P52278 (PIP_LACHE) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 67.
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: Proline iminopeptidase Short name=PIP EC=3.4.11.5 Alternative name(s): Prolyl aminopeptidase Short name=PAP | ||||
| Gene names |
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| Organism | Lactobacillus helveticus (Lactobacillus suntoryeus) | ||||
| Taxonomic identifier | 1587 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus |
Protein attributes
| Sequence length | 294 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Releases the N-terminal proline from various substrates. Hydrolyzes only di- and tripeptides with proline in the first position. Ref.1 |
| Catalytic activity | Release of N-terminal proline from a peptide. Ref.1 |
| Subunit structure | Homodimer. Ref.1 |
| Subcellular location | Cell envelope Potential. |
| Sequence similarities | Belongs to the peptidase S33 family. |
| Biophysicochemical properties | Kinetic parameters: KM=0.8 mM for Pro-pNA (at 40 degrees Celsius and pH 7.5) Ref.1 Vmax=350 mmol/min/mg enzyme with Pro-pNA as substrate pH dependence: Optimum pH is 7.5. At pH values above 7.5, the activity sharply decreases. Temperature dependence: Optimum activity at 40 degrees Celsius. |
Ontologies
| Keywords | |
|---|---|
| Molecular function | Aminopeptidase Hydrolase Protease |
| Gene Ontology (GO) | |
| Biological process | proteolysis Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: InterPro envelopeInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "An operon from Lactobacillus helveticus composed of a proline iminopeptidase gene (pepI) and two genes coding for putative members of the ABC transporter family of proteins." Varmanen P., Rantanen T., Palva A. Microbiology 142:3459-3468(1996) [PubMed: 9004508] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. Strain: 53/7. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Z56283 Genomic DNA. Translation: CAA91231.1. |
3D structure databases | |
| ProteinModelPortal | P52278. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR005945. Pept_S33_TRI_F1. IPR002410. Peptidase_S33. [Graphical view] |
| PIRSF | PIRSF005539. Pept_S33_TRI_F1. 1 hit. |
| PRINTS | PR00793. PROAMNOPTASE. |
| TIGRFAMs | TIGR01250. Pro_imino_pep_2. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | PIP_LACHE | ||||||||
| Accession | Primary (citable) accession number: P52278 | ||||||||
| 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