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P36655

- DSBD_ECOLI

UniProt

P36655 - DSBD_ECOLI

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Protein

Thiol:disulfide interchange protein DsbD

Gene

dsbD

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.

Catalytic activityi

Protein dithiol + NAD(P)+ = protein disulfide + NAD(P)H.

GO - Molecular functioni

  1. electron carrier activity Source: UniProtKB-HAMAP
  2. oxidoreductase activity Source: EcoliWiki
  3. protein disulfide oxidoreductase activity Source: EcoCyc
  4. protein-disulfide reductase activity Source: UniProtKB-HAMAP
  5. transmembrane electron transfer carrier Source: EcoCyc

GO - Biological processi

  1. cell redox homeostasis Source: EcoCyc
  2. cellular response to temperature stimulus Source: EcoliWiki
  3. cytochrome complex assembly Source: EcoliWiki
  4. oxidation-reduction process Source: EcoCyc
  5. response to drug Source: EcoliWiki
  6. transmembrane transport Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Cytochrome c-type biogenesis, Electron transport, Transport

Keywords - Ligandi

NAD

Enzyme and pathway databases

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

Protein family/group databases

TCDBi5.A.1.1.1. the disulfide bond oxidoreductase d (dsbd) family.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:dsbD
Synonyms:cutA2, cycZ, dipZ
Ordered Locus Names:b4136, JW5734
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG12178. dipZ.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasmic side of plasma membrane Source: EcoCyc
  2. integral component of plasma membrane Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi13 – 131C → A: No loss of activity. 1 Publication
Mutagenesisi122 – 1221C → A: Loss of activity. 3 Publications
Mutagenesisi128 – 1281C → A: Loss of activity. 3 Publications
Mutagenesisi182 – 1821C → A: Loss of activity. 3 Publications
Mutagenesisi301 – 3011C → A: No loss of activity. 3 Publications
Mutagenesisi304 – 3041C → A: Loss of activity. 3 Publications
Mutagenesisi480 – 4801C → A: Loss of activity; when associated with A-483. 3 Publications
Mutagenesisi483 – 4831C → A: Loss of activity; when associated with A-480. 3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Chaini20 – 565546Thiol:disulfide interchange protein DsbDPRO_0000007373Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi122 ↔ 128Redox-activeCurated
Disulfide bondi182 ↔ 304Redox-activeCurated
Disulfide bondi480 ↔ 483Redox-activeCurated

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP36655.

Expressioni

Gene expression databases

GenevestigatoriP36655.

Interactioni

Protein-protein interaction databases

DIPiDIP-9476N.
STRINGi511145.b4136.

Structurei

Secondary structure

1
565
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi25 – 284
Helixi33 – 364
Beta strandi37 – 448
Beta strandi47 – 548
Beta strandi58 – 614
Helixi62 – 643
Beta strandi66 – 749
Beta strandi83 – 875
Turni88 – 903
Beta strandi91 – 966
Beta strandi98 – 11922
Beta strandi121 – 1233
Turni124 – 1263
Beta strandi132 – 1376
Helixi456 – 46611
Beta strandi471 – 4766
Helixi481 – 4899
Turni490 – 4923
Helixi494 – 4996
Turni500 – 5023
Beta strandi503 – 5097
Helixi515 – 5239
Beta strandi528 – 5358
Helixi543 – 5453
Beta strandi547 – 5493
Helixi553 – 56210

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP36655.
SMRiP36655. Positions 23-143, 447-563.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36655.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini20 – 162143PeriplasmicSequence AnalysisAdd
BLAST
Topological domaini184 – 20724CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini229 – 24214PeriplasmicSequence AnalysisAdd
BLAST
Topological domaini264 – 29532CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini317 – 3226PeriplasmicSequence Analysis
Topological domaini344 – 35613CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini378 – 3836PeriplasmicSequence Analysis
Topological domaini405 – 41713CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini439 – 565127PeriplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei163 – 18321HelicalSequence AnalysisAdd
BLAST
Transmembranei208 – 22821HelicalSequence AnalysisAdd
BLAST
Transmembranei243 – 26321HelicalSequence AnalysisAdd
BLAST
Transmembranei296 – 31621HelicalSequence AnalysisAdd
BLAST
Transmembranei323 – 34321HelicalSequence AnalysisAdd
BLAST
Transmembranei357 – 37721HelicalSequence AnalysisAdd
BLAST
Transmembranei384 – 40421HelicalSequence AnalysisAdd
BLAST
Transmembranei418 – 43821HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini434 – 565132ThioredoxinAdd
BLAST

Sequence similaritiesi

Belongs to the thioredoxin family. DsbD subfamily.Curated
Contains 1 thioredoxin domain.Curated

Keywords - Domaini

Redox-active center, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG4232.
HOGENOMiHOG000254981.
InParanoidiP36655.
KOiK04084.
OMAiTHILWAG.
OrthoDBiEOG69D3B9.
PhylomeDBiP36655.

