P0A2I0 (DSBA_SALEN) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 33.
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 | Salmonella enteritidis | ||
| Taxonomic identifier | 149539 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella |
Protein attributes
| Sequence length | 207 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 | Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. It is required for pilus biogenesis 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 |
| 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 – 19 | 19 | By similarity | ||||||||
| Chain | 20 – 207 | 188 | Thiol:disulfide interchange protein DsbA | PRO_0000034264 | |||||||
Regions | |||||||||||
| Domain | 20 – 158 | 139 | Thioredoxin | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 49 ↔ 52 | Redox-active By similarity | |||||||||
Sequences
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References
| [1] | Mendoza-del-Cueto M.T., Rotger-Anglada R. Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 82139. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF067152 Genomic DNA. Translation: AAC17906.1. |
3D structure databases | |
| ProteinModelPortal | P0A2I0. |
| SMR | P0A2I0. Positions 20-207. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | P0A2I0. |
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_SALEN | ||||||||
| Accession | Primary (citable) accession number: P0A2I0 Secondary accession number(s): O30848, O69191 | ||||||||
| 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