Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P36655 (DSBD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thiol:disulfide interchange protein DsbD

EC=1.8.1.8
Alternative name(s):
C-type cytochrome biogenesis protein CycZ
Inner membrane copper tolerance protein
Protein-disulfide reductase
Short name=Disulfide reductase
Gene names
Name:dsbD
Synonyms:cutA2, cycZ, dipZ
Ordered Locus Names:b4136, JW5734
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length565 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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-Rule MF_00399

Catalytic activity

Protein dithiol + NAD(P)+ = protein disulfide + NAD(P)H. HAMAP-Rule MF_00399

Subcellular location

Cell inner membrane; Multi-pass membrane protein HAMAP-Rule 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.

Sequence similarities

Belongs to the thioredoxin family. DsbD subfamily.

Contains 1 thioredoxin domain.

Sequence caution

The sequence CAA54781.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA85375.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.8
Chain20 – 565546Thiol:disulfide interchange protein DsbD HAMAP-Rule MF_00399
PRO_0000007373

Regions

Topological domain20 – 162143Periplasmic Potential
Transmembrane163 – 18321Helical; Potential
Topological domain184 – 20724Cytoplasmic Potential
Transmembrane208 – 22821Helical; Potential
Topological domain229 – 24214Periplasmic Potential
Transmembrane243 – 26321Helical; Potential
Topological domain264 – 29532Cytoplasmic Potential
Transmembrane296 – 31621Helical; Potential
Topological domain317 – 3226Periplasmic Potential
Transmembrane323 – 34321Helical; Potential
Topological domain344 – 35613Cytoplasmic Potential
Transmembrane357 – 37721Helical; Potential
Topological domain378 – 3836Periplasmic Potential
Transmembrane384 – 40421Helical; Potential
Topological domain405 – 41713Cytoplasmic Potential
Transmembrane418 – 43821Helical; Potential
Topological domain439 – 565127Periplasmic Potential
Domain434 – 565132Thioredoxin

Amino acid modifications

Disulfide bond122 ↔ 128Redox-active Probable
Disulfide bond182 ↔ 304Redox-active Probable
Disulfide bond480 ↔ 483Redox-active Probable

Experimental info

Mutagenesis131C → A: No loss of activity. Ref.11
Mutagenesis1221C → A: Loss of activity. Ref.7 Ref.8 Ref.11
Mutagenesis1281C → A: Loss of activity. Ref.7 Ref.8 Ref.11
Mutagenesis1821C → A: Loss of activity. Ref.7 Ref.8 Ref.11
Mutagenesis3011C → A: No loss of activity. Ref.7 Ref.8 Ref.11
Mutagenesis3041C → A: Loss of activity. Ref.7 Ref.8 Ref.11
Mutagenesis4801C → A: Loss of activity; when associated with A-483. Ref.7 Ref.8 Ref.11
Mutagenesis4831C → A: Loss of activity; when associated with A-480. Ref.7 Ref.8 Ref.11

Secondary structure

............................................. 565
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P36655 [UniParc].

Last modified June 1, 2001. Version 4.
Checksum: 41EFAA1C9EAC6C5F

FASTA56561,795
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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 277:1453-1462(1997) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.
PIRS56364.
RefSeqNP_418559.1. NC_000913.3.
YP_492279.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JPEX-ray1.90A20-151[»]
1JZDX-ray2.30C20-151[»]
1L6PX-ray1.65A20-144[»]
1VRSX-ray2.85A/B/C20-162[»]
D/E/F438-565[»]
1Z5YX-ray1.94D20-162[»]
2FWEX-ray1.65A438-565[»]
2FWFX-ray1.30A438-565[»]
2FWGX-ray1.10A438-565[»]
2FWHX-ray0.99A438-565[»]
3PFUX-ray1.80A21-151[»]
4IP1X-ray2.47A444-565[»]
4IP6X-ray2.23A444-565[»]
ProteinModelPortalP36655.
SMRP36655. Positions 23-143, 447-563.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9476N.
STRING511145.b4136.

Protein family/group databases

TCDB5.A.1.1.1. the disulfide bond oxidoreductase d (dsbd) family.

Proteomic databases

PRIDEP36655.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC77096; AAC77096; b4136.
BAE78138; BAE78138; BAE78138.
GeneID12933697.
948649.
KEGGecj:Y75_p4023.
eco:b4136.
PATRIC32123839. VBIEscCol129921_4267.

Organism-specific databases

EchoBASEEB2095.
EcoGeneEG12178. dipZ.

Phylogenomic databases

eggNOGCOG4232.
HOGENOMHOG000254981.
KOK04084.
OMAIYLMARI.
OrthoDBEOG69D3B9.
PhylomeDBP36655.
ProtClustDBPRK00293.

Enzyme and pathway databases

BioCycEcoCyc:DSBD-MONOMER.
ECOL316407:JW5734-MONOMER.
MetaCyc:DSBD-MONOMER.

Gene expression databases

GenevestigatorP36655.

Family and domain databases

Gene3D2.60.40.1250. 1 hit.
3.40.30.10. 1 hit.
HAMAPMF_00399. DbsD.
InterProIPR003834. Cyt_c_assmbl_TM_dom.
IPR028250. DsbDN.
IPR022910. Thiol_diS_interchange_DbsD.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
[Graphical view]
PANTHERPTHR32234. PTHR32234. 1 hit.
PfamPF11412. DsbC. 1 hit.
PF02683. DsbD. 1 hit.
[Graphical view]
SUPFAMSSF52833. SSF52833. 1 hit.
SSF74863. SSF74863. 1 hit.
PROSITEPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP36655.
PROP36655.

Entry information

Entry nameDSBD_ECOLI
AccessionPrimary (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: April 16, 2014
This is version 154 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

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