Family and domain databases

Gene3Di2.60.40.1250. 1 hit.
3.40.30.10. 1 hit.
HAMAPiMF_00399. DbsD.
InterProiIPR003834. Cyt_c_assmbl_TM_dom.
IPR028250. DsbDN.
IPR022910. Thiol_diS_interchange_DbsD.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
[Graphical view]
PANTHERiPTHR32234. PTHR32234. 1 hit.
PfamiPF11412. DsbC. 1 hit.
PF02683. DsbD. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
SSF74863. SSF74863. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P36655 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAQRIFTLIL LLCSTSVFAG LFDAPGRSQF VPADQAFAFD FQQNQHDLNL
60 70 80 90 100
TWQIKDGYYL YRKQIRITPE HAKIADVQLP QGVWHEDEFY GKSEIYRDRL
110 120 130 140 150
TLPVTINQAS AGATLTVTYQ GCADAGFCYP PETKTVPLSE VVANNAAPQP
160 170 180 190 200
VSVPQQEQPT AQLPFSALWA LLIGIGIAFT PCVLPMYPLI SGIVLGGKQR
210 220 230 240 250
LSTARALLLT FIYVQGMALT YTALGLVVAA AGLQFQAALQ HPYVLIGLAI
260 270 280 290 300
VFTLLAMSMF GLFTLQLPSS LQTRLTLMSN RQQGGSPGGV FVMGAIAGLI
310 320 330 340 350
CSPCTTAPLS AILLYIAQSG NMWLGGGTLY LYALGMGLPL MLITVFGNRL
360 370 380 390 400
LPKSGPWMEQ VKTAFGFVIL ALPVFLLERV IGDVWGLRLW SALGVAFFGW
410 420 430 440 450
AFITSLQAKR GWMRIVQIIL LAAALVSVRP LQDWAFGATH TAQTQTHLNF
460 470 480 490 500
TQIKTVDELN QALVEAKGKP VMLDLYADWC VACKEFEKYT FSDPQVQKAL
510 520 530 540 550
ADTVLLQANV TANDAQDVAL LKHLNVLGLP TILFFDGQGQ EHPQARVTGF
560
MDAETFSAHL RDRQP
Length:565
Mass (Da):61,795
Last modified:June 1, 2001 - v4
Checksum:i41EFAA1C9EAC6C5F
GO

Sequence cautioni

The sequence CAA54781.1 differs from that shown. Reason: Erroneous initiation.
The sequence CAA85375.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiS56364.
RefSeqiNP_418559.1. NC_000913.3.
YP_492279.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC77096; AAC77096; b4136.
BAE78138; BAE78138; BAE78138.
GeneIDi12933697.
948649.
KEGGiecj:Y75_p4023.
eco:b4136.
PATRICi32123839. VBIEscCol129921_4267.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi S56364.
RefSeqi NP_418559.1. NC_000913.3.
YP_492279.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
3PFU X-ray 1.80 A 21-151 [» ]
4IP1 X-ray 2.47 A 444-565 [» ]
4IP6 X-ray 2.23 A 444-565 [» ]
ProteinModelPortali P36655.
SMRi P36655. Positions 23-143, 447-563.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-9476N.
STRINGi 511145.b4136.

Protein family/group databases

TCDBi 5.A.1.1.1. the disulfide bond oxidoreductase d (dsbd) family.

Proteomic databases

PRIDEi P36655.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC77096 ; AAC77096 ; b4136 .
BAE78138 ; BAE78138 ; BAE78138 .
GeneIDi 12933697.
948649.
KEGGi ecj:Y75_p4023.
eco:b4136.
PATRICi 32123839. VBIEscCol129921_4267.

Organism-specific databases

EchoBASEi EB2095.
EcoGenei EG12178. dipZ.

Phylogenomic databases

eggNOGi COG4232.
HOGENOMi HOG000254981.
InParanoidi P36655.
KOi K04084.
OMAi THILWAG.
OrthoDBi EOG69D3B9.
PhylomeDBi P36655.

Enzyme and pathway databases

BioCyci EcoCyc:DSBD-MONOMER.
ECOL316407:JW5734-MONOMER.
MetaCyc:DSBD-MONOMER.

Miscellaneous databases

EvolutionaryTracei P36655.
PROi P36655.

Gene expression databases

Genevestigatori P36655.

Family and domain databases

Gene3Di 2.60.40.1250. 1 hit.
3.40.30.10. 1 hit.
HAMAPi MF_00399. DbsD.
InterProi IPR003834. Cyt_c_assmbl_TM_dom.
IPR028250. DsbDN.
IPR022910. Thiol_diS_interchange_DbsD.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
[Graphical view ]
PANTHERi PTHR32234. PTHR32234. 1 hit.
Pfami PF11412. DsbC. 1 hit.
PF02683. DsbD. 1 hit.
[Graphical view ]
SUPFAMi SSF52833. SSF52833. 1 hit.
SSF74863. SSF74863. 1 hit.
PROSITEi PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiDSBD_ECOLI
AccessioniPrimary (citable) accession number: P36655
Secondary accession number(s): P76796, Q2M6G8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 2001
Last modified: October 29, 2014
This is version 157 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

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

External Data

Dasty 3