Reviewed,
UniProtKB/Swiss-Prot P27195 (PPCF_ELIMR)
Last modified
June 16, 2009.
Version 53.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Prolyl endopeptidase EC=3.4.21.26 Alternative name(s): Proline-specific endopeptidase Short name=PSE Short name=PE Post-proline cleaving enzyme |
| Organism | Elizabethkingia miricola (Chryseobacterium miricola) |
| Taxonomic identifier | 172045 [NCBI] |
| Taxonomic lineage | Bacteria › Bacteroidetes › Flavobacteria › Flavobacteriales › Flavobacteriaceae › Elizabethkingia |
Protein attributes
| Sequence length | 705 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long. Has an absolute requirement for an X-Pro bond in the trans configuration immediately preceding the Pro-Y scissible bond. |
| Catalytic activity | Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides. |
| Subunit structure | Monomer. |
| Subcellular location | |
| Sequence similarities | Belongs to the peptidase S9A family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Periplasm |
| Domain | Signal |
| Molecular function | Hydrolase Protease Serine protease |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | proteolysis Inferred from electronic annotation. Source: InterPro |
| Cellular component | periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Characterization of a prolyl endopeptidase from Flavobacterium meningosepticum. Complete sequence and localization of the active-site serine." Chevallier S., Goeltz P., Thibault P., Banville D., Gagnon J. J. Biol. Chem. 267:8192-8199(1992) [PubMed: 1569074] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: ATCC 33958. |
Cross-references
Sequence databases | |
|---|---|
| M81461 Genomic DNA. Translation: AAA24925.1. | |
3D structure databases | |
| HSSP | HSSP built from PDB template 1O6G based on UniProtKB P23687. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | S09.001. |
Family and domain databases | |
| InterPro | IPR002471. Pept_S9_AS. IPR001375. Peptidase_S9. IPR002470. Peptidase_S9A. IPR004106. Peptidase_S9A_N. [Graphical view] |
| PANTHER | PTHR11757. Peptidase_S9A. 1 hit. |
| Pfam | PF00326. Peptidase_S9. 1 hit. PF02897. Peptidase_S9_N. 1 hit. [Graphical view] |
| PRINTS | PR00862. PROLIGOPTASE. |
| PROSITE | PS00708. PRO_ENDOPEP_SER. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PPCF_ELIMR | ||||||||
| Accession | Primary (citable) accession number: P27195 | ||||||||
| 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


