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P0A2I0 (DSBA_SALEN) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thiol:disulfide interchange protein DsbA
Gene names
Name:dsbA
OrganismSalmonella enteritidis
Taxonomic identifier149539 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length207 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred 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 componentPeriplasm
   DomainRedox-active center
Signal
   PTMDisulfide bond
Gene Ontology (GO)
   Biological processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

   Cellular componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionprotein disulfide oxidoreductase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 By similarity
Chain20 – 207188Thiol:disulfide interchange protein DsbA
PRO_0000034264

Regions

Domain20 – 158139Thioredoxin

Amino acid modifications

Disulfide bond49 ↔ 52Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A2I0 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 8260C50145FD3655

FASTA20722,911
        10         20         30         40         50         60 
MKKIWLALAG MVLAFSASAA QISDGKQYIT LDKPVAGEPQ VLEFFSFYCP HCYQFEEVLH 

        70         80         90        100        110        120 
VSDNVKKKLP EGTKMTKYHV EFLGPLGKEL TQAWAVAMAL GVEDKVTVPL FEAVQKTQTV 

       130        140        150        160        170        180 
QSAADIRKVF VDAGVKGEDY DAAWNSFVVK SLVAQQEKAA ADLQLQGVPA MFVNGKYQIN 

       190        200 
PQGMDTSSMD VFVQQYADTV KYLVDKK 

« Hide

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

ProteinModelPortalP0A2I0.
SMRP0A2I0. Positions 20-207.
ModBaseSearch...

Proteomic databases

PRIDEP0A2I0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR001853. DSBA-like_thioredoxin_dom.
IPR023205. Thiol:disulphide_interchange.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 2 hits.
PfamPF01323. DSBA. 1 hit.
[Graphical view]
PIRSFPIRSF001488. Tdi_protein. 1 hit.
SUPFAMSSF52833. Thiordxn-like_fd. 1 hit.
PROSITEPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDSBA_SALEN
AccessionPrimary (citable) accession number: P0A2I0
Secondary accession number(s): O30848, O69191
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: December 14, 2011
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families