Reviewed,
UniProtKB/Swiss-Prot Q7WD42 (AMPA_BORBR)
Last modified
February 9, 2010.
Version 39.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Probable cytosol aminopeptidase EC=3.4.11.1 Alternative name(s): Leucine aminopeptidase Short name=LAP Leucyl aminopeptidase | ||||
| Gene names |
| ||||
| Organism | Bordetella bronchiseptica (Alcaligenes bronchisepticus) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 518 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella |
Protein attributes
| Sequence length | 499 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 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 MF_00181 |
| Cofactor | Binds 2 manganese ions per subunit By similarity. HAMAP MF_00181 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_00181. |
| 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: InterPro |
| 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 – 499 | 499 | Probable cytosol aminopeptidase HAMAP MF_00181 | PRO_0000165724 | |||||
Sites | |||||||||
| Active site | 283 | 1 | Potential | ||||||
| Active site | 357 | 1 | Potential | ||||||
| Metal binding | 271 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 276 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 276 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 294 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 353 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 355 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 355 | 1 | Manganese 2 By similarity | ||||||
Sequences
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References
| [1] | "Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. Maskell D.J.Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RB50 / ATCC BAA-588 / NCTC 13252. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX640448 Genomic DNA. Translation: CAE35710.1. |
| RefSeq | NP_890271.1. |
3D structure databases | |
| SMR | Q7WD42. Positions 1-499. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | M17.003. |
Genome annotation databases | |
| GeneID | 2661335. |
| KEGG | bbr:BB3736. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG742580. |
| OMA | LGHHISG. |
| PhylomeDB | Q7WD42. |
Enzyme and pathway databases | |
| BioCyc | BBRO257310:BB3736-MONOMER. |
| BRENDA | 3.4.11.1. 413. |
Family and domain databases | |
| HAMAP | MF_00181. Cytosol_peptidase_M17. [Tree] |
| InterPro | IPR011356. Peptidase_M17. IPR000819. Peptidase_M17_C. IPR008283. Peptidase_M17_N. [Graphical view] |
| PANTHER | PTHR11963:SF3. Peptidase_M17. 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_BORBR | ||||||||
| Accession | Primary (citable) accession number: Q7WD42 | ||||||||
| Entry history |
| ||||||||
| 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


