Q1CM01 (AMPA_YERPN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 49.
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: Probable cytosol aminopeptidase EC=3.4.11.1 | ||||||
| Gene names |
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| Organism | Yersinia pestis bv. Antiqua (strain Nepal516) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 377628 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Yersinia › ![]() |
Protein attributes
| Sequence length | 503 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides By similarity. HAMAP-Rule MF_00181 |
| Catalytic activity | Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. HAMAP-Rule MF_00181 Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. |
| Cofactor | Binds 2 manganese ions per subunit 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: UniProtKB-KW |
| 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: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 503 | 503 | Probable cytosol aminopeptidase HAMAP-Rule MF_00181 | PRO_1000020005 | |||||
Sites | |||||||||
| Active site | 282 | 1 | Potential | ||||||
| Active site | 356 | 1 | Potential | ||||||
| Metal binding | 270 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 275 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 275 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 293 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 352 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 354 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 354 | 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: Nepal516. |
| [2] | "Yersinia pestis Nepal516A whole genome shotgun sequencing project." Plunkett G. III, Anderson B.D., Baumler D.J., Burland V., Cabot E.L., Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Munk A.C., Tapia R., Green L.D., Rogers Y.C., Detter J.C., Bruce D.C., Brettin T.S. Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000305 Genomic DNA. Translation: ABG16979.1. ACNQ01000006 Genomic DNA. Translation: EEO78446.1. |
| RefSeq | YP_646579.1. NC_008149.1. |
3D structure databases | |
| ProteinModelPortal | Q1CM01. |
| SMR | Q1CM01. Positions 1-503. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 377628.YPN_0647. |
Proteomic databases | |
| PRIDE | Q1CM01. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABG16979; ABG16979; YPN_0647. EEO78446; EEO78446; YP516_0683. |
| GeneID | 4125286. |
| KEGG | ypn:YPN_0647. |
| PATRIC | 18600353. VBIYerPes46733_0861. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0260. |
| HOGENOM | HOG000243132. |
| KO | K01255. |
| OMA | LMSVMEY. |
| ProtClustDB | PRK00913. |
Family and domain databases | |
| HAMAP | MF_00181. Cytosol_peptidase_M17. |
| InterPro | IPR011356. Leucine_aapep/pepB. IPR000819. Peptidase_M17_C. IPR023042. Peptidase_M17_leu_NH2_pept. IPR008283. Peptidase_M17_N. [Graphical view] |
| PANTHER | PTHR11963:SF3. PTHR11963:SF3. 1 hit. |
| Pfam | PF00883. Peptidase_M17. 1 hit. PF02789. Peptidase_M17_N. 1 hit. [Graphical view] |
| PRINTS | PR00481. LAMNOPPTDASE. |
| PROSITE | PS00631. CYTOSOL_AP. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | AMPA_YERPN | ||||||||
| Accession | Primary (citable) accession number: Q1CM01 Secondary accession number(s): C4GPL4 | ||||||||
| 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
