Q9PHR3 (DSBD_CAMJE) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 81.
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 DsbD EC=1.8.1.8 Alternative name(s): Protein-disulfide reductase Short name=Disulfide reductase | ||||
| Gene names |
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| Organism | Campylobacter jejuni | ||||
| Taxonomic identifier | 197 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter |
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. HAMAP MF_00399 |
| 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 HAMAP MF_00399. |
| Sequence similarities | Belongs to the thioredoxin family. DsbD subfamily. Contains 1 thioredoxin domain. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 16 | 16 | Potential | ||||||||
| Chain | 17 – 567 | 551 | Thiol:disulfide interchange protein DsbD HAMAP MF_00399 | PRO_0000007372 | |||||||
Regions | |||||||||||
| Topological domain | 17 – 166 | 150 | Periplasmic Potential | ||||||||
| Transmembrane | 167 – 187 | 21 | Helical; Potential | ||||||||
| Topological domain | 188 – 211 | 24 | Cytoplasmic Potential | ||||||||
| Transmembrane | 212 – 232 | 21 | Helical; Potential | ||||||||
| Topological domain | 233 – 247 | 15 | Periplasmic Potential | ||||||||
| Transmembrane | 248 – 268 | 21 | Helical; Potential | ||||||||
| Topological domain | 269 – 289 | 21 | Cytoplasmic Potential | ||||||||
| Transmembrane | 290 – 310 | 21 | Helical; Potential | ||||||||
| Topological domain | 311 – 332 | 22 | Periplasmic Potential | ||||||||
| Transmembrane | 333 – 353 | 21 | Helical; Potential | ||||||||
| Topological domain | 354 – 361 | 8 | Cytoplasmic Potential | ||||||||
| Transmembrane | 362 – 382 | 21 | Helical; Potential | ||||||||
| Topological domain | 383 – 385 | 3 | Periplasmic Potential | ||||||||
| Transmembrane | 386 – 406 | 21 | Helical; Potential | ||||||||
| Topological domain | 407 – 417 | 11 | Cytoplasmic Potential | ||||||||
| Transmembrane | 418 – 438 | 21 | Helical; Potential | ||||||||
| Topological domain | 439 – 567 | 129 | Periplasmic Potential | ||||||||
| Domain | 430 – 567 | 138 | Thioredoxin | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 111 ↔ 117 | Redox-active By similarity | |||||||||
| Disulfide bond | 186 ↔ 307 | Redox-active By similarity | |||||||||
| Disulfide bond | 488 ↔ 491 | Redox-active By similarity | |||||||||
Sequences
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References
| [1] | "The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. Barrell B.G.Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AL111168 Genomic DNA. Translation: CAL34749.1. |
| PIR | B81408. |
| RefSeq | YP_002344033.1. NC_002163.1. |
3D structure databases | |
| ProteinModelPortal | Q9PHR3. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q9PHR3. 3 interactions. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 904931. |
| GenomeReviews | Gene locus Cj0603c in contig AL111168_GR. |
| KEGG | cje:Cj0603c. |
| PATRIC | 20058150. VBICamJej33762_0595. |
Phylogenomic databases | |
| HOGENOM | HBG640883. |
| OMA | RNGHEIG. |
| PhylomeDB | Q9PHR3. |
| ProtClustDB | CLSK878853. |
Enzyme and pathway databases | |
| BioCyc | CJEJ192222:CJ0603C-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00399. DbsD. [Tree] |
| InterPro | IPR003834. Cyt_c_assmbl_TM_dom. IPR022910. Thiol_diS_interchange_DbsD. IPR005746. Thioredoxin. IPR012336. Thioredoxin-like_fold. IPR013766. Thioredoxin_domain. [Graphical view] |
| Gene3D | G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit. |
| KO | K04084. |
| PANTHER | PTHR10438. Trx. 1 hit. |
| Pfam | PF02683. DsbD. 1 hit. PF00085. Thioredoxin. 1 hit. [Graphical view] |
| SUPFAM | SSF52833. Thiordxn-like_fd. 1 hit. |
| PROSITE | PS00194. THIOREDOXIN_1. False negative. PS51352. THIOREDOXIN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DSBD_CAMJE | ||||||||
| Accession | Primary (citable) accession number: Q9PHR3 Secondary accession number(s): Q0PAR4 | ||||||||
| 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 |

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