Q9HSC3 · LONB_HALSA
- ProteinArchaeal Lon protease
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids702 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Degrades polypeptides processively (By similarity).
Features
Showing features for binding site, active site.
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 | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | ATP-dependent peptidase activity | |
Molecular Function | serine-type endopeptidase activity | |
Biological Process | protein catabolic process | |
Biological Process | proteolysis | |
Biological Process | regulation of DNA-templated transcription |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameArchaeal Lon protease
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Halobacteriaceae > Halobacterium > Halobacterium salinarum NRC-34001
Accessions
- Primary accessionQ9HSC3
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 | 1-183 | Cytoplasmic | ||||
Sequence: MSNESTNDAPPDDDPDDPEPSVDHDDTDGLQDDPADSVDDAGEVDDLENLGSDVGVEGDVSIDEDNAEDDLLGGLRIDDTSDITVPDRLVDQVIGQEAAREIVKRAAKQHRHVMMIGSPGTGKSLLAKAMSRLLPKESLQDVLVYHNPDDSNEPKVRTVPAGKGEQIVDAHKEEARKRNQMRS | ||||||
Transmembrane | 184-201 | Helical | ||||
Sequence: FLMWIMILLAVGYALLIA | ||||||
Topological domain | 202-206 | Extracellular | ||||
Sequence: TPARP | ||||||
Transmembrane | 207-223 | Helical | ||||
Sequence: LLALLSAAGIYLLFRYT | ||||||
Topological domain | 224-702 | Cytoplasmic | ||||
Sequence: NRGSDAMVPKLLINNADRQVAPFEDATGAHAGAMLGDVRHDPFQSGGMATPSHERVEAGSIQKANKGVLFIDEINTLDVRSQQKLMTAIQEGEFSITGQSERSSGAMVQTEAVPCDFIMVAAGNMDAMENMHPALRSRIKGYGYEVYMDDTIEDTPDMRRKYARFVAQEVEKDGNLPHFAPDAIRELILEAKRRAGRKDSLTLKLRDLGGLVRVAGDIARSEGHDLTQRSDVLEAKKRSRSIEQQFVDNYIQRRKDYELGTTSEEAVGRVNGLAVMGGDSGIMLPVMAEITPAQSQEEGRIYATGQLKEMAEEAVENVSAIIKKFSDENMSEKDTHIQFVQAGEGGVDGDSASITVATAVISALEDIPVAQELAMTGSLSVRGDVLPVGGVTHKIEAAAKAGCERVIIPKANEDDVMIEDEYEEQIEIIPVTHISEVLDVALVGEPEKDSLVDRLKSITGKALDSASDSGTTGGNPSPQ |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000076152 | 1-702 | Archaeal Lon protease | |||
Sequence: MSNESTNDAPPDDDPDDPEPSVDHDDTDGLQDDPADSVDDAGEVDDLENLGSDVGVEGDVSIDEDNAEDDLLGGLRIDDTSDITVPDRLVDQVIGQEAAREIVKRAAKQHRHVMMIGSPGTGKSLLAKAMSRLLPKESLQDVLVYHNPDDSNEPKVRTVPAGKGEQIVDAHKEEARKRNQMRSFLMWIMILLAVGYALLIATPARPLLALLSAAGIYLLFRYTNRGSDAMVPKLLINNADRQVAPFEDATGAHAGAMLGDVRHDPFQSGGMATPSHERVEAGSIQKANKGVLFIDEINTLDVRSQQKLMTAIQEGEFSITGQSERSSGAMVQTEAVPCDFIMVAAGNMDAMENMHPALRSRIKGYGYEVYMDDTIEDTPDMRRKYARFVAQEVEKDGNLPHFAPDAIRELILEAKRRAGRKDSLTLKLRDLGGLVRVAGDIARSEGHDLTQRSDVLEAKKRSRSIEQQFVDNYIQRRKDYELGTTSEEAVGRVNGLAVMGGDSGIMLPVMAEITPAQSQEEGRIYATGQLKEMAEEAVENVSAIIKKFSDENMSEKDTHIQFVQAGEGGVDGDSASITVATAVISALEDIPVAQELAMTGSLSVRGDVLPVGGVTHKIEAAAKAGCERVIIPKANEDDVMIEDEYEEQIEIIPVTHISEVLDVALVGEPEKDSLVDRLKSITGKALDSASDSGTTGGNPSPQ |
Proteomic databases
Interaction
Subunit
Homohexamer. Organized in a ring with a central cavity (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-63 | Disordered | ||||
Sequence: MSNESTNDAPPDDDPDDPEPSVDHDDTDGLQDDPADSVDDAGEVDDLENLGSDVGVEGDVSID | ||||||
Compositional bias | 9-23 | Acidic residues | ||||
Sequence: APPDDDPDDPEPSVD | ||||||
Compositional bias | 29-63 | Acidic residues | ||||
Sequence: GLQDDPADSVDDAGEVDDLENLGSDVGVEGDVSID | ||||||
Domain | 487-667 | Lon proteolytic | ||||
Sequence: EEAVGRVNGLAVMGGDSGIMLPVMAEITPAQSQEEGRIYATGQLKEMAEEAVENVSAIIKKFSDENMSEKDTHIQFVQAGEGGVDGDSASITVATAVISALEDIPVAQELAMTGSLSVRGDVLPVGGVTHKIEAAAKAGCERVIIPKANEDDVMIEDEYEEQIEIIPVTHISEVLDVALVG |
Sequence similarities
Belongs to the peptidase S16 family. Archaeal LonB subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length702
- Mass (Da)76,017
- Last updated2001-03-01 v1
- Checksum203624C9836B2736
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 9-23 | Acidic residues | ||||
Sequence: APPDDDPDDPEPSVD | ||||||
Compositional bias | 29-63 | Acidic residues | ||||
Sequence: GLQDDPADSVDDAGEVDDLENLGSDVGVEGDVSID |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE004437 EMBL· GenBank· DDBJ | AAG18884.1 EMBL· GenBank· DDBJ | Genomic DNA |