Reviewed, UniProtKB/Swiss-Prot P36655 (DSBD_ECOLI)

Names and origin

Protein names

Recommended name:
    Thiol:disulfide interchange protein dsbD
    EC=1.8.1.8
Alternative name(s):
    Protein-disulfide reductase
      Short name=Disulfide reductase
    C-type cytochrome biogenesis protein cycZ
    Inner membrane copper tolerance protein

Gene names

Name:	dsbD
Synonyms:	cutA2, cycZ, dipZ
Ordered Locus Names:	b4136, JW5734

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	565 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 to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm, thereby maintaining the active site of dsbC, dsbE and dsbG in a reduced state. This transfer involves a cascade of disulfide bond formation and reduction steps. HAMAP MF_00399
Catalytic activity	Protein dithiol + NAD(P)+ = protein disulfide + NAD(P)H. HAMAP MF_00399
Subcellular location	Cell inner membrane; Multi-pass membrane protein HAMAP MF_00399.
Miscellaneous	The consequences of replacement of the cysteines with alanines were found to depend on the conditions tested and on the reporter system used for the analysis, and then differ depending on the references. HAMAP MF_00399
Sequence similarities	Belongs to the thioredoxin family. DsbD subfamily. Contains 1 thioredoxin domain.

Ontologies

Keywords
Biological process	Cytochrome c-type biogenesis Electron transport Transport
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Redox-active center Signal Transmembrane
Ligand	NAD
Molecular function	Oxidoreductase
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 cytochrome complex assembly Inferred from electronic annotation. Source: HAMAP electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: HAMAP
Molecular function	electron carrier activity Inferred from electronic annotation. Source: HAMAP protein-disulfide reductase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Ref.8

Chain

20 – 565

546

Thiol:disulfide interchange protein dsbD HAMAP MF_00399

PRO_0000007373

Regions

Topological domain

20 – 162

143

Periplasmic Potential

Transmembrane

163 – 183

21

Potential

Topological domain

184 – 207

24

Cytoplasmic Potential

Transmembrane

208 – 228

21

Potential

Topological domain

229 – 242

14

Periplasmic Potential

Transmembrane

243 – 263

21

Potential

Topological domain

264 – 295

32

Cytoplasmic Potential

Transmembrane

296 – 316

21

Potential

Topological domain

317 – 322

6

Periplasmic Potential

Transmembrane

323 – 343

21

Potential

Topological domain

344 – 356

13

Cytoplasmic Potential

Transmembrane

357 – 377

21

Potential

Topological domain

378 – 383

6

Periplasmic Potential

Transmembrane

384 – 404

21

Potential

Topological domain

405 – 417

13

Cytoplasmic Potential

Transmembrane

418 – 438

21

Potential

Topological domain

439 – 565

127

Periplasmic Potential

Domain

434 – 565

132

Thioredoxin

Amino acid modifications

Disulfide bond

122 ↔ 128

Redox-active Probable

Disulfide bond

182 ↔ 304

Redox-active Probable

Disulfide bond

480 ↔ 483

Redox-active Probable

Experimental info

Mutagenesis

13

1

C → A: No loss of activity. Ref.11

Mutagenesis

122

1

C → A: Loss of activity. Ref.8 Ref.11 Ref.7

Mutagenesis

128

1

C → A: Loss of activity. Ref.8 Ref.11 Ref.7

Mutagenesis

182

1

C → A: Loss of activity. Ref.8 Ref.11 Ref.7

Mutagenesis

301

1

C → A: No loss of activity. Ref.8 Ref.11 Ref.7

Mutagenesis

304

1

C → A: Loss of activity. Ref.8 Ref.11 Ref.7

Mutagenesis

480

1

C → A: Loss of activity; when associated with A-483. Ref.8 Ref.11 Ref.7

Mutagenesis

483

1

C → A: Loss of activity; when associated with A-480. Ref.8 Ref.11 Ref.7

Secondary structure

1

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565

Helix Strand Turn

Details...

