O51132 (AMPM_BORBU) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 85.
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 | Borrelia burgdorferi (Lyme disease spirochete) | ||||
| Taxonomic identifier | 139 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Borrelia › Borrelia burgdorferi group |
Protein attributes
| Sequence length | 251 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Removes the amino-terminal methionine from nascent proteins. |
| 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 Reference 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 – 251 | 251 | Methionine aminopeptidase | PRO_0000148928 | |||||
Sites | |||||||||
| Metal binding | 96 | 1 | Cobalt 1 By similarity | ||||||
| Metal binding | 107 | 1 | Cobalt 1 By similarity | ||||||
| Metal binding | 107 | 1 | Cobalt 2 By similarity | ||||||
| Metal binding | 170 | 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 | 177 | 1 | Substrate By similarity | ||||||
Sequences
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References
| [1] | "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi." Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J. Venter J.C.Nature 390:580-586(1997) [PubMed: 9403685] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE000783 Genomic DNA. Translation: AAC66499.1. |
| PIR | A70113. |
| RefSeq | NP_212239.1. NC_001318.1. |
3D structure databases | |
| ProteinModelPortal | O51132. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | M24.001. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBORT00000008780; EBBORP00000008110; EBBORG00000008779. |
| GeneID | 1194941. |
| GenomeReviews | Gene locus BB_0105 in contig AE000783_GR. |
| KEGG | bbu:BB0105. |
| NMPDR | fig|224326.1.peg.489. |
| PATRIC | 20556816. VBIBorBur75917_0503. |
| TIGR | BB_0105. |
Phylogenomic databases | |
| GeneTree | EBGT00050000006914. |
| HOGENOM | HBG299384. |
| OMA | CEILTDR. |
| PhylomeDB | O51132. |
| ProtClustDB | CLSK507358. |
Enzyme and pathway databases | |
| BioCyc | BBUR224326:BB_0105-MONOMER. |
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. |
| 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. |
| PROSITE | PS00680. MAP_1. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | AMPM_BORBU | ||||||||
| Accession | Primary (citable) accession number: O51132 | ||||||||
| 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