Reviewed,
UniProtKB/Swiss-Prot Q89A99 (LON_BUCBP)
Last modified
June 16, 2009.
Version 45.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: ATP-dependent protease La EC=3.4.21.53 | ||||
| Gene names |
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| Organism | Buchnera aphidicola subsp. Baizongia pistaciae [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 135842 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera |
Protein attributes
| Sequence length | 780 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Degrades short-lived regulatory and abnormal proteins in presence of ATP. Degrades the regulatory proteins rcsA and sulA. Hydrolyzes two ATPs for each peptide bond cleaved in the protein substrate By similarity. |
| Catalytic activity | Hydrolysis of proteins in presence of ATP. |
| Subunit structure | Homotetramer By similarity. |
| Subcellular location | |
| Sequence similarities | Belongs to the peptidase S16 family. Contains 1 Lon domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Hydrolase Protease Serine 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 | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent peptidase activityInferred from electronic annotation. Source: InterPro serine-type endopeptidase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Reductive genome evolution in Buchnera aphidicola." van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A. Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed: 12522265] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| AE016826 Genomic DNA. Translation: AAO27131.1. | |
| RefSeq | NP_778026.1. |
3D structure databases | |
| SMR | Q89A99. Positions 491-584, 594-775. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | S16.001. |
Genome annotation databases | |
| GeneID | 1058354. |
| GenomeReviews | Gene locus bbp_421 in contig AE016826_GR. |
| KEGG | bab:bbp421. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q89A99. |
| OMA | Q89A99. VMKESIQ. |
Enzyme and pathway databases | |
| BioCyc | BAPH224915:BBP_421-MON. |
Family and domain databases | |
| InterPro | IPR003593. ATPase_AAA+_core. IPR003959. ATPase_AAA_core. IPR008269. Pept_S16_C. IPR004815. Pept_S16_lon. IPR003111. Pept_S16_N. IPR008268. Peptidase_S16_AS. IPR001984. Peptidase_S16_C. [Graphical view] |
| Pfam | PF00004. AAA. 1 hit. PF02190. LON. 1 hit. PF05362. Lon_C. 1 hit. [Graphical view] |
| PRINTS | PR00830. ENDOLAPTASE. |
| SMART | SM00382. AAA. 1 hit. SM00464. LON. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00763. lon. 1 hit. |
| PROSITE | PS01046. LON_SER. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LON_BUCBP | ||||||||
| Accession | Primary (citable) accession number: Q89A99 | ||||||||
| 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


