P0A080 (AMPM_STAA1) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 53.
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: Methionine aminopeptidase Short name=MAP EC=3.4.11.18 Alternative name(s): Peptidase M | ||||
| Gene names |
| ||||
| Organism | Staphylococcus aureus (strain Mu3 / ATCC 700698) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 418127 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Staphylococcus |
Protein attributes
| Sequence length | 252 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Removes the amino-terminal methionine from nascent proteins By similarity. |
| Catalytic activity | Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides. |
| Cofactor | Binds 2 cobalt ions per subunit. The true nature of the physiological cofactor is under debate. The enzyme is also active with zinc, manganese or divalent iron ions By similarity. |
| Sequence similarities | Belongs to the peptidase M24A family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Cobalt Metal-binding |
| Molecular function | Aminopeptidase Hydrolase Protease |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | cellular process Inferred from electronic annotation. Source: InterPro proteolysisInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW 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 – 252 | 252 | Methionine aminopeptidase | PRO_0000148960 | |||||
Sites | |||||||||
| Metal binding | 93 | 1 | Cobalt 1 By similarity | ||||||
| Metal binding | 104 | 1 | Cobalt 1 By similarity | ||||||
| Metal binding | 104 | 1 | Cobalt 2 By similarity | ||||||
| Metal binding | 168 | 1 | Cobalt 2 By similarity | ||||||
| Metal binding | 202 | 1 | Cobalt 2 By similarity | ||||||
| Metal binding | 233 | 1 | Cobalt 1 By similarity | ||||||
| Metal binding | 233 | 1 | Cobalt 2 By similarity | ||||||
| Binding site | 76 | 1 | Substrate By similarity | ||||||
| Binding site | 175 | 1 | Substrate By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Identification of the up- and down-regulated genes in vancomycin-resistant Staphylococcus aureus strains Mu3 and Mu50 by cDNA differential hybridization method." Kuroda M., Kuwahara-Arai K., Hiramatsu K. Biochem. Biophys. Res. Commun. 269:485-490(2000) [PubMed: 10708580] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Mutated response regulator graR is responsible for phenotypic conversion of Staphylococcus aureus from heterogeneous vancomycin-intermediate resistance to vancomycin-intermediate resistance." Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K. Antimicrob. Agents Chemother. 52:45-53(2008) [PubMed: 17954695] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Mu3 / ATCC 700698. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB035448 Genomic DNA. Translation: BAB03321.1. AP009324 Genomic DNA. Translation: BAF78756.1. |
| RefSeq | YP_001442463.1. NC_009782.1. |
3D structure databases | |
| ProteinModelPortal | P0A080. |
| SMR | P0A080. Positions 1-249. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P0A080. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBSTAT00000003491; EBSTAP00000003390; EBSTAG00000003491. |
| GeneID | 5560524. |
| GenomeReviews | Gene locus SAHV_1873 in contig AP009324_GR. |
| KEGG | saw:SAHV_1873. |
| PATRIC | 19558890. VBIStaAur127830_1924. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0024. |
| GeneTree | EBGT00050000023792. |
| HOGENOM | HBG299384. |
| OMA | VFTVEPF. |
| ProtClustDB | PRK05716. |
Enzyme and pathway databases | |
| BioCyc | SAUR418127:SAHV_1873-MONOMER. |
| BRENDA | 3.4.11.18. 5870. |
Family and domain databases | |
| InterPro | IPR001714. Pept_M24_MAP. IPR000994. Pept_M24_structural-domain. IPR002467. Pept_M24A_MAP1. [Graphical view] |
| Gene3D | G3DSA:3.90.230.10. Peptidase_M24_cat_core. 1 hit. |
| KO | K01265. |
| Pfam | PF00557. Peptidase_M24. 1 hit. [Graphical view] |
| PRINTS | PR00599. MAPEPTIDASE. |
| SUPFAM | SSF55920. Peptidase_M24_cat_core. 1 hit. |
| TIGRFAMs | TIGR00500. Met_pdase_I. 1 hit. |
| ProtoNet | Search... |
Other | |
| BindingDB | P0A080. |
Entry information
| Entry name | AMPM_STAA1 | ||||||||
| Accession | Primary (citable) accession number: P0A080 Secondary accession number(s): A7X411, Q9KWL1 | ||||||||
| 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