Thiol:disulfide interchange protein DsbA precursor

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P0AEG4 (DSBA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 76. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Thiol:disulfide interchange protein DsbA

Gene names

Name:	dsbA
Synonyms:	dsf, ppfA
Ordered Locus Names:	b3860, JW3832

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

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. Ref.11

Subcellular location

Periplasm.

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 Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro cellular response to antibiotic Inferred from mutant phenotype PubMed 7628442. Source: EcoliWiki
Cellular_component	outer membrane-bounded periplasmic space Inferred from direct assay Ref.1. Source: EcoCyc
Molecular_function	protein disulfide isomerase activity Inferred from direct assay Ref.1. Source: EcoliWiki protein disulfide oxidoreductase activity Inferred from direct assay Ref.1. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
phoA	P00634	2	EBI-549711,EBI-552958

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

Ref.7 Ref.8 Ref.9

Chain

20 – 208

189

Thiol:disulfide interchange protein DsbA

PRO_0000034252

Regions

Domain

20 – 150

131

Thioredoxin

Amino acid modifications

Disulfide bond

49 ↔ 52

Redox-active Ref.15

Secondary structure

208

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0AEG4 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 10527E876FCAEE55
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FASTA

208

23,105

        10         20         30         40         50         60 
MKKIWLALAG LVLAFSASAA QYEDGKQYTT LEKPVAGAPQ VLEFFSFFCP HCYQFEEVLH 

        70         80         90        100        110        120 
ISDNVKKKLP EGVKMTKYHV NFMGGDLGKD LTQAWAVAMA LGVEDKVTVP LFEGVQKTQT 

       130        140        150        160        170        180 
IRSASDIRDV FINAGIKGEE YDAAWNSFVV KSLVAQQEKA AADVQLRGVP AMFVNGKYQL 

       190        200 
NPQGMDTSNM DVFVQQYADT VKYLSEKK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a protein required for disulfide bond formation in vivo." Bardwell J.C.A., McGovern K., Beckwith J. Cell 67:581-589(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme." Kamitani S., Akiyama Y., Ito K. EMBO J. 11:57-62(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[3]	"Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes." Plunkett G. III, Burland V., Daniels D.L., Blattner F.R. Nucleic Acids Res. 21:3391-3398(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	Grauschopf U., Winther J., Korber P., Zander T., Dallinger P., Bardwell J.C.A. Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49.
[7]	"The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo." Zapun A., Bardwell J.C.A., Creighton T.E. Biochemistry 32:5083-5092(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-24, CHARACTERIZATION.
[8]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-31. Strain: K12 / EMG2.
[9]	"Protein identification with N and C-terminal sequence tags in proteome projects." Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F. J. Mol. Biol. 278:599-608(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-23. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[10]	"Why is DsbA such an oxidizing disulfide catalyst?" Grauschopf U., Winther J.R., Korber P., Zander T., Dallinger P., Bardwell J.C.A. Cell 83:947-955(1995) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF PRO-50 AND HIS-51.
[11]	"In vitro catalysis of oxidative folding of disulfide-bonded proteins by the Escherichia coli dsbA (ppfA) gene product." Akiyama Y., Kamitani S., Kusukawa N., Ito K. J. Biol. Chem. 267:22440-22445(1992) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[13]	"Crystal structure of the DsbA protein required for disulphide bond formation in vivo." Martin J.L., Bardwell J.C.A., Kuriyan J. Nature 365:464-468(1993) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[14]	"The uncharged surface features surrounding the active site of Escherichia coli DsbA are conserved and are implicated in peptide binding." Guddat L.W., Bardwell J.C.A., Zander T., Martin J.L. Protein Sci. 6:1148-1156(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[15]	"Structural analysis of three His32 mutants of DsbA: support for an electrostatic role of His32 in DsbA stability." Guddat L.W., Bardwell J.C.A., Glockshuber R., Huber-Wunderlich M., Zander T., Martin J.L. Protein Sci. 6:1893-1900(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF HIS-51 MUTANTS, DISULFIDE BOND.
[16]	"Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization." Guddat L.W., Bardwell J.C.A., Martin J.L. Structure 6:757-767(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[17]	"Structure of reduced DsbA from Escherichia coli in solution." Schirra H.J., Renner C., Czisch M., Huber-Wunderlich M., Holak T.A., Glockshuber R. Biochemistry 37:6263-6276(1998) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
[18]	"On the role of the cis-proline residue in the active site of DsbA." Charbonnier J.-B., Belin P., Moutiez M., Stura E.A., Quemeneur E. Protein Sci. 8:96-105(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[19]	"Intriguing conformation changes associated with the trans/cis isomerization of a prolyl residue in the active site of the DsbA C33A mutant." Ondo-Mbele E., Vives C., Kone A., Serre L. J. Mol. Biol. 347:555-563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT ALA-52 OF 20-208.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

