Reviewed,
UniProtKB/Swiss-Prot Q5PIQ0 (DSBD_SALPA)
Last modified
June 16, 2009.
Version 41.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Thiol:disulfide interchange protein dsbD EC=1.8.1.8 Alternative name(s): Protein-disulfide reductase Short name=Disulfide reductase | ||||
| Gene names |
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| Organism | Salmonella paratyphi A [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 54388 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella |
Protein attributes
| Sequence length | 567 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 to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps By similarity. |
| Catalytic activity | Protein dithiol + NAD(P)+ = protein disulfide + NAD(P)H. HAMAP MF_00399 |
| Subcellular location | Cell inner membrane; Multi-pass membrane protein By similarity. |
| Sequence similarities | Belongs to the thioredoxin family. DsbD subfamily. Contains 1 thioredoxin domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cytochrome c-type biogenesis Electron transport Transport |
| Cellular component | Cell inner membrane Cell membrane Membrane |
| Domain | Redox-active center Signal Transmembrane |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| PTM | Disulfide bond |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | cell redox homeostasis Inferred from electronic annotation. Source: InterPro cytochrome complex assemblyInferred from electronic annotation. Source: HAMAP electron transport chainInferred from electronic annotation. Source: UniProtKB-KW transportInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | electron carrier activity Inferred from electronic annotation. Source: HAMAP protein-disulfide reductase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 19 | 19 | Potential | ||||||||
| Chain | 20 – 567 | 548 | Thiol:disulfide interchange protein dsbD HAMAP MF_00399 | PRO_0000304395 | |||||||
Regions | |||||||||||
| Transmembrane | 166 – 186 | 21 | Potential | ||||||||
| Transmembrane | 211 – 231 | 21 | Potential | ||||||||
| Transmembrane | 246 – 266 | 21 | Potential | ||||||||
| Transmembrane | 299 – 319 | 21 | Potential | ||||||||
| Transmembrane | 326 – 346 | 21 | Potential | ||||||||
| Transmembrane | 360 – 380 | 21 | Potential | ||||||||
| Transmembrane | 387 – 407 | 21 | Potential | ||||||||
| Transmembrane | 418 – 438 | 21 | Potential | ||||||||
| Domain | 435 – 567 | 133 | Thioredoxin | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 122 ↔ 128 | Redox-active By similarity | |||||||||
| Disulfide bond | 185 ↔ 307 | Redox-active By similarity | |||||||||
| Disulfide bond | 482 ↔ 485 | Redox-active By similarity | |||||||||
Sequences
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References
| [1] | "Comparison of genome degradation in Paratyphi A and Typhi, human-restricted serovars of Salmonella enterica that cause typhoid." McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S., Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R., Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F. Wilson R.K.Nat. Genet. 36:1268-1274(2004) [PubMed: 15531882] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 9150 / SARB42. |
Cross-references
Sequence databases | |
|---|---|
| CP000026 Genomic DNA. Translation: AAV79880.1. | |
| RefSeq | YP_153192.1. |
3D structure databases | |
| SMR | Q5PIQ0. Positions 23-143, 449-567. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 3176146. |
| GenomeReviews | Gene locus SPA4139 in contig CP000026_GR. |
| KEGG | spt:SPA4139. |
| NMPDR | fig|295319.3.peg.3423. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q5PIQ0. |
| OMA | Q5PIQ0. TITHILW. |
Enzyme and pathway databases | |
| BioCyc | SENT295319:SPA4139-MON. |
Family and domain databases | |
| HAMAP | MF_00399. [Tree] |
| InterPro | IPR003834. Cyt_c_assmbl_TM. IPR017936. Thioredoxin-like. IPR015467. Thioredoxin_core. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. IPR012335. Thioredoxin_fold. [Graphical view] |
| Gene3D | G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit. |
| PANTHER | PTHR10438. Trx. 1 hit. |
| Pfam | PF02683. DsbD. 1 hit. PF00085. Thioredoxin. 1 hit. [Graphical view] |
| PROSITE | PS00194. THIOREDOXIN_1. 1 hit. PS51352. THIOREDOXIN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DSBD_SALPA | ||||||||
| Accession | Primary (citable) accession number: Q5PIQ0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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