Helix

33 – 36

4

Beta strand

37 – 44

8

Beta strand

47 – 54

8

Beta strand

58 – 61

4

Helix

62 – 64

3

Beta strand

66 – 74

9

Beta strand

83 – 87

5

Turn

88 – 90

3

Beta strand

91 – 96

6

Beta strand

98 – 119

22

Beta strand

121 – 123

3

Turn

124 – 126

3

Beta strand

132 – 137

6

Helix

456 – 466

11

Beta strand

471 – 476

6

Helix

481 – 489

9

Turn

490 – 492

3

Helix

494 – 499

6

Turn

500 – 502

3

Beta strand

503 – 509

7

Helix

515 – 523

9

Beta strand

528 – 535

8

Helix

543 – 545

3

Helix

553 – 561

9

Sequences

	Sequence		Length	Mass (Da)
	P36655-1 [UniParc]. Last modified June 1, 2001. Version 4. Checksum: 41EFAA1C9EAC6C5F	FASTA	565	61,795
	10 20 30 40 50 60 MAQRIFTLIL LLCSTSVFAG LFDAPGRSQF VPADQAFAFD FQQNQHDLNL TWQIKDGYYL 70 80 90 100 110 120 YRKQIRITPE HAKIADVQLP QGVWHEDEFY GKSEIYRDRL TLPVTINQAS AGATLTVTYQ 130 140 150 160 170 180 GCADAGFCYP PETKTVPLSE VVANNAAPQP VSVPQQEQPT AQLPFSALWA LLIGIGIAFT 190 200 210 220 230 240 PCVLPMYPLI SGIVLGGKQR LSTARALLLT FIYVQGMALT YTALGLVVAA AGLQFQAALQ 250 260 270 280 290 300 HPYVLIGLAI VFTLLAMSMF GLFTLQLPSS LQTRLTLMSN RQQGGSPGGV FVMGAIAGLI 310 320 330 340 350 360 CSPCTTAPLS AILLYIAQSG NMWLGGGTLY LYALGMGLPL MLITVFGNRL LPKSGPWMEQ 370 380 390 400 410 420 VKTAFGFVIL ALPVFLLERV IGDVWGLRLW SALGVAFFGW AFITSLQAKR GWMRIVQIIL 430 440 450 460 470 480 LAAALVSVRP LQDWAFGATH TAQTQTHLNF TQIKTVDELN QALVEAKGKP VMLDLYADWC 490 500 510 520 530 540 VACKEFEKYT FSDPQVQKAL ADTVLLQANV TANDAQDVAL LKHLNVLGLP TILFFDGQGQ 550 560 EHPQARVTGF MDAETFSAHL RDRQP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli." Missiakas D., Schwager F., Raina S. EMBO J. 14:3415-3424(1995) [PubMed: 7628442] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
[2]	"Molecular genetics of a chromosomal locus involved in copper tolerance in Escherichia coli K-12." Fong S.-T., Camakaris J., Lee B.T.O. Mol. Microbiol. 15:1127-1137(1995) [PubMed: 7623666] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The biogenesis of c-type cytochromes in Escherichia coli requires a membrane-bound protein, DipZ, with a protein disulphide isomerase-like domain." Crooke H.R., Cole J.A. Mol. Microbiol. 15:1139-1150(1995) [PubMed: 7623667] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[4]	"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R. Nucleic Acids Res. 23:2105-2119(1995) [PubMed: 7610040] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"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.
[6]	"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.
[7]	"Escherichia coli DipZ: anatomy of a transmembrane protein disulphide reductase in which three pairs of cysteine residues, one in each of three domains, contribute differentially to function." Gordon E.H.J., Page M.D., Willis A.C., Ferguson S.J. Mol. Microbiol. 35:1360-1374(2000) [PubMed: 10760137] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-8 AND 20-34, TOPOLOGY, MUTAGENESIS OF CYS-122; CYS-128; CYS-182; CYS-301; CYS-304; CYS-480 AND CYS-483.
[8]	"Transfer of electrons across the cytoplasmic membrane by DsbD, a membrane protein involved in thiol-disulphide exchange and protein folding in the bacterial periplasm." Chung J., Chen T., Missiakas D. Mol. Microbiol. 35:1099-1109(2000) [PubMed: 10712691] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-27, TOPOLOGY, MUTAGENESIS OF CYS-122; CYS-128; CYS-182; CYS-301; CYS-304; CYS-480 AND CYS-483. Strain: BL21-DE3.
[9]	Missiakas D., Hughes G.J., Frutiger S., Paquet N., Raina S. Submitted (MAY-1995) to UniProtKB Cited for: PROTEIN SEQUENCE OF 78-82.
[10]	"Specific thiol compounds complement deficiency in c-type cytochrome biogenesis in Escherichia coli carrying a mutation in a membrane-bound disulphide isomerase-like protein." Sambongi Y., Ferguson S.J. FEBS Lett. 353:235-238(1994) [PubMed: 7957865] [Abstract] Cited for: CHARACTERIZATION.
[11]	"Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli." Stewart E.J., Katzen F., Beckwith J. EMBO J. 18:5963-5971(1999) [PubMed: 10545108] [Abstract] Cited for: TOPOLOGY, MUTAGENESIS OF CYS-13; CYS-122; CYS-128; CYS-182; CYS-301; CYS-304; CYS-480 AND CYS-483. Strain: DHB4 and RI242.
[12]	"Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade." Katzen F., Beckwith J. Cell 103:769-779(2000) [PubMed: 11114333] [Abstract] Cited for: CHARACTERIZATION.
[13]	"DsbD-catalyzed transport of electrons across the membrane of Escherichia coli." Krupp R., Chan C., Missiakas D. J. Biol. Chem. 276:3696-3701(2001) [PubMed: 11085993] [Abstract] Cited for: CHARACTERIZATION. Strain: K38.
[14]	"Global topology analysis of the Escherichia coli inner membrane proteome." Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G. Science 308:1321-1323(2005) [PubMed: 15919996] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS]. Strain: K12 / MG1655 / ATCC 47076.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z36905 Genomic DNA. Translation: CAA85375.1. Different initiation.
X77707 Genomic DNA. Translation: CAA54781.1. Different initiation.
U14003 Genomic DNA. Translation: AAA97035.1.
U00096 Genomic DNA. Translation: AAC77096.1.
AP009048 Genomic DNA. Translation: BAE78138.1.

