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Protein

Thiol:disulfide interchange protein DsbA

Gene

dsbA

Organism
Shigella flexneri
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Thiol:disulfide interchange protein DsbA
Gene namesi
Name:dsbA
Ordered Locus Names:SF3931, S3816
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
Proteomesi
  • UP000002673 Componenti: Chromosome
  • UP000001006 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919By similarityAdd
BLAST
Chaini20 – 208189Thiol:disulfide interchange protein DsbAPRO_0000034267Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi49 ↔ 52Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP52235.

Interactioni

Protein-protein interaction databases

STRINGi198214.SF3931.

Structurei

Secondary structure

1
208
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni25 – 273Combined sources
Beta strandi28 – 303Combined sources
Beta strandi40 – 456Combined sources
Helixi50 – 578Combined sources
Helixi61 – 688Combined sources
Beta strandi75 – 795Combined sources
Beta strandi81 – 844Combined sources
Helixi85 – 10117Combined sources
Helixi104 – 11613Combined sources
Helixi124 – 13310Combined sources
Helixi138 – 1458Combined sources
Helixi148 – 16316Combined sources
Beta strandi168 – 1747Combined sources
Turni175 – 1773Combined sources
Beta strandi178 – 1803Combined sources
Helixi182 – 1843Combined sources
Helixi190 – 20516Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DKSX-ray1.90A/B/C/D20-208[»]
ProteinModelPortaliP52235.
SMRiP52235. Positions 20-208.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52235.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 150131ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the thioredoxin family. DsbA subfamily.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Signal

Phylogenomic databases

eggNOGiENOG4108Z33. Bacteria.
COG0526. LUCA.
HOGENOMiHOG000265316.
KOiK03673.
OMAiDKVSPLM.
OrthoDBiEOG68Q0Q6.

Family and domain databases

Gene3Di3.40.30.10. 2 hits.
InterProiIPR001853. DSBA-like_thioredoxin_dom.
IPR023205. DsbA/DsbL.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
[Graphical view]
PfamiPF01323. DSBA. 1 hit.
[Graphical view]
PIRSFiPIRSF001488. Tdi_protein. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P52235-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKIWLALAG LVLAFSASAA QYEDGKQYTT LEKPVAGAPQ VLEFFSFFCP
60 70 80 90 100
HCYQFEEVLH ISDNVKKKLP EGVKMTKYHV NFMGGDLGKD LTQAWAVAMA
110 120 130 140 150
LGVEDKVTVP LFEGVQKTQT IRSASDIRDV FINAGIKGEE YDAAWNSFVV
160 170 180 190 200
KSLVAQQEKA AADVQLRGVP AMFVNGKYQL NPQGMDTSNM DVFVQQYADT

VKYLSEEK
Length:208
Mass (Da):23,105
Last modified:January 10, 2003 - v2
Checksum:i105A5E876FCAEE55
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti68 – 681K → I in BAA07407 (PubMed:7761426).Curated
Sequence conflicti98 – 981A → V in BAA07407 (PubMed:7761426).Curated
Sequence conflicti134 – 1341A → E in BAA07407 (PubMed:7761426).Curated
Sequence conflicti161 – 1611A → E in BAA07407 (PubMed:7761426).Curated
Sequence conflicti183 – 1853QGM → KGL in BAA07407 (PubMed:7761426).Curated
Sequence conflicti207 – 2071E → K in BAA07407 (PubMed:7761426).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38253 Genomic DNA. Translation: BAA07407.1.
AE005674 Genomic DNA. Translation: AAN45366.1.
AE014073 Genomic DNA. Translation: AAP18832.1.
RefSeqiNP_709659.1. NC_004337.2.
WP_000725335.1. NZ_LM651928.1.

Genome annotation databases

EnsemblBacteriaiAAN45366; AAN45366; SF3931.
AAP18832; AAP18832; S3816.
GeneIDi1023438.
KEGGisfl:SF3931.
sfx:S3816.
PATRICi18709501. VBIShiFle31049_4175.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38253 Genomic DNA. Translation: BAA07407.1.
AE005674 Genomic DNA. Translation: AAN45366.1.
AE014073 Genomic DNA. Translation: AAP18832.1.
RefSeqiNP_709659.1. NC_004337.2.
WP_000725335.1. NZ_LM651928.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DKSX-ray1.90A/B/C/D20-208[»]
ProteinModelPortaliP52235.
SMRiP52235. Positions 20-208.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198214.SF3931.

Proteomic databases

PaxDbiP52235.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN45366; AAN45366; SF3931.
AAP18832; AAP18832; S3816.
GeneIDi1023438.
KEGGisfl:SF3931.
sfx:S3816.
PATRICi18709501. VBIShiFle31049_4175.

Phylogenomic databases

eggNOGiENOG4108Z33. Bacteria.
COG0526. LUCA.
HOGENOMiHOG000265316.
KOiK03673.
OMAiDKVSPLM.
OrthoDBiEOG68Q0Q6.

Miscellaneous databases

EvolutionaryTraceiP52235.

Family and domain databases

Gene3Di3.40.30.10. 2 hits.
InterProiIPR001853. DSBA-like_thioredoxin_dom.
IPR023205. DsbA/DsbL.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
[Graphical view]
PfamiPF01323. DSBA. 1 hit.
[Graphical view]
PIRSFiPIRSF001488. Tdi_protein. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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.
    , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
    Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 301 / Serotype 2a.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700930 / 2457T / Serotype 2a.

Entry informationi

Entry nameiDSBA_SHIFL
AccessioniPrimary (citable) accession number: P52235
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 10, 2003
Last modified: November 11, 2015
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.