A0AAF1DAR3 · A0AAF1DAR3_9NEIS
- ProteinATP-dependent protease ATPase subunit HslU
- GenehslU
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids440 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
function
ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
Features
Showing features for binding 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 | HslUV protease complex | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | peptidase activity | |
Molecular Function | proteasome-activating activity | |
Biological Process | protein unfolding | |
Biological Process | proteolysis involved in protein catabolic process |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameATP-dependent protease ATPase subunit HslU
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Neisseriales > Neisseriaceae > Eikenella
Accessions
- Primary accessionA0AAF1DAR3
Subcellular Location
Interaction
Subunit
A double ring-shaped homohexamer of HslV is capped on each side by a ring-shaped HslU homohexamer. The assembly of the HslU/HslV complex is dependent on binding of ATP.
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 46-332 | AAA+ ATPase | ||||
Sequence: VPKNILMIGPTGVGKTEIARRLARLANAPFIKIEATKFTEVGYVGRDVDSIVRDLMEIALKNLREQAVRKNRARAQDAAENRVLDALLPPPPQTGFEGEPAEPQPESHTRKKFREMLRQGELDDKEINIELSQASPTSMQVMGPPGMEEFSSQLQDMFANLSKGRTKPHKIKVAAAMKLLLDEEAAKLINEEELREQAVHAVEQHGIVFLDEIDKIAADSNRHGGDVSRQGVQRDLLPLVEGTTVQTKYGMIKTDHILFIASGAFHLSKPSDLIPELQGRFPIRVEL | ||||||
Region | 131-154 | Disordered | ||||
Sequence: ALLPPPPQTGFEGEPAEPQPESHT | ||||||
Domain | 335-428 | Clp ATPase C-terminal | ||||
Sequence: LTVEDFQAILTSTDASLTKQYQALLATDGVELDFAPDGITRLAEIAFQVNEKTENIGARRLHTVLEKLLEDVSFHAPQGTTQITAAYVDERLAE |
Sequence similarities
Belongs to the ClpX chaperone family. HslU subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length440
- Mass (Da)48,976
- Last updated2024-05-29 v1
- ChecksumC3E4601D34463D69
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP038018 EMBL· GenBank· DDBJ | QED92908.1 EMBL· GenBank· DDBJ | Genomic DNA |