Reviewed,
UniProtKB/Swiss-Prot O31147 (LON_MYCSM)
Last modified
June 16, 2009.
Version 57.
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 |
| ||
| Organism | Mycobacterium smegmatis | ||
| Taxonomic identifier | 1772 [NCBI] | ||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium |
Protein attributes
| Sequence length | 779 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
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. |
| Subcellular location | |
| 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 |
| 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)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 779 | 779 | ATP-dependent protease La | PRO_0000076141 | |||||
Regions | |||||||||
| Domain | 6 – 188 | 183 | Lon | ||||||
| Nucleotide binding | 352 – 359 | 8 | ATP Potential | ||||||
Sites | |||||||||
| Active site | 675 | 1 | |||||||
| Active site | 718 | 1 | By similarity | ||||||
Experimental info | |||||||||
| Mutagenesis | 675 | 1 | S → A or T: Loss of activity. | ||||||
| Mutagenesis | 675 | 1 | S → C: Retains some activity. | ||||||
Sequences
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References
| [1] | "The lon protease from Mycobacterium smegmatis: molecular cloning, sequence analysis, functional expression, and enzymatic characterization." Roudiak S.G., Seth A., Knipfer N., Shrader T.E. Biochemistry 37:377-386(1998) [PubMed: 9425059] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| AF030688 Genomic DNA. Translation: AAB86425.1. | |
3D structure databases | |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 3.4.21.53. 259. |
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_MYCSM | ||||||||
| Accession | Primary (citable) accession number: O31147 | ||||||||
| 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


