B2HP18 (PCP_MYCMM) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 36.
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 | Mycobacterium marinum (strain ATCC BAA-535 / M) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 216594 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › ![]() |
Protein attributes
| Sequence length | 222 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 – 222 | 222 | Pyrrolidone-carboxylate peptidase HAMAP-Rule MF_00417 | PRO_1000124001 | |||||
Sites | |||||||||
| Active site | 80 | 1 | By similarity | ||||||
| Active site | 146 | 1 | By similarity | ||||||
| Active site | 170 | 1 | By similarity | ||||||
Sequences
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References
| [1] | "Insights from the complete genome sequence of Mycobacterium marinum on the evolution of Mycobacterium tuberculosis." Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K., Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C., Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K., Lord A., Moule S. Cole S.T.Genome Res. 18:729-741(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-535 / M. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000854 Genomic DNA. Translation: ACC39060.1. |
| RefSeq | YP_001848915.1. NC_010612.1. |
3D structure databases | |
| ProteinModelPortal | B2HP18. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 216594.MMAR_0598. |
Protein family/group databases | |
| MEROPS | C15.001. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ACC39060; ACC39060; MMAR_0598. |
| GeneID | 6224848. |
| KEGG | mmi:MMAR_0598. |
| PATRIC | 18061905. VBIMycMar75906_0645. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG2039. |
| HOGENOM | HOG000242641. |
| KO | K01304. |
| OMA | HENGSNA. |
| ProtClustDB | PRK13195. |
Enzyme and pathway databases | |
| BioCyc | MMAR216594:GJOB-599-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] |
| 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_MYCMM | ||||||||
| Accession | Primary (citable) accession number: B2HP18 | ||||||||
| 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
