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Q0T9Q5 (DSBD_ECOL5) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Thiol:disulfide interchange protein DsbD
EC=1.8.1.8
Alternative name(s):
Protein-disulfide reductase
Short name=Disulfide reductase
Gene names
Name:dsbD
Ordered Locus Names:ECP_4380
OrganismEscherichia coli O6:K15:H31 (strain 536 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier362663 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length565 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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. This transfer involves a cascade of disulfide bond formation and reduction steps By similarity. 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 By similarity HAMAP MF_00399.

Sequence similarities

Belongs to the thioredoxin family. DsbD subfamily.

Contains 1 thioredoxin domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 565546Thiol:disulfide interchange protein DsbD HAMAP MF_00399
PRO_0000304388

Regions

Transmembrane163 – 18321Helical; Potential
Transmembrane208 – 22821Helical; Potential
Transmembrane243 – 26321Helical; Potential
Transmembrane289 – 30921Helical; Potential
Transmembrane323 – 34321Helical; Potential
Transmembrane357 – 37721Helical; Potential
Transmembrane384 – 40421Helical; Potential
Domain434 – 565132Thioredoxin

Amino acid modifications

Disulfide bond122 ↔ 128Redox-active By similarity
Disulfide bond182 ↔ 304Redox-active By similarity
Disulfide bond480 ↔ 483Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0T9Q5 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: ADA960811AFC4C62

FASTA56561,915
        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 VVANNEASQP 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 FIMGAIAGLI 

       310        320        330        340        350        360 
CSPCTTAPLS AILLYIAQSG NMWLGGGTLY LYALGMGLPL MLITVFGNRL LPKSGPWMEQ 

       370        380        390        400        410        420 
VKTAFGFVIL ALPVFLLERV IGDIWGLRLW SALGVAFFGW AFITSLQAKR GWMRVVQIIL 

       430        440        450        460        470        480 
LAAALVSVRP LQDWAFGETH TAQTQTHLNF TQIKTVDELN QALVEAKGKP VMLDLYADWC 

       490        500        510        520        530        540 
VACKEFEKYT FSDPQVQKAL ADTVLLQANV TANDAQDVAL LKHLNVLGLP TILFFDGQGQ 

       550        560 
EHPQARVTGF MDAETFSAHL RDRQP

« Hide

References

[1]"Role of pathogenicity island-associated integrases in the genome plasticity of uropathogenic Escherichia coli strain 536."
Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.
Mol. Microbiol. 61:584-595(2006) [PubMed: 16879640] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 536 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000247 Genomic DNA. Translation: ABG72324.1.
RefSeqYP_672225.1. NC_008253.1.

3D structure databases

ProteinModelPortalQ0T9Q5.
SMRQ0T9Q5. Positions 23-143, 447-563.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0T9Q5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000048518; EBESCP00000046707; EBESCG00000047568.
GeneID4190449.
GenomeReviewsGene locus ECP_4380 in contig CP000247_GR.
KEGGecp:ECP_4380.
PATRIC18199701. VBIEscCol77757_4430.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4232.
GeneTreeEBGT00050000010835.
HOGENOMHBG640883.
OMATHILWAG.
PhylomeDBQ0T9Q5.
ProtClustDBPRK00293.

Enzyme and pathway databases

BioCycECOL362663:ECP_4380-MONOMER.

Family and domain databases

HAMAPMF_00399. DbsD.
[Tree]
InterProIPR003834. Cyt_c_assmbl_TM_dom.
IPR022910. Thiol_diS_interchange_DbsD.
IPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
KOK04084.
PANTHERPTHR10438. Trx. 1 hit.
PfamPF02683. DsbD. 1 hit.
PF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMSSF52833. Thiordxn-like_fd. 1 hit.
PROSITEPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDSBD_ECOL5
AccessionPrimary (citable) accession number: Q0T9Q5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 5, 2006
Last modified: January 25, 2012
This is version 48 of the entry and version 1 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

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