P0C2B2 (DSBA_PSEAE) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 36.
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 | Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) | ||||
| Taxonomic identifier | 208964 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas |
Protein attributes
| Sequence length | 211 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 Reference 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 – 22 | 22 | Potential | ||||||||||||||||||||||||||||||||||||
| Chain | 23 – 211 | 189 | Thiol:disulfide interchange protein DsbA | PRO_0000034262 | |||||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||||
| Domain | 23 – 203 | 181 | Thioredoxin | ||||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 56 ↔ 59 | Redox-active Potential | |||||||||||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 209 | 1 | Missing Ref.1 | ||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||
| Helix | 22 – 24 | 3 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 31 – 33 | 3 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 46 – 52 | 7 | |||||||||||||||||||||||||||||||||||||
| Helix | 57 – 71 | 15 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 77 – 83 | 7 | |||||||||||||||||||||||||||||||||||||
| Turn | 90 – 92 | 3 | |||||||||||||||||||||||||||||||||||||
| Helix | 96 – 102 | 7 | |||||||||||||||||||||||||||||||||||||
| Helix | 107 – 118 | 12 | |||||||||||||||||||||||||||||||||||||
| Helix | 127 – 134 | 8 | |||||||||||||||||||||||||||||||||||||
| Helix | 141 – 148 | 8 | |||||||||||||||||||||||||||||||||||||
| Turn | 151 – 153 | 3 | |||||||||||||||||||||||||||||||||||||
| Helix | 157 – 167 | 11 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 174 – 177 | 4 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 181 – 184 | 4 | |||||||||||||||||||||||||||||||||||||
| Helix | 192 – 210 | 19 | |||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning and sequencing of a dsbA-homologous gene from Pseudomonas aeruginosa." Leipelt M., Schneidinger B., Jaeger K.-E. Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228. |
| [2] | "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen." Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. Olson M.V.Nature 406:959-964(2000) [PubMed: 10984043] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | U84726 Genomic DNA. Translation: AAB41795.1. AE004091 Genomic DNA. Translation: AAG08874.1. | ||||||||||||
| PIR | H82960. | ||||||||||||
| RefSeq | NP_254176.1. NC_002516.2. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P0C2B2. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| GeneID | 877731. | ||||||||||||
| GenomeReviews | Gene locus PA5489 in contig AE004091_GR. | ||||||||||||
| KEGG | pae:PA5489. | ||||||||||||
| PATRIC | 19845865. VBIPseAer58763_5754. | ||||||||||||
Organism-specific databases | |||||||||||||
| PseudoCAP | PA5489. | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOGENOM | HBG680642. | ||||||||||||
| OMA | EVPKIKA. | ||||||||||||
| ProtClustDB | CLSK869391. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | PAER208964:PA5489-MONOMER. | ||||||||||||
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. | ||||||||||||
| KO | K03673. | ||||||||||||
| 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_PSEAE | ||||||||
| Accession | Primary (citable) accession number: P0C2B2 Secondary accession number(s): P95460 | ||||||||
| Entry history |
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| 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 |

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