B2P6S8 (B2P6S8_ECO57) Unreviewed, UniProtKB/TrEMBL
Last modified
April 3, 2013.
Version 34.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Peptidase T HAMAP-Rule MF_00550 EC=3.4.11.4 HAMAP-Rule MF_00550 Alternative name(s): Aminotripeptidase HAMAP-Rule MF_00550 Tripeptide aminopeptidase HAMAP-Rule MF_00550 | ||||
| Gene names |
| ||||
| Organism | Escherichia coli O157:H7 str. EC4113 EMBL EDU54147.1 | ||||
| Taxonomic identifier | 444452 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › ![]() |
Protein attributes
| Sequence length | 408 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
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 SAAS SAAS010161 |
| Cofactor | Binds 2 zinc ions per subunit By similarity. HAMAP-Rule MF_00550 SAAS SAAS010161 |
| Subcellular location | Cytoplasm By similarity HAMAP-Rule MF_00550 SAAS SAAS010161. |
| Sequence similarities | Belongs to the peptidase M20B family. HAMAP-Rule MF_00550 |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm HAMAP-Rule MF_00550 SAAS SAAS010161 |
| Ligand | Metal-binding HAMAP-Rule MF_00550 SAAS SAAS010161 Zinc HAMAP-Rule MF_00550 SAAS SAAS010161 |
| Molecular function | Aminopeptidase HAMAP-Rule MF_00550 SAAS SAAS010161 EMBL EDU54147.1 Hydrolase Metalloprotease HAMAP-Rule MF_00550 SAAS SAAS010161 Protease |
| 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 | ||||
Sites | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Active site | 80 | 1 | By similarity HAMAP-Rule MF_00550 | ||||||
| Active site | 173 | 1 | Proton acceptor By similarity HAMAP-Rule MF_00550 | ||||||
| Metal binding | 78 | 1 | Zinc 1 By similarity HAMAP-Rule MF_00550 | ||||||
| Metal binding | 140 | 1 | Zinc 1 By similarity HAMAP-Rule MF_00550 | ||||||
| Metal binding | 140 | 1 | Zinc 2 By similarity HAMAP-Rule MF_00550 | ||||||
| Metal binding | 174 | 1 | Zinc 2 By similarity HAMAP-Rule MF_00550 | ||||||
| Metal binding | 196 | 1 | Zinc 1 By similarity HAMAP-Rule MF_00550 | ||||||
| Metal binding | 379 | 1 | Zinc 2 By similarity HAMAP-Rule MF_00550 | ||||||
Sequences
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References
| [1] | Rosovitz M.J., Ravel J. Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: EC4113 EMBL EDU54147.1. |
| [2] | "Annotation of Escherichia coli O157:H7 str. EC4113." Eppinger M., Ravel J., Mammel M.K., LeClerc J.E., Cebula T.A., Sebastian Y. Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: EC4113 EMBL EDU54147.1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | ABHP01000017 Genomic DNA. Translation: EDU54147.1. |
3D structure databases | |
| ProteinModelPortal | B2P6S8. |
| SMR | B2P6S8. Positions 1-408. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EDU54147; EDU54147; ECH7EC4113_4569. |
| PATRIC | 26598921. VBIEscCol134660_2699. |
Phylogenomic databases | |
| OMA | YVYATIP. |
Family and domain databases | |
| 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 | B2P6S8_ECO57 | ||||||||
| Accession | Primary (citable) accession number: B2P6S8 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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