Reviewed, UniProtKB/Swiss-Prot P0AEG4 (DSBA_ECOLI)

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) [Complete 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
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 binding Inferred from physical interaction. Source: IntAct protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
dsbB	P0A6M2	1	EBI-549711,EBI-1170740
rpsB	P0A7V0	1	EBI-549711,EBI-543439

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

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.14

Secondary structure

1

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208

Helix Strand Turn

Details...

Helix

1 – 10

10

Turn

25 – 27

3

Beta strand

28 – 30

3

Beta strand

40 – 45

6

Helix

50 – 57

8

Helix

61 – 68

8

Beta strand

75 – 79

5

Beta strand

81 – 84

4

Helix

85 – 100

16

Helix

104 – 116

13

Helix

124 – 133

10

Helix

138 – 145

8

Helix

148 – 163

16

Beta strand

168 – 174

7

Turn

175 – 177

3

Beta strand

178 – 180

3

Helix

182 – 184

3

Helix

190 – 205

16

Sequences

	Sequence		Length	Mass (Da)
	P0AEG4-1 [UniParc]. Last modified December 6, 2005. Version 1. Checksum: 10527E876FCAEE55	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

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: 1934062] [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: 1740115] [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: 8346018] [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: 9278503] [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: 16738553] [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: 8494885] [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: 9298646] [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: 9600841] [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: 8521518] [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: 1429594] [Abstract] Cited for: FUNCTION.
[12]	"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: 8413591] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[13]	"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: 9194175] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[14]	"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: 9300489] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF HIS-51 MUTANTS, DISULFIDE BOND.
[15]	"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: 9655827] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[16]	"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: 9572841] [Abstract] Cited for: STRUCTURE BY NMR.
[17]	"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: 10210188] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[18]	"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: 15755450] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT ALA-52 OF 20-208.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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

AP_003947.1.
NP_418297.1.

3D structure databases

PDBPDBe

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	[»]
2ZUP	X-ray	3.70	A	20-208	[»]
3E9J	X-ray	3.70	B/E	20-208	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P0AEG4. 18 interactions.

2-D gel databases

SWISS-2DPAGE

P0AEG4.

ECO2DBASE

E021.1. 6TH EDITION.
E021.2. 6TH EDITION.

Genome annotation databases

GeneID

948353.

GenomeReviews

Gene locus JW3832 in contig AP009048_GR.
Gene locus b3860 in contig U00096_GR.

KEGG

ecj:JW3832.
eco:b3860.

Organism-specific databases

EchoBASE

EB1274.

EcoGene

EG11297. dsbA.

CMR

Search...

Phylogenomic databases

HOGENOM

P0AEG4.

OMA

P0AEG4. EGVHYEV.

Enzyme and pathway databases

BioCyc

EcoCyc:DISULFOXRED-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_ECOLI

Accession

Primary (citable) accession number: P0AEG4
Secondary accession number(s): P24991 , Q2M8F8, Q46951, Q46952

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	December 6, 2005
Last modified:	June 16, 2009
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)