsin, generates bacteriorhodopsin.
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length262
- Mass (Da)28,256
- Last updated1989-07-01 v2
- Checksum38AC8A364C8C7F21
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 118 | in Ref. 6; AA sequence | ||||
Sequence: Q → E | ||||||
Sequence conflict | 124 | in Ref. 6; AA sequence | ||||
Sequence: L → I | ||||||
Sequence conflict | 130 | in Ref. 6; AA sequence | ||||
Sequence: I → L | ||||||
Sequence conflict | 151 | in Ref. 6; AA sequence | ||||
Sequence: Missing | ||||||
Sequence conflict | 159 | in Ref. 6; AA sequence | ||||
Sequence: L → S | ||||||
Sequence conflict | 219 | in Ref. 6; AA sequence | ||||
Sequence: L → A |
Mass Spectrometry
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
V00474 EMBL· GenBank· DDBJ | CAA23744.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M11720 EMBL· GenBank· DDBJ | AAA72504.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X70293 EMBL· GenBank· DDBJ | CAA49774.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE004437 EMBL· GenBank· DDBJ | AAG19772.1 EMBL· GenBank· DDBJ | Genomic DNA |