Reviewed,
UniProtKB/Swiss-Prot O84348 (LON_CHLTR)
Last modified
June 16, 2009.
Version 61.
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 | Chlamydia trachomatis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 813 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia |
Protein attributes
| Sequence length | 819 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] | "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia trachomatis." Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L., Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W. Science 282:754-759(1998) [PubMed: 9784136] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: D/UW-3/Cx. |
Cross-references
Sequence databases | |
|---|---|
| AE001273 Genomic DNA. Translation: AAC67939.1. | |
| PIR | C71527. |
| RefSeq | NP_219851.1. |
3D structure databases | |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | S16.002. |
Genome annotation databases | |
| GeneID | 884768. |
| GenomeReviews | Gene locus CT_344 in contig AE001273_GR. |
| KEGG | ctr:CT344. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | O84348. |
| OMA | O84348. LPWGVYG. |
Enzyme and pathway databases | |
| BioCyc | CTRA315277:CT344-MON. |
| BRENDA | 3.4.21.53. 108. |
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_CHLTR | ||||||||
| Accession | Primary (citable) accession number: O84348 | ||||||||
| 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


