Reviewed,
UniProtKB/Swiss-Prot P0AE20 (AMPM_ECO57)
Last modified
November 3, 2009.
Version 31.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Methionine aminopeptidase Short name=MAP EC=3.4.11.18 Alternative name(s): Peptidase M | ||||
| Gene names |
| ||||
| Organism | Escherichia coli O157:H7 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83334 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 264 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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. Binds 1 sodium ion per subunit. The sodium ion has a structural role By similarity. |
| Subunit structure | Monomer 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: InterPro |
| Molecular function | aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW cobalt 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 – 264 | 264 | Methionine aminopeptidase | PRO_0000148938 | |||||
Sites | |||||||||
| Metal binding | 97 | 1 | Cobalt 1 By similarity | ||||||
| Metal binding | 108 | 1 | Cobalt 1 By similarity | ||||||
| Metal binding | 108 | 1 | Cobalt 2 By similarity | ||||||
| Metal binding | 171 | 1 | Cobalt 2 By similarity | ||||||
| Metal binding | 204 | 1 | Cobalt 2 By similarity | ||||||
| Metal binding | 235 | 1 | Cobalt 1 By similarity | ||||||
| Metal binding | 235 | 1 | Cobalt 2 By similarity | ||||||
| Binding site | 79 | 1 | Substrate By similarity | ||||||
| Binding site | 99 | 1 | Substrate By similarity | ||||||
| Binding site | 178 | 1 | Substrate By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. Blattner F.R.Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC. |
| [2] | "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. Shinagawa H.DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC. |
Cross-references
Sequence databases | |
|---|---|
| AE005174 Genomic DNA. Translation: AAG54470.1. BA000007 Genomic DNA. Translation: BAB33593.1. | |
| PIR | B85501. B90650. |
| RefSeq | NP_285862.1. NP_308197.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 913847. 956892. |
| GenomeReviews | Gene locus Z0178 in contig AE005174_GR. Gene locus ECs0170 in contig BA000007_GR. |
| KEGG | ece:Z0178. ecs:ECs0170. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P0AE20. |
| OMA | VIQKHAE. |
Enzyme and pathway databases | |
| BioCyc | ECOL83334:ECS0170-MON. |
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. |
| PANTHER | PTHR10804:SF13. Pept_M24A_MAP1. 1 hit. PTHR10804. Peptidase_M24_cat_core. 1 hit. |
| Pfam | PF00557. Peptidase_M24. 1 hit. [Graphical view] |
| PRINTS | PR00599. MAPEPTIDASE. |
| TIGRFAMs | TIGR00500. met_pdase_I. 1 hit. |
| PROSITE | PS00680. MAP_1. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| BindingDB | P0AE20. |
Entry information
| Entry name | AMPM_ECO57 | ||||||||
| Accession | Primary (citable) accession number: P0AE20 Secondary accession number(s): P07906 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


