Reviewed,
UniProtKB/Swiss-Prot O66605 (LON_AQUAE)
Last modified
June 16, 2009.
Version 67.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: ATP-dependent protease La EC=3.4.21.53 | ||||
| Gene names |
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| Organism | Aquifex aeolicus [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 63363 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Aquificae › Aquificales › Aquificaceae › Aquifex |
Protein attributes
| Sequence length | 795 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Degrades short-lived regulatory and abnormal proteins in presence of ATP. Hydrolyzes two ATPs for each peptide bond cleaved in the protein substrate By similarity. |
| Catalytic activity | Hydrolysis of proteins in presence of ATP. |
| Subunit structure | Homotetramer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the peptidase S16 family. Contains 1 Lon domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Hydrolase Protease Serine protease |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | proteolysis Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent peptidase activityInferred from electronic annotation. Source: InterPro serine-type endopeptidase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus." Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V. Nature 392:353-358(1998) [PubMed: 9537320] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: VF5. |
Cross-references
Sequence databases | |
|---|---|
| AE000657 Genomic DNA. Translation: AAC06568.1. | |
| PIR | A70322. |
| RefSeq | NP_213165.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1192839. |
| GenomeReviews | Gene locus aq_242 in contig AE000657_GR. |
| KEGG | aae:aq_242. |
| NMPDR | fig|224324.1.peg.180. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | O66605. |
| OMA | O66605. GAIPKEG. |
Enzyme and pathway databases | |
| BioCyc | AAEO224324:AQ_242-MON. |
| BRENDA | 3.4.21.53. 189781. |
Family and domain databases | |
| InterPro | IPR003593. ATPase_AAA+_core. IPR003959. ATPase_AAA_core. IPR008269. Pept_S16_C. IPR004815. Pept_S16_lon. IPR003111. Pept_S16_N. IPR008268. Peptidase_S16_AS. IPR001984. Peptidase_S16_C. [Graphical view] |
| Pfam | PF00004. AAA. 1 hit. PF02190. LON. 1 hit. PF05362. Lon_C. 1 hit. [Graphical view] |
| PRINTS | PR00830. ENDOLAPTASE. |
| SMART | SM00382. AAA. 1 hit. SM00464. LON. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00763. lon. 1 hit. |
| PROSITE | PS01046. LON_SER. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LON_AQUAE | ||||||||
| Accession | Primary (citable) accession number: O66605 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


