Reviewed,
UniProtKB/Swiss-Prot O69300 (LON_CAMJE)
Last modified
June 16, 2009.
Version 64.
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 | Campylobacter jejuni [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 197 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter |
Protein attributes
| Sequence length | 791 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)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 791 | 791 | ATP-dependent protease La | PRO_0000076128 | |||||
Regions | |||||||||
| Domain | 12 – 201 | 190 | Lon | ||||||
| Nucleotide binding | 364 – 371 | 8 | ATP Potential | ||||||
Sites | |||||||||
| Active site | 697 | 1 | By similarity | ||||||
| Active site | 740 | 1 | By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 302 | 1 | I → V in CAA76672. Ref.1 | ||||||
| Sequence conflict | 531 | 1 | S → F in CAA76672. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning and expression of the Campylobacter jejuni lon gene detected by RNA arbitrarily primed PCR." Thies F.L., Hartung H.-P., Giegerich G. FEMS Microbiol. Lett. 165:329-334(1998) [PubMed: 9742705] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. Barrell B.G.Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2. |
Cross-references
Sequence databases | |
|---|---|
| Y17166 Genomic DNA. Translation: CAA76672.1. AL111168 Genomic DNA. Translation: CAL35190.1. | |
| PIR | D81310. |
| RefSeq | YP_002344466.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | O69300. 1 interaction. |
Protein family/group databases | |
| MEROPS | S16.001. |
Genome annotation databases | |
| GeneID | 905364. |
| GenomeReviews | Gene locus Cj1073c in contig AL111168_GR. |
| KEGG | cje:Cj1073c. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | O69300. |
| OMA | O69300. IVNGLAW. |
Enzyme and pathway databases | |
| BioCyc | CJEJ192222:CJ1073C-MON. |
| BRENDA | 3.4.21.53. 255835. |
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_CAMJE | ||||||||
| Accession | Primary (citable) accession number: O69300 Secondary accession number(s): Q0P9I1, Q9PNM1 | ||||||||
| 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


