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Protein

Thiol:disulfide interchange protein DsbA

Gene

dsbA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 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. Required for pilus biogenesis. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway.2 Publications

GO - Molecular functioni

  • protein disulfide isomerase activity Source: EcoliWiki
  • protein disulfide oxidoreductase activity Source: EcoCyc

GO - Biological processi

  • cell redox homeostasis Source: InterPro
  • cellular response to antibiotic Source: EcoliWiki

Enzyme and pathway databases

BioCyciEcoCyc:DISULFOXRED-MONOMER.
MetaCyc:DISULFOXRED-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Thiol:disulfide interchange protein DsbA
Gene namesi
Name:dsbA
Synonyms:dsf, ppfA
Ordered Locus Names:b3860, JW3832
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11297. dsbA.

Subcellular locationi

GO - Cellular componenti

  • outer membrane-bounded periplasmic space Source: EcoCyc

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Disruption phenotypei

Induction of the PhoP/PhoQ two-component regulatory system, suppressed by 50 µM CuSO4.1 Publication

Chemistry databases

ChEMBLiCHEMBL3559645.
DrugBankiDB08689. UBIQUINONE-1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 193 PublicationsAdd BLAST19
ChainiPRO_000003425220 – 208Thiol:disulfide interchange protein DsbAAdd BLAST189

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi49 ↔ 52Redox-activePROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP0AEG4.
PRIDEiP0AEG4.

2D gel databases

SWISS-2DPAGEiP0AEG4.

Interactioni

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi4261200. 132 interactors.
DIPiDIP-35886N.
IntActiP0AEG4. 20 interactors.
MINTiMINT-1247943.
STRINGi316385.ECDH10B_4049.

Chemistry databases

BindingDBiP0AEG4.

Structurei

Secondary structure

1208
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni25 – 27Combined sources3
Beta strandi28 – 30Combined sources3
Beta strandi40 – 45Combined sources6
Helixi50 – 57Combined sources8
Helixi61 – 66Combined sources6
Beta strandi75 – 79Combined sources5
Beta strandi81 – 84Combined sources4
Helixi85 – 101Combined sources17
Helixi104 – 116Combined sources13
Helixi124 – 133Combined sources10
Helixi138 – 146Combined sources9
Helixi148 – 163Combined sources16
Beta strandi168 – 174Combined sources7
Turni175 – 177Combined sources3
Beta strandi178 – 180Combined sources3
Helixi182 – 184Combined sources3
Helixi190 – 205Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A23NMR-A20-208[»]
1A24NMR-A20-208[»]
1A2JX-ray2.00A20-208[»]
1A2LX-ray2.70A/B20-208[»]
1A2MX-ray2.70A/B20-208[»]
1AC1X-ray2.00A/B20-208[»]
1ACVX-ray1.90A/B20-208[»]
1BQ7X-ray2.80A/B/C/D/E/F20-208[»]
1DSBX-ray2.00A/B20-208[»]
1FVJX-ray2.06A/B20-208[»]
1FVKX-ray1.70A/B20-208[»]
1TI1X-ray2.60A20-208[»]
1U3AX-ray2.00A/B/D/E20-208[»]
1UN2X-ray2.40A20-118[»]
2B3SX-ray1.96A/B20-208[»]
2B6MX-ray2.65A/B20-208[»]
2HI7X-ray3.70A20-208[»]
2LEGNMR-A20-208[»]
2NDONMR-A20-208[»]
2ZUPX-ray3.70A20-208[»]
3E9JX-ray3.70B/E20-208[»]
4TKYX-ray2.50A/B/C/D20-208[»]
4ZIJX-ray1.78A/B20-207[»]
ProteinModelPortaliP0AEG4.
SMRiP0AEG4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AEG4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – 150ThioredoxinPROSITE-ProRule annotationAdd BLAST131

Sequence similaritiesi

Belongs to the thioredoxin family. DsbA subfamily.Curated

Keywords - Domaini

Redox-active center, Signal

Phylogenomic databases

eggNOGiENOG4108Z33. Bacteria.
COG0526. LUCA.
HOGENOMiHOG000265316.
InParanoidiP0AEG4.
KOiK03673.
PhylomeDBiP0AEG4.

Family and domain databases

CDDicd03019. DsbA_DsbA. 1 hit.
InterProiView protein in InterPro
IPR001853. DSBA-like_thioredoxin_dom.
IPR023205. DsbA/DsbL.
IPR036249. Thioredoxin-like_sf.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
PfamiView protein in Pfam
PF01323. DSBA. 1 hit.
PIRSFiPIRSF001488. Tdi_protein. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiView protein in PROSITE
PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P0AEG4-1 [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

VKYLSEKK
Length:208
Mass (Da):23,105
Last modified:December 6, 2005 - v1
Checksum:i10527E876FCAEE55
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80762 Genomic DNA. Translation: CAA56736.1.
M77746 Genomic DNA. Translation: AAA23715.1.
X63186 Genomic DNA. Translation: CAA44868.1.
L19201 Genomic DNA. Translation: AAB02995.1.
U00096 Genomic DNA. Translation: AAC76858.1.
AP009048 Genomic DNA. Translation: BAE77448.1.
U35817 Genomic DNA. Translation: AAC43519.1.
U35818 Genomic DNA. Translation: AAC43520.1.
U35819 Genomic DNA. Translation: AAC43521.1.
U35820 Genomic DNA. Translation: AAC43522.1.
U35821 Genomic DNA. Translation: AAC43523.1.
U35822 Genomic DNA. Translation: AAC43524.1.
U35823 Genomic DNA. Translation: AAC43525.1.
U35824 Genomic DNA. Translation: AAC43526.1.
U35825 Genomic DNA. Translation: AAC43527.1.
U36828 Genomic DNA. Translation: AAC43528.1.
U36829 Genomic DNA. Translation: AAC43529.1.
U36830 Genomic DNA. Translation: AAC43530.1.
U36831 Genomic DNA. Translation: AAC43531.1.
U36832 Genomic DNA. Translation: AAC43532.1.
U36833 Genomic DNA. Translation: AAC43533.1.
U36834 Genomic DNA. Translation: AAC43534.1.
U36835 Genomic DNA. Translation: AAC43535.1.
U35662 Genomic DNA. Translation: AAA82614.1.
PIRiA39292.
RefSeqiNP_418297.1. NC_000913.3.
WP_000725337.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76858; AAC76858; b3860.
BAE77448; BAE77448; BAE77448.
GeneIDi948353.
KEGGiecj:JW3832.
eco:b3860.
PATRICifig|1411691.4.peg.2855.

Similar proteinsi

Entry informationi

Entry nameiDSBA_ECOLI
AccessioniPrimary (citable) accession number: P0AEG4
Secondary accession number(s): P24991
, Q2M8F8, Q46951, Q46952
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: October 25, 2017
This is version 110 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families