A9R3Y5 (PCP_YERPG) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 47.
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 | Yersinia pestis bv. Antiqua (strain Angola) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 349746 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Yersinia › ![]() |
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. HAMAP-Rule MF_00417 |
| Subcellular location | Cytoplasm By similarity HAMAP-Rule MF_00417. |
| 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_1000124010 | |||||
Sites | |||||||||
| Active site | 80 | 1 | By similarity | ||||||
| Active site | 143 | 1 | By similarity | ||||||
| Active site | 167 | 1 | By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals new insights into the evolution and pangenome of the plague bacterium." Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S., Achtman M., Lindler L.E., Ravel J. J. Bacteriol. 192:1685-1699(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Angola. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000901 Genomic DNA. Translation: ABX87326.1. |
| RefSeq | YP_001607918.1. NC_010159.1. |
3D structure databases | |
| ProteinModelPortal | A9R3Y5. |
| SMR | A9R3Y5. Positions 1-209. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 349746.YpAngola_A3594. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABX87326; ABX87326; YpAngola_A3594. |
| GeneID | 5802070. |
| KEGG | ypg:YpAngola_A3594. |
| PATRIC | 18576862. VBIYerPes97331_4181. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG2039. |
| HOGENOM | HOG000242641. |
| KO | K01304. |
| OMA | AYFTQLP. |
| ProtClustDB | PRK13197. |
Enzyme and pathway databases | |
| BioCyc | YPES349746:GHPB-3603-MONOMER. |
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_YERPG | ||||||||
| Accession | Primary (citable) accession number: A9R3Y5 | ||||||||
| 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
