Q9RHV8 (DSBA_BURCE) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 50.
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: Thiol:disulfide interchange protein DsbA | ||
| Gene names |
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| Organism | Burkholderia cepacia (Pseudomonas cepacia) | ||
| Taxonomic identifier | 292 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › Burkholderia cepacia complex |
Protein attributes
| Sequence length | 212 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 | Involved in disulfide-bond formation. Acts by transferring its disulfide bond to other proteins. Involved in the production of protease and alkaline phosphatase, motility, metal resistance, and multi-drug resistance. |
| Subcellular location | Periplasm By similarity. |
| Sequence similarities | Belongs to the thioredoxin family. DsbA subfamily. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Periplasm |
| Domain | Redox-active center Signal |
| PTM | Disulfide bond |
| Gene Ontology (GO) | |
| Biological process | cell redox homeostasis Inferred from electronic annotation. Source: InterPro |
| Cellular component | periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "The DsbA-DsbB disulfide bond formation system of Burkholderia cepacia is involved in the production of protease and alkaline phosphatase, motility, metal resistance, and multi-drug resistance." Hayashi S., Abe M., Kimoto M., Furukawa S., Nakazawa T. Microbiol. Immunol. 44:41-50(2000) [PubMed: 10711598] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: KF1. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB012578 Genomic DNA. Translation: BAA89224.1. |
3D structure databases | |
| ProteinModelPortal | Q9RHV8. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR001853. DSBA-like_thioredoxin_dom. IPR023205. Thiol:disulphide_interchange. IPR012336. Thioredoxin-like_fold. IPR017937. Thioredoxin_CS. [Graphical view] |
| Gene3D | G3DSA:3.40.30.10. Thioredoxin_fold. 2 hits. |
| Pfam | PF01323. DSBA. 1 hit. [Graphical view] |
| PIRSF | PIRSF001488. Tdi_protein. 1 hit. |
| SUPFAM | SSF52833. Thiordxn-like_fd. 1 hit. |
| PROSITE | PS00194. THIOREDOXIN_1. 1 hit. PS51352. THIOREDOXIN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DSBA_BURCE | ||||||||
| Accession | Primary (citable) accession number: Q9RHV8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with