P0C2T8 (AMPN_LACLC) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 20.
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: Aminopeptidase N EC=3.4.11.2 Alternative name(s): Alanine aminopeptidase Lysyl aminopeptidase Short name=Lys-AP | ||||
| Gene names |
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| Organism | Lactococcus lactis subsp. cremoris (Streptococcus cremoris) | ||||
| Taxonomic identifier | 1359 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Lactococcus |
Protein attributes
| Sequence length | 846 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 | Aminopeptidase with broad substrate specificity to several peptides. It has more affinity for oligopeptides than for dipeptides. It plays an essential role in the metabolism, it may be involved in nitrogen supply or protein turnover By similarity. |
| Catalytic activity | Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide. |
| Cofactor | Binds 1 zinc ion per subunit By similarity. |
| Subunit structure | Monomer By similarity. |
| Subcellular location | Cytoplasm By similarity. Note: It may be secreted through an unknown mechanism By similarity. |
| Sequence similarities | Belongs to the peptidase M1 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | Metal-binding Zinc |
| Molecular function | Aminopeptidase Hydrolase Metalloprotease Protease |
| Technical term | Direct protein sequencing |
| 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 | aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW metallopeptidase activityInferred from electronic annotation. Source: UniProtKB-KW zinc ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.2 | ||||||
| Chain | 2 – 846 | 845 | Aminopeptidase N | PRO_0000095075 | |||||
Regions | |||||||||
| Region | 252 – 256 | 5 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 289 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 288 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 292 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 311 | 1 | Zinc; catalytic By similarity | ||||||
| Binding site | 120 | 1 | Substrate By similarity | ||||||
| Site | 375 | 1 | Transition state stabilizer By similarity | ||||||
Sequences
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References
| [1] | "Sequence of a gene (lap) encoding a 95.3-kDa aminopeptidase from Lactococcus lactis ssp. cremoris Wg2." Stroman P. Gene 113:107-112(1992) [PubMed: 1563625] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Wg2. |
| [2] | "Purification and characterization of an aminopeptidase from Lactococcus lactis subsp. cremoris Wg2." Tan P.S.T., Konings W.N. Appl. Environ. Microbiol. 56:526-532(1990) [PubMed: 16348128] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-34. Strain: Wg2. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X61230 Genomic DNA. Translation: CAA43547.1. |
| PIR | JN0324. |
3D structure databases | |
| ProteinModelPortal | P0C2T8. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR001930. Peptidase_M1. IPR014782. Peptidase_M1_N. [Graphical view] |
| PANTHER | PTHR11533. Peptidase_M1. 1 hit. |
| Pfam | PF01433. Peptidase_M1. 1 hit. [Graphical view] |
| PRINTS | PR00756. ALADIPTASE. |
| PROSITE | PS00142. ZINC_PROTEASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | AMPN_LACLC | ||||||||
| Accession | Primary (citable) accession number: P0C2T8 Secondary accession number(s): P37897 | ||||||||
| 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 |

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