Q7W2Q0 (DSBA_BORPA) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 54.
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 |
| ||||
| Organism | Bordetella parapertussis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 519 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella |
Protein attributes
| Sequence length | 209 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Involved in disulfide-bond formation. Acts by transferring its disulfide bond to other proteins By similarity. |
| Subcellular location | Periplasm By similarity. |
| Sequence similarities | Belongs to the thioredoxin family. DsbA subfamily. Contains 1 thioredoxin domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Periplasm |
| Domain | Redox-active center Signal |
| PTM | Disulfide bond |
| Technical term | 3D-structure Complete proteome |
| 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)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 27 | 27 | Potential | ||||||||||||||||||||||||||||||||
| Chain | 28 – 209 | 182 | Thiol:disulfide interchange protein DsbA | PRO_0000245631 | |||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||
| Domain | 28 – 166 | 139 | Thioredoxin | ||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||
| Disulfide bond | 58 ↔ 61 | Redox-active By similarity | |||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||
| Beta strand | 48 – 54 | 7 | |||||||||||||||||||||||||||||||||
| Helix | 59 – 73 | 15 | |||||||||||||||||||||||||||||||||
| Beta strand | 79 – 85 | 7 | |||||||||||||||||||||||||||||||||
| Helix | 93 – 104 | 12 | |||||||||||||||||||||||||||||||||
| Helix | 110 – 119 | 10 | |||||||||||||||||||||||||||||||||
| Turn | 128 – 130 | 3 | |||||||||||||||||||||||||||||||||
| Helix | 134 – 137 | 4 | |||||||||||||||||||||||||||||||||
| Helix | 142 – 149 | 8 | |||||||||||||||||||||||||||||||||
| Helix | 152 – 167 | 16 | |||||||||||||||||||||||||||||||||
| Beta strand | 175 – 177 | 3 | |||||||||||||||||||||||||||||||||
| Beta strand | 182 – 184 | 3 | |||||||||||||||||||||||||||||||||
| Turn | 186 – 188 | 3 | |||||||||||||||||||||||||||||||||
| Helix | 197 – 208 | 12 | |||||||||||||||||||||||||||||||||
Sequences
| ||||||||||||||||||
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: 12822 / ATCC BAA-587 / NCTC 13253. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | BX640436 Genomic DNA. Translation: CAE39633.1. | ||||||||||||
| RefSeq | NP_886482.1. NC_002928.3. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | Q7W2Q0. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| GeneID | 1665561. | ||||||||||||
| GenomeReviews | Gene locus BPP4354 in contig BX470249_GR. | ||||||||||||
| KEGG | bpa:BPP4354. | ||||||||||||
| PATRIC | 21152831. VBIBorPar43418_4569. | ||||||||||||
Organism-specific databases | |||||||||||||
| CMR | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOGENOM | HBG680642. | ||||||||||||
| OMA | THEALYA. | ||||||||||||
| PhylomeDB | Q7W2Q0. | ||||||||||||
| ProtClustDB | CLSK919918. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | BPAR257311:BPP4354-MONOMER. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR001853. DSBA-like_thioredoxin_dom. IPR023205. Thiol:disulphide_interchange. IPR012336. Thioredoxin-like_fold. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit. | ||||||||||||
| KO | K03673. | ||||||||||||
| Pfam | PF01323. DSBA. 1 hit. PF00085. Thioredoxin. 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_BORPA | ||||||||
| Accession | Primary (citable) accession number: Q7W2Q0 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with