A39292.

RefSeq

NP_418297.1. NC_000913.2.
YP_491589.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A23	NMR	-	A	20-208	[»]
1A24	NMR	-	A	20-208	[»]
1A2J	X-ray	2.00	A	20-208	[»]
1A2L	X-ray	2.70	A/B	20-208	[»]
1A2M	X-ray	2.70	A/B	20-208	[»]
1AC1	X-ray	2.00	A/B	20-208	[»]
1ACV	X-ray	1.90	A/B	20-208	[»]
1BQ7	X-ray	2.80	A/B/C/D/E/F	20-208	[»]
1DSB	X-ray	2.00	A/B	20-208	[»]
1FVJ	X-ray	2.06	A/B	20-208	[»]
1FVK	X-ray	1.70	A/B	20-208	[»]
1TI1	X-ray	2.60	A	20-208	[»]
1U3A	X-ray	2.00	A/B/D/E	20-208	[»]
1UN2	X-ray	2.40	A	20-208	[»]
2B3S	X-ray	1.96	A/B	20-208	[»]
2B6M	X-ray	2.65	A/B	20-208	[»]
2HI7	X-ray	3.70	A	20-208	[»]
2LEG	NMR	-	A	20-208	[»]
2ZUP	X-ray	3.70	A	20-208	[»]
3E9J	X-ray	3.70	B/E	20-208	[»]

ProteinModelPortal

P0AEG4.

SMR

P0AEG4. Positions 20-207.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35886N.

IntAct

P0AEG4. 19 interactions.

MINT

MINT-1247943.

STRING

511145.b3860.

2D gel databases

SWISS-2DPAGE

P0AEG4.

Proteomic databases

PaxDb

P0AEG4.

PRIDE

P0AEG4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76858; AAC76858; b3860.
BAE77448; BAE77448; BAE77448.

GeneID

12932206.
948353.

KEGG

ecj:Y75_p3325.
eco:b3860.

PATRIC

32123217. VBIEscCol129921_3969.

Organism-specific databases

EchoBASE

EB1274.

EcoGene

EG11297. dsbA.

Phylogenomic databases

eggNOG

COG0526.

HOGENOM

HOG000265316.

K03673.

OMA

YMVKNDG.

ProtClustDB

PRK10954.

Enzyme and pathway databases

BioCyc

EcoCyc:DISULFOXRED-MONOMER.
ECOL316407:JW3832-MONOMER.
MetaCyc:DISULFOXRED-MONOMER.

Gene expression databases

Genevestigator

P0AEG4.

Family and domain databases

Gene3D

3.40.30.10. 2 hits.

InterPro

IPR001853. DSBA-like_thioredoxin_dom.
IPR023205. Thiol:disulphide_interchange.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
[Graphical view]

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...

Other

EvolutionaryTrace

P0AEG4.

Entry information

Entry name

DSBA_ECOLI

Accession

Primary (citable) accession number: P0AEG4
Secondary accession number(s): P24991

Q46952

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	December 6, 2005
Last modified:	May 1, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents