P65805 (PEPT_STAAM) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 64.
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: Peptidase T EC=3.4.11.4 Alternative name(s): Aminotripeptidase Short name=Tripeptidase Tripeptide aminopeptidase | ||||
| Gene names |
| ||||
| Organism | Staphylococcus aureus (strain Mu50 / ATCC 700699) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 158878 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus › ![]() |
Protein attributes
| Sequence length | 408 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Cleaves the N-terminal amino acid of tripeptides By similarity. HAMAP-Rule MF_00550 |
| Catalytic activity | Release of the N-terminal residue from a tripeptide. HAMAP-Rule MF_00550 |
| Cofactor | Binds 2 zinc ions per subunit By similarity. HAMAP-Rule MF_00550 |
| Subcellular location | Cytoplasm By similarity HAMAP-Rule MF_00550. |
| Sequence similarities | Belongs to the peptidase M20B family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | Metal-binding Zinc |
| Molecular function | Aminopeptidase Hydrolase Metalloprotease Protease |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | peptide metabolic process Inferred from electronic annotation. Source: InterPro proteolysisInferred from electronic annotation. Source: HAMAP |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | metallopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW tripeptide aminopeptidase activityInferred from electronic annotation. Source: HAMAP zinc ion bindingInferred 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 – 408 | 408 | Peptidase T HAMAP-Rule MF_00550 | PRO_0000185316 | |||||
Sites | |||||||||
| Active site | 80 | 1 | By similarity | ||||||
| Active site | 174 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 78 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 140 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 140 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 175 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 197 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 379 | 1 | Zinc 2 By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Whole genome sequencing of meticillin-resistant Staphylococcus aureus." Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. Hiramatsu K.Lancet 357:1225-1240(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Mu50 / ATCC 700699. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BA000017 Genomic DNA. Translation: BAB56905.1. |
| RefSeq | NP_371267.1. NC_002758.2. |
3D structure databases | |
| ProteinModelPortal | P65805. |
| SMR | P65805. Positions 1-406. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 158878.SAV0743. |
2D gel databases | |
| World-2DPAGE | 0002:P65805. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | BAB56905; BAB56905; SAV0743. |
| GeneID | 1120716. |
| KEGG | sav:SAV0743. |
| PATRIC | 19562158. VBIStaAur52173_0760. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG2195. |
| HOGENOM | HOG000032390. |
| KO | K01258. |
| OMA | YVYATIP. |
| ProtClustDB | PRK05469. |
Enzyme and pathway databases | |
| BioCyc | SAUR158878:GJJ5-760-MONOMER. |
Family and domain databases | |
| Gene3D | 3.30.70.360. 1 hit. |
| HAMAP | MF_00550. Aminopeptidase_M20. |
| InterPro | IPR001261. ArgE/DapE_CS. IPR002933. Peptidase_M20. IPR011650. Peptidase_M20_dimer. IPR010161. Peptidase_M20B. [Graphical view] |
| Pfam | PF07687. M20_dimer. 1 hit. PF01546. Peptidase_M20. 1 hit. [Graphical view] |
| PIRSF | PIRSF037215. Peptidase_M20B. 1 hit. |
| SUPFAM | SSF55031. Peptidase_M20_dimer. 1 hit. |
| TIGRFAMs | TIGR01882. peptidase-T. 1 hit. |
| PROSITE | PS00758. ARGE_DAPE_CPG2_1. 1 hit. PS00759. ARGE_DAPE_CPG2_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PEPT_STAAM | ||||||||
| Accession | Primary (citable) accession number: P65805 Secondary accession number(s): Q99VN1 | ||||||||
| Entry history |
| ||||||||
| 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
