P0C114 (DEGPL_BRUAB) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 48.
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: Probable periplasmic serine endoprotease DegP-like EC=3.4.21.107 Alternative name(s): Protease Do | ||||
| Gene names |
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| Organism | Brucella abortus biovar 1 (strain 9-941) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 262698 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › ![]() |
Protein attributes
| Sequence length | 513 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Might be efficient in the degradation of transiently denatured and unfolded proteins which accumulate in the periplasm following stress conditions By similarity. |
| Catalytic activity | Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-|-Val. |
| Subcellular location | Periplasm Potential. |
| Sequence similarities | Belongs to the peptidase S1B family. Contains 2 PDZ (DHR) domains. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Stress response |
| Cellular component | Periplasm |
| Domain | Repeat Signal |
| Molecular function | Hydrolase Protease Serine protease |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | proteolysis Inferred from electronic annotation. Source: UniProtKB-KW response to stressInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | outer membrane-bounded periplasmic space Inferred from sequence or structural similarity. Source: UniProtKB |
| Molecular_function | serine-type endopeptidase activity Inferred from sequence or structural similarity. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 25 | 25 | Potential | ||||||
| Chain | 26 – 513 | 488 | Probable periplasmic serine endoprotease DegP-like | PRO_0000026925 | |||||
Regions | |||||||||
| Domain | 300 – 391 | 92 | PDZ 1 | ||||||
| Domain | 414 – 500 | 87 | PDZ 2 | ||||||
| Region | 125 – 299 | 175 | Serine protease | ||||||
| Region | 255 – 257 | 3 | Substrate binding By similarity | ||||||
| Region | 312 – 316 | 5 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 152 | 1 | Charge relay system Potential | ||||||
| Active site | 182 | 1 | Charge relay system Potential | ||||||
| Active site | 257 | 1 | Charge relay system Potential | ||||||
Sequences
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References
| [1] | "Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis." Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C. J. Bacteriol. 187:2715-2726(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 9-941. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE017223 Genomic DNA. Translation: AAX74005.1. |
| RefSeq | YP_221366.1. NC_006932.1. |
3D structure databases | |
| ProteinModelPortal | P0C114. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 262698.BruAb1_0630. |
Proteomic databases | |
| PRIDE | P0C114. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAX74005; AAX74005; BruAb1_0630. |
| GeneID | 3339359. |
| KEGG | bmb:BruAb1_0630. |
| PATRIC | 17822861. VBIBruAbo15061_0667. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0265. |
| HOGENOM | HOG000223640. |
| KO | K01362. |
| OMA | DEGGLES. |
| ProtClustDB | CLSK864818. |
Enzyme and pathway databases | |
| BioCyc | BABO262698:GJC2-636-MONOMER. |
Family and domain databases | |
| InterPro | IPR001478. PDZ. IPR011782. Pept_S1C_Do. IPR001254. Peptidase_S1. IPR001940. Peptidase_S1C. IPR009003. Trypsin-like_Pept_dom. [Graphical view] |
| Pfam | PF13180. PDZ_2. 2 hits. PF00089. Trypsin. 1 hit. [Graphical view] |
| PRINTS | PR00834. PROTEASES2C. |
| SMART | SM00228. PDZ. 2 hits. [Graphical view] |
| SUPFAM | SSF50156. PDZ. 2 hits. SSF50494. Pept_Ser_Cys. 1 hit. |
| TIGRFAMs | TIGR02037. degP_htrA_DO. 1 hit. |
| PROSITE | PS50106. PDZ. 2 hits. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DEGPL_BRUAB | ||||||||
| Accession | Primary (citable) accession number: P0C114 Secondary accession number(s): P0A3Z6, Q44597, Q57EC9 | ||||||||
| 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 |
| Brucella abortus strain 9-941 Brucella abortus (strain 9-941): entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with
