Q9HJ89 · LONB_THEAC
- ProteinArchaeal Lon protease
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids657 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.196 mM | ATP |
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 > Candidatus Thermoplasmatota > Thermoplasmata > Thermoplasmatales > Thermoplasmataceae > Thermoplasma
Accessions
- Primary accessionQ9HJ89
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 | 1-123 | Cytoplasmic | ||||
Sequence: MEENIESVEEWVNKLDIETTKDIHVPKLLFDQVIGQDQAGEIVKKAALQRRHVILIGEPGTGKSMLAQSMVDFLPKSELEDILVFPNPEDPNKPKIKTVPAGKGKEIVRQYQIKAEREKRDRS | ||||||
Transmembrane | 124-144 | Helical | ||||
Sequence: RSIMFVIFSVVLLGIIAAIVL | ||||||
Topological domain | 145 | Extracellular | ||||
Sequence: R | ||||||
Transmembrane | 146-166 | Helical | ||||
Sequence: SITLIFFAIMAAAFLYMAMAF | ||||||
Topological domain | 167-657 | Cytoplasmic | ||||
Sequence: NPVIRNERAMVPKLLVSHNPNDKPPFVDSTGAHSGALLGDVRHDPFQSGGLETPAHERVEAGNIHKAHKGVLFIDEINLLRPEDQQAILTALQEKKYPISGQSERSAGAMVQTEPVPCDFVLVAAGNYDAIRNMHPALRSRIRGYGYEVVVNDYMDDNDENRRKLVQFIAQEVEKDKKIPHFDKSAIIEVIKEAQKRSGRRNKLTLRLRELGGLVRVAGDIAVSQKKTVVTAADVIAAKNLAKPLEQQIADRSIEIKKIYKTFRTEGSVVGMVNGLAVVGADTGMSEYTGVVLPIVAEVTPAEHKGAGNIIATGKLGDIAKEAVLNVSAVFKKLTGKDISNMDIHIQFVGTYEGVEGDSASVSIATAVISAIENIPVDQSVAMTGSLSVRGDVLPVGGVTAKVEAAIEAGLNKVIVPELNYSDIILDADHVNKIEIIPAKTIEDVLRVALVNSPEKEKLFDRISNLINAAKIIKPQRPATPATTRAGNNAA |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 63 | Completely abolishes ATPase activity and makes peptidase activity independent on ATP stimulus. | ||||
Sequence: K → A | ||||||
Mutagenesis | 241 | Retains 5% ATPase activity. Proteolytic activity is greatly impaired and cannot be stimulated by nucleotides. | ||||
Sequence: D → A | ||||||
Mutagenesis | 293 | Severely reduces ATPase and proteolytic activity. | ||||
Sequence: N → A | ||||||
Mutagenesis | 305 | Decreases ATPase activity. Completely abolishes peptidase activity in the absence of ATP, but ATP-stimulated peptidase activity i close to wild-type levels. | ||||
Sequence: R → A | ||||||
Mutagenesis | 375 | Almost completely abolishes ATPase activity and severely reduces proteolytic activity. | ||||
Sequence: R → A | ||||||
Mutagenesis | 382 | Decreases ATPase activity. Completely abolishes peptidase activity in the absence of ATP, but ATP-stimulated peptidase activity i close to wild-type levels. | ||||
Sequence: R → A | ||||||
Mutagenesis | 525 | Abolishes peptidase activity, but retains ATPase activity. | ||||
Sequence: S → A | ||||||
Mutagenesis | 568 | Abolishes peptidase activity, but retains ATPase activity. | ||||
Sequence: K → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000076154 | 1-657 | Archaeal Lon protease | |||
Sequence: MEENIESVEEWVNKLDIETTKDIHVPKLLFDQVIGQDQAGEIVKKAALQRRHVILIGEPGTGKSMLAQSMVDFLPKSELEDILVFPNPEDPNKPKIKTVPAGKGKEIVRQYQIKAEREKRDRSRSIMFVIFSVVLLGIIAAIVLRSITLIFFAIMAAAFLYMAMAFNPVIRNERAMVPKLLVSHNPNDKPPFVDSTGAHSGALLGDVRHDPFQSGGLETPAHERVEAGNIHKAHKGVLFIDEINLLRPEDQQAILTALQEKKYPISGQSERSAGAMVQTEPVPCDFVLVAAGNYDAIRNMHPALRSRIRGYGYEVVVNDYMDDNDENRRKLVQFIAQEVEKDKKIPHFDKSAIIEVIKEAQKRSGRRNKLTLRLRELGGLVRVAGDIAVSQKKTVVTAADVIAAKNLAKPLEQQIADRSIEIKKIYKTFRTEGSVVGMVNGLAVVGADTGMSEYTGVVLPIVAEVTPAEHKGAGNIIATGKLGDIAKEAVLNVSAVFKKLTGKDISNMDIHIQFVGTYEGVEGDSASVSIATAVISAIENIPVDQSVAMTGSLSVRGDVLPVGGVTAKVEAAIEAGLNKVIVPELNYSDIILDADHVNKIEIIPAKTIEDVLRVALVNSPEKEKLFDRISNLINAAKIIKPQRPATPATTRAGNNAA |
Proteomic databases
Interaction
Subunit
Homohexamer. Organized in a ring with a central cavity.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 433-618 | Lon proteolytic | ||||
Sequence: GSVVGMVNGLAVVGADTGMSEYTGVVLPIVAEVTPAEHKGAGNIIATGKLGDIAKEAVLNVSAVFKKLTGKDISNMDIHIQFVGTYEGVEGDSASVSIATAVISAIENIPVDQSVAMTGSLSVRGDVLPVGGVTAKVEAAIEAGLNKVIVPELNYSDIILDADHVNKIEIIPAKTIEDVLRVALVN |
Sequence similarities
Belongs to the peptidase S16 family. Archaeal LonB subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length657
- Mass (Da)71,601
- Last updated2001-03-01 v1
- ChecksumFD465CD99F5B38F7
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL445066 EMBL· GenBank· DDBJ | CAC12209.1 EMBL· GenBank· DDBJ | Genomic DNA |