O87765 (PCP_LACLM) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 81.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Pyrrolidone-carboxylate peptidase EC=3.4.19.3 Alternative name(s): 5-oxoprolyl-peptidase Pyroglutamyl-peptidase I Short name=PGP-I Short name=Pyrase | ||||
| Gene names |
| ||||
| Organism | Lactococcus lactis subsp. cremoris (strain MG1363) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 416870 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Lactococcus › ![]() |
Protein attributes
| Sequence length | 215 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Removes 5-oxoproline from various penultimate amino acid residues except L-proline By similarity. HAMAP-Rule MF_00417 |
| Catalytic activity | Release of an N-terminal pyroglutamyl group from a polypeptide, the second amino acid generally not being Pro. HAMAP-Rule MF_00417 |
| Subunit structure | Homotetramer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the peptidase C15 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Molecular function | Hydrolase Protease Thiol protease |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | proteolysis Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | cysteine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW pyroglutamyl-peptidase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 215 | 215 | Pyrrolidone-carboxylate peptidase HAMAP-Rule MF_00417 | PRO_0000184722 | |||||
Sites | |||||||||
| Active site | 78 | 1 | By similarity | ||||||
| Active site | 141 | 1 | By similarity | ||||||
| Active site | 165 | 1 | By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "A natural large chromosomal inversion in Lactococcus lactis is mediated by homologous recombination between two insertion sequences." Daveran-Mingot M.L., Campo N., Ritzenthaler P., le Bourgeois P. J. Bacteriol. 180:4834-4842(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Pyrrolidone carboxyl peptidase of Lactococcus lactis MG1363." Buist G., Haandrikman A.J., Benus G., Feenstra B., Venema G., Kok J. Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [3] | "The complete genome sequence of the lactic acid bacterial paradigm Lactococcus lactis subsp. cremoris MG1363." Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C., Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P., van Sinderen D., Kok J. J. Bacteriol. 189:3256-3270(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MG1363. |
| [4] | "Identification and characterisation of a gene encoding aminoacylase activity from Lactococcus lactis MG1363." Curley P., van Sinderen D. FEMS Microbiol. Lett. 183:177-182(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 103-215. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AJ223960 Genomic DNA. Translation: CAA11691.1. AJ223962 Genomic DNA. Translation: CAA11699.1. AF323462 Genomic DNA. Translation: AAK20299.1. AM406671 Genomic DNA. Translation: CAL97264.1. AF168363 Genomic DNA. Translation: AAF36226.1. |
| RefSeq | YP_001032004.1. NC_009004.1. |
3D structure databases | |
| ProteinModelPortal | O87765. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 416870.llmg_0663. |
Protein family/group databases | |
| MEROPS | C15.001. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAL97264; CAL97264; llmg_0663. |
| GeneID | 4797823. |
| KEGG | llm:llmg_0663. |
| PATRIC | 22282430. VBILacLac4574_0679. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG2039. |
| HOGENOM | HOG000242641. |
| KO | K01304. |
| OMA | AYFTQLP. |
| ProtClustDB | PRK13197. |
Family and domain databases | |
| Gene3D | 3.40.630.20. 1 hit. |
| HAMAP | MF_00417. Pyrrolid_peptidase. |
| InterPro | IPR000816. Peptidase_C15. IPR016125. Peptidase_C15-like. [Graphical view] |
| PANTHER | PTHR23402. PTHR23402. 1 hit. |
| Pfam | PF01470. Peptidase_C15. 1 hit. [Graphical view] |
| PIRSF | PIRSF015592. Prld-crbxl_pptds. 1 hit. |
| PRINTS | PR00706. PYROGLUPTASE. |
| SUPFAM | SSF53182. Peptidase_C15-like. 1 hit. |
| TIGRFAMs | TIGR00504. pyro_pdase. 1 hit. |
| PROSITE | PS01334. PYRASE_CYS. 1 hit. PS01333. PYRASE_GLU. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PCP_LACLM | ||||||||
| Accession | Primary (citable) accession number: O87765 Secondary accession number(s): A2RJ15, Q9L9P5, Q9R805 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with
