Reviewed,
UniProtKB/Swiss-Prot Q04723 (PEPC_LACLC)
Last modified
January 20, 2009.
Version 58.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Aminopeptidase C EC=3.4.22.40 Alternative name(s): Bleomycin hydrolase | ||
| Gene names |
| ||
| Organism | Lactococcus lactis subsp. cremoris (Streptococcus cremoris) | ||
| Taxonomic identifier | 1359 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Lactococcus |
Protein attributes
| Sequence length | 436 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 | Hydrolyzes naphthylamide-substituted amino acids as well as di- and tripeptides in which the half-cystine residue is involved in a disulfide loop, notably in oxytocin and vasopressin. Has also a bleomycin hydrolase activity. |
| Catalytic activity | Inactivates bleomycin B2 (a cytotoxic glycometallopeptide) by hydrolysis of a carboxyamide bond of beta-aminoalanine, but also shows general aminopeptidase activity. The specificity varies somewhat with source, but amino acid arylamides of Met, Leu and Ala are preferred. |
| Subunit structure | Homohexamer. |
| Sequence similarities | Belongs to the peptidase C1 family. |
Ontologies
| Keywords | |
|---|---|
| Molecular function | Aminopeptidase Hydrolase Protease Thiol protease |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | proteolysis Inferred from electronic annotation. Source: InterPro |
| Molecular function | aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW cysteine-type endopeptidase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Cloning and sequencing of pepC, a cysteine aminopeptidase gene from Lactococcus lactis subsp. cremoris AM2." Chapot-Chartier M.P., Nardi M., Chopin M.-C., Chopin A., Gripon J.-C. Appl. Environ. Microbiol. 59:330-333(1993) [PubMed: 8439160] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-16. Strain: AM2. |
| [2] | "Catalytic properties of the cysteine aminopeptidase PepC, a bacterial bleomycin hydrolase." Mistou M.Y., Gripon J.-C. Biochim. Biophys. Acta 1383:63-70(1998) [PubMed: 9546047] [Abstract] Cited for: CHARACTERIZATION. |
Cross-references
Sequence databases | |
|---|---|
| M86245 Genomic DNA. Translation: AAA74514.1. | |
| PIR | B48957. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1CB5 based on UniProtKB Q13867. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | C01.086. |
Enzyme and pathway databases | |
| BRENDA | 3.4.22.40. 289716. |
Family and domain databases | |
| InterPro | IPR000169. Pept_cys_AS. IPR004134. Peptidase_C1B. [Graphical view] |
| PANTHER | PTHR10363. Peptidase_C1B. 1 hit. |
| Pfam | PF03051. Peptidase_C1_2. 1 hit. [Graphical view] |
| PIRSF | PIRSF005700. PepC. 1 hit. |
| PROSITE | PS00640. THIOL_PROTEASE_ASN. False negative. PS00139. THIOL_PROTEASE_CYS. 1 hit. PS00639. THIOL_PROTEASE_HIS. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PEPC_LACLC | ||||||||
| Accession | Primary (citable) accession number: Q04723 | ||||||||
| 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