PIR

S56364.

RefSeq

AP_004637.1.
NP_418559.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JPE	X-ray	1.90	A	20-151	[»]
1JZD	X-ray	2.30	C	20-151	[»]
1L6P	X-ray	1.65	A	20-144	[»]
1VRS	X-ray	2.85	A/B/C	20-162	[»]
			D/E/F	438-565	[»]
1Z5Y	X-ray	1.94	D	20-162	[»]
2FWE	X-ray	1.65	A	438-565	[»]
2FWF	X-ray	1.30	A	438-565	[»]
2FWG	X-ray	1.10	A	438-565	[»]
2FWH	X-ray	0.99	A	438-565	[»]

SMR

P36655. Positions 144-169.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9476N.

STRING

P36655.

Protein family/group databases

TCDB

5.A.1.1.1. disulfide bond oxidoreductase D (DsbD) family.

Genome annotation databases

GeneID

948649.

GenomeReviews

Gene locus JW5734 in contig AP009048_GR.
Gene locus b4136 in contig U00096_GR.

KEGG

ecj:JW5734.
eco:b4136.

Organism-specific databases

EchoBASE

EB2095.

EcoGene

EG12178. dipZ.

CMR

Search...

Phylogenomic databases

eggNOG

COG4232.

HOGENOM

HBG640883.

OMA

THILWAG.

Enzyme and pathway databases

BioCyc

EcoCyc:DSBD-MONOMER.
ECOL168927:B4136-MONOMER.

Gene expression databases

Genevestigator

P36655.

Family and domain databases

HAMAP

MF_00399. DbsD.
[Tree]

InterPro

IPR003834. Cyt_c_assmbl_TM_dom.
IPR017936. Thioredoxin-like.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
IPR012335. Thioredoxin_fold.
[Graphical view]

Gene3D

G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

Pfam

PF02683. DsbD. 1 hit.
PF00085. Thioredoxin. 1 hit.
[Graphical view]

PROSITE

PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

DSBD_ECOLI

Accession

Primary (citable) accession number: P36655
Secondary accession number(s): P76796, Q2M6G8

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 2001
Last modified:	January 19, 2010
This is version 113 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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