Reviewed,
UniProtKB/Swiss-Prot Q6HBY2 (AMPA_BACHK)
Last modified
November 3, 2009.
Version 36.
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 |
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| Organism | Bacillus thuringiensis subsp. konkukian [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 180856 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 494 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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. |
| 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. |
| 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: 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 – 494 | 494 | Probable cytosol aminopeptidase HAMAP MF_00181 | PRO_0000165721 | |||||
Sites | |||||||||
| Active site | 272 | 1 | Potential | ||||||
| Active site | 346 | 1 | Potential | ||||||
| Metal binding | 260 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 265 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 265 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 283 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 342 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 344 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 344 | 1 | Manganese 2 By similarity | ||||||
Sequences
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References
| [1] | "Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis." Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P. Gilna P.J. Bacteriol. 188:3382-3390(2006) [PubMed: 16621833] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 97-27. |
Cross-references
Sequence databases | |
|---|---|
| AE017355 Genomic DNA. Translation: AAT63193.1. | |
| RefSeq | YP_038944.1. |
3D structure databases | |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | M17.010. |
Genome annotation databases | |
| GeneID | 2854154. |
| GenomeReviews | Gene locus BT9727_4633 in contig AE017355_GR. |
| KEGG | btk:BT9727_4633. |
| NMPDR | fig|281309.1.peg.4584. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q6HBY2. |
| OMA | ASMETDE. |
Enzyme and pathway databases | |
| BioCyc | BTHU281309:BT9727_4633-MON. |
Family and domain databases | |
| HAMAP | MF_00181. [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_BACHK | ||||||||
| Accession | Primary (citable) accession number: Q6HBY2 | ||||||||
| 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


