Reviewed,
UniProtKB/Swiss-Prot P54413 (CLPP_CAMJE)
Last modified
June 16, 2009.
Version 60.
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 Clp protease proteolytic subunit EC=3.4.21.92 Alternative name(s): Endopeptidase Clp | ||||
| Gene names |
| ||||
| Organism | Campylobacter jejuni [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 197 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter |
Protein attributes
| Sequence length | 194 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins By similarity. |
| Catalytic activity | Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec; and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs). HAMAP MF_00444 |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the peptidase S14 family. |
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: HAMAP |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein bindingInferred from physical interaction. Source: IntAct serine-type endopeptidase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| fliG | Q0PBJ0 | 1 | EBI-1326702,EBI-1191336 | |
| fliM | Q0PC73 | 1 | EBI-1326702,EBI-1191095 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 194 | 194 | ATP-dependent Clp protease proteolytic subunit HAMAP MF_00444 | PRO_0000179524 | |||||
Sites | |||||||||
| Active site | 97 | 1 | By similarity | ||||||
| Active site | 122 | 1 | By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "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. |
| [2] | "The gene for Campylobacter trigger factor: evidence for multiple transcription start sites and protein products." Griffiths P.L., Park R.W.A., Connerton I.F. Microbiology 141:1359-1367(1995) [PubMed: 7670637] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49. Strain: NCTC 11168 / Serotype O:2. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| AL111168 Genomic DNA. Translation: CAL34361.1. X85954 Genomic DNA. Translation: CAA59932.1. | |
| PIR | G81437. |
| RefSeq | YP_002343650.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1TYF based on UniProtKB P19245. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P54413. 97 interactions. |
Genome annotation databases | |
| GeneID | 906014. |
| GenomeReviews | Gene locus Cj0192c in contig AL111168_GR. |
| KEGG | cje:Cj0192c. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P54413. |
| OMA | P54413. PDIVTIC. |
Enzyme and pathway databases | |
| BioCyc | CJEJ192222:CJ0192C-MON. |
| BRENDA | 3.4.21.92. 255835. |
Family and domain databases | |
| HAMAP | MF_00444. [Tree] |
| InterPro | IPR001907. Pept_S14_ClpP. IPR018215. Pept_S14_ClpP_CS. [Graphical view] |
| PANTHER | PTHR10381. Pept_S14_ClpP. 1 hit. |
| Pfam | PF00574. CLP_protease. 1 hit. [Graphical view] |
| PRINTS | PR00127. CLPPROTEASEP. |
| TIGRFAMs | TIGR00493. clpP. 1 hit. |
| PROSITE | PS00382. CLP_PROTEASE_HIS. 1 hit. PS00381. CLP_PROTEASE_SER. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CLPP_CAMJE | ||||||||
| Accession | Primary (citable) accession number: P54413 Secondary accession number(s): Q0PBU7, Q9PIT7 | ||||||||
| 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


