Q1C5H7 (PEPB_YERPA) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 42.
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 B EC=3.4.11.23 Alternative name(s): Aminopeptidase B | ||||
| Gene names |
| ||||
| Organism | Yersinia pestis bv. Antiqua (strain Antiqua) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 360102 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Yersinia › ![]() |
Protein attributes
| Sequence length | 432 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Probably plays an important role in intracellular peptide degradation By similarity. HAMAP-Rule MF_00504 |
| Catalytic activity | Release of an N-terminal amino acid, Xaa, from a peptide or arylamide. Xaa is preferably Glu or Asp but may be other amino acids, including Leu, Met, His, Cys and Gln. HAMAP-Rule MF_00504 |
| Cofactor | Binds 2 manganese ions per subunit By similarity. |
| Subunit structure | Homohexamer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the peptidase M17 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | Manganese Metal-binding |
| Molecular function | Aminopeptidase Hydrolase Protease |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | proteolysis Inferred from electronic annotation. Source: HAMAP |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | aminopeptidase activity Inferred from electronic annotation. Source: HAMAP manganese ion bindingInferred from electronic annotation. Source: HAMAP metalloexopeptidase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 432 | 432 | Peptidase B HAMAP-Rule MF_00504 | PRO_0000258500 | |||||
Sites | |||||||||
| Active site | 208 | 1 | Potential | ||||||
| Active site | 282 | 1 | Potential | ||||||
| Metal binding | 196 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 201 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 201 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 219 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 278 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 280 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 280 | 1 | Manganese 2 By similarity | ||||||
Sequences
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References
| [1] | "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516: evidence of gene reduction in an emerging pathogen." Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M., Worsham P., Chu M.C., Andersen G.L. J. Bacteriol. 188:4453-4463(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Antiqua. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000308 Genomic DNA. Translation: ABG14295.1. |
| RefSeq | YP_652240.1. NC_008150.1. |
3D structure databases | |
| ProteinModelPortal | Q1C5H7. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 360102.YPA_2330. |
Proteomic databases | |
| PRIDE | Q1C5H7. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABG14295; ABG14295; YPA_2330. |
| GeneID | 4121210. |
| KEGG | ypa:YPA_2330. |
| PATRIC | 18584214. VBIYerPes1796_2918. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0260. |
| HOGENOM | HOG000243130. |
| KO | K07751. |
| OMA | KLAGDGW. |
| ProtClustDB | PRK05015. |
Family and domain databases | |
| HAMAP | MF_00504. Aminopeptidase_M17. |
| InterPro | IPR011356. Leucine_aapep/pepB. IPR008330. Pept_M17_PepB. IPR000819. Peptidase_M17_C. [Graphical view] |
| PANTHER | PTHR11963:SF3. PTHR11963:SF3. 1 hit. |
| Pfam | PF12404. DUF3663. 1 hit. PF00883. Peptidase_M17. 1 hit. [Graphical view] |
| PIRSF | PIRSF036388. Ctsl_amnpptdse_B. 1 hit. |
| PRINTS | PR00481. LAMNOPPTDASE. |
| PROSITE | PS00631. CYTOSOL_AP. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PEPB_YERPA | ||||||||
| Accession | Primary (citable) accession number: Q1C5H7 | ||||||||
| 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
