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Protein

Thiol:disulfide interchange protein DsbD

Gene

dsbD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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

  • electron carrier activity Source: UniProtKB-HAMAP
  • oxidoreductase activity Source: EcoliWiki
  • protein disulfide oxidoreductase activity Source: EcoCyc
  • protein-disulfide reductase activity Source: UniProtKB-HAMAP
  • transmembrane electron transfer carrier Source: EcoCyc

GO - Biological processi

  • cell redox homeostasis Source: EcoCyc
  • cellular response to temperature stimulus Source: EcoliWiki
  • cytochrome complex assembly Source: EcoliWiki
  • oxidation-reduction process Source: EcoCyc
  • response to drug Source: EcoliWiki
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12178. dipZ.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini20 – 162PeriplasmicSequence analysisAdd BLAST143
Transmembranei163 – 183HelicalSequence analysisAdd BLAST21
Topological domaini184 – 207CytoplasmicSequence analysisAdd BLAST24
Transmembranei208 – 228HelicalSequence analysisAdd BLAST21
Topological domaini229 – 242PeriplasmicSequence analysisAdd BLAST14
Transmembranei243 – 263HelicalSequence analysisAdd BLAST21
Topological domaini264 – 295CytoplasmicSequence analysisAdd BLAST32
Transmembranei296 – 316HelicalSequence analysisAdd BLAST21
Topological domaini317 – 322PeriplasmicSequence analysis6
Transmembranei323 – 343HelicalSequence analysisAdd BLAST21
Topological domaini344 – 356CytoplasmicSequence analysisAdd BLAST13
Transmembranei357 – 377HelicalSequence analysisAdd BLAST21
Topological domaini378 – 383PeriplasmicSequence analysis6
Transmembranei384 – 404HelicalSequence analysisAdd BLAST21
Topological domaini405 – 417CytoplasmicSequence analysisAdd BLAST13
Transmembranei418 – 438HelicalSequence analysisAdd BLAST21
Topological domaini439 – 565PeriplasmicSequence analysisAdd BLAST127

GO - Cellular componenti

  • cytoplasmic side of plasma membrane Source: EcoCyc
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi13C → A: No loss of activity. 1 Publication1
Mutagenesisi122C → A: Loss of activity. 3 Publications1
Mutagenesisi128C → A: Loss of activity. 3 Publications1
Mutagenesisi182C → A: Loss of activity. 3 Publications1
Mutagenesisi301C → A: No loss of activity. 3 Publications1
Mutagenesisi304C → A: Loss of activity. 3 Publications1
Mutagenesisi480C → A: Loss of activity; when associated with A-483. 3 Publications1
Mutagenesisi483C → A: Loss of activity; when associated with A-480. 3 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 191 PublicationAdd BLAST19
ChainiPRO_000000737320 – 565Thiol:disulfide interchange protein DsbDAdd BLAST546

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi122 ↔ 128Redox-activeCurated
Disulfide bondi182 ↔ 304Redox-activeCurated
Disulfide bondi480 ↔ 483Redox-activeCurated

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP36655.
PRIDEiP36655.

Interactioni

Protein-protein interaction databases

BioGridi4262691. 1010 interactors.
DIPiDIP-9476N.
STRINGi511145.b4136.

Structurei

Secondary structure

1565
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi25 – 28Combined sources4
Helixi33 – 36Combined sources4
Beta strandi37 – 44Combined sources8
Beta strandi47 – 54Combined sources8
Beta strandi58 – 61Combined sources4
Helixi62 – 64Combined sources3
Beta strandi66 – 74Combined sources9
Beta strandi83 – 87Combined sources5
Turni88 – 90Combined sources3
Beta strandi91 – 96Combined sources6
Beta strandi98 – 119Combined sources22
Beta strandi121 – 123Combined sources3
Turni124 – 126Combined sources3
Beta strandi132 – 137Combined sources6
Helixi456 – 466Combined sources11
Beta strandi471 – 476Combined sources6
Helixi481 – 489Combined sources9
Turni490 – 492Combined sources3
Helixi494 – 499Combined sources6
Turni500 – 502Combined sources3
Beta strandi503 – 509Combined sources7
Helixi515 – 523Combined sources9
Beta strandi528 – 535Combined sources8
Helixi543 – 545Combined sources3
Beta strandi547 – 549Combined sources3
Helixi553 – 562Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36655.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini434 – 565ThioredoxinAdd BLAST132

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

eggNOGiENOG4105CSG. Bacteria.
COG4232. LUCA.
HOGENOMiHOG000254981.
InParanoidiP36655.
KOiK04084.
OMAiMEKQVFG.
PhylomeDBiP36655.

Family and domain databases

Gene3Di2.60.40.1250. 1 hit.
3.40.30.10. 1 hit.
HAMAPiMF_00399. DbsD. 1 hit.
InterProiIPR003834. Cyt_c_assmbl_TM_dom.
IPR028250. DsbDN.
IPR022910. Thiol_diS_interchange_DbsD.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR32234:SF0. PTHR32234:SF0. 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.

P36655-1 [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 differs from that shown. Reason: Erroneous initiation.Curated
The sequence CAA85375 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_000068922.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77096; AAC77096; b4136.
BAE78138; BAE78138; BAE78138.
GeneIDi948649.
KEGGiecj:JW5734.
eco:b4136.
PATRICi32123839. VBIEscCol129921_4267.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_000068922.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262691. 1010 interactors.
DIPiDIP-9476N.
STRINGi511145.b4136.

Protein family/group databases

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

Proteomic databases

PaxDbiP36655.
PRIDEiP36655.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77096; AAC77096; b4136.
BAE78138; BAE78138; BAE78138.
GeneIDi948649.
KEGGiecj:JW5734.
eco:b4136.
PATRICi32123839. VBIEscCol129921_4267.

Organism-specific databases

EchoBASEiEB2095.
EcoGeneiEG12178. dipZ.

Phylogenomic databases

eggNOGiENOG4105CSG. Bacteria.
COG4232. LUCA.
HOGENOMiHOG000254981.
InParanoidiP36655.
KOiK04084.
OMAiMEKQVFG.
PhylomeDBiP36655.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP36655.
PROiP36655.

Family and domain databases

Gene3Di2.60.40.1250. 1 hit.
3.40.30.10. 1 hit.
HAMAPiMF_00399. DbsD. 1 hit.
InterProiIPR003834. Cyt_c_assmbl_TM_dom.
IPR028250. DsbDN.
IPR022910. Thiol_diS_interchange_DbsD.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR32234:SF0. PTHR32234:SF0. 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]
ProtoNetiSearch...

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: November 2, 2016
This is version 169 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.