Reviewed,
UniProtKB/Swiss-Prot P52235 (DSBA_SHIFL)
Last modified
July 7, 2009.
Version 66.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Thiol:disulfide interchange protein dsbA | ||||
| Gene names |
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| Organism | Shigella flexneri [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 623 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella |
Protein attributes
| Sequence length | 208 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 | 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. |
| Subcellular location | |
| 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 | outer membrane-bounded periplasmic space Inferred from electronic annotation. Source: InterPro |
| 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 – 208 | 189 | Thiol:disulfide interchange protein dsbA | PRO_0000034267 | |||||||
Regions | |||||||||||
| Domain | 20 – 150 | 131 | Thioredoxin | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 49 ↔ 52 | Redox-active By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 68 | 1 | K → I in BAA07407. Ref.1 | ||||||||
| Sequence conflict | 98 | 1 | A → V in BAA07407. Ref.1 | ||||||||
| Sequence conflict | 134 | 1 | A → E in BAA07407. Ref.1 | ||||||||
| Sequence conflict | 161 | 1 | A → E in BAA07407. Ref.1 | ||||||||
| Sequence conflict | 183 – 185 | 3 | QGM → KGL in BAA07407. Ref.1 | ||||||||
| Sequence conflict | 207 | 1 | E → K in BAA07407. Ref.1 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Disulfide oxidoreductase activity of Shigella flexneri is required for release of Ipa proteins and invasion of epithelial cells." Watarai M., Tobe T., Yoshikawa M., Sasakawa C. Proc. Natl. Acad. Sci. U.S.A. 92:4927-4931(1995) [PubMed: 7761426] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: YSH6000 / Serotype 2a. |
| [2] | "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157." Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. Yu J.Nucleic Acids Res. 30:4432-4441(2002) [PubMed: 12384590] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 301 / Serotype 2a. |
| [3] | "Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T." Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R. Infect. Immun. 71:2775-2786(2003) [PubMed: 12704152] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700930 / 2457T / Serotype 2a. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| D38253 Genomic DNA. Translation: BAA07407.1. AE005674 Genomic DNA. Translation: AAN45366.1. AE014073 Genomic DNA. Translation: AAP18832.1. | |||||||||||||
| RefSeq | NP_709659.1. NP_839021.1. | ||||||||||||
3D structure databases | |||||||||||||
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| SMR | P52235. Positions 20-207. | ||||||||||||
| ModBase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| GeneID | 1023438. 1080031. | ||||||||||||
| GenomeReviews | Gene locus SF3931 in contig AE005674_GR. Gene locus S3816 in contig AE014073_GR. | ||||||||||||
| KEGG | sfl:SF3931. sfx:S3816. | ||||||||||||
Organism-specific databases | |||||||||||||
| CMR | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOGENOM | P52235. | ||||||||||||
| OMA | P52235. EGVHYEV. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | SFLE198214:AAN45366.1-MON. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR001853. OxRdtase_DSBA. IPR017936. Thioredoxin-like. IPR017937. Thioredoxin_CS. IPR012335. Thioredoxin_fold. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit. | ||||||||||||
| Pfam | PF01323. DSBA. 1 hit. [Graphical view] | ||||||||||||
| PROSITE | PS00194. THIOREDOXIN_1. 1 hit. PS51352. THIOREDOXIN_2. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | DSBA_SHIFL | ||||||||
| Accession | Primary (citable) accession number: P52235 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


