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Reviewed, UniProtKB/Swiss-Prot P58162 (DSBD_ECO57)

Last modified June 16, 2009. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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: Z5741, ECs5117
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length565 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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 By similarity.

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.

Sequence similarities

Belongs to the thioredoxin family. DsbD subfamily.

Contains 1 thioredoxin domain.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 By similarity
Chain20 – 565546Thiol:disulfide interchange protein dsbD HAMAP MF_00399
PRO_0000007374

Regions

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

Amino acid modifications

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

Secondary structure

1 ..................... 565
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P58162-1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 249C27E5A2BB2930

FASTA56561,839
        10         20         30         40         50         60 
MAQRIFTLIL LLCSTSVFAG LFDAPGRSQF VPVDQAFAFD FQQNQHDLNL TWQIKDGYYL 

        70         80         90        100        110        120 
YRKQIRITPE HAKIADVQLP QGVWHEDEFY GKSEIYRDRL TLPVTINQAS AGATLTVTYQ 

       130        140        150        160        170        180 
GCADAGFCYP PETKTVPLSE VVANNAASQP VSVPQQEQPT AQLPFSALWA LLIGIGIAFT 

       190        200        210        220        230        240 
PCVLPMYPLI SGIVLGGKQR LSTARALLLT FIYVQGMALT YTALGLVVAA AGLQFQAALQ 

       250        260        270        280        290        300 
HPYVLIGLTI VFTLLAMSMF GLLTLQLPSS LQTRLTLMSN RQQGGSPGGV FIMGTIAGLI 

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

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

       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

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Cross-references

Sequence databases

AE005174 Genomic DNA. Translation: AAG59335.1.
BA000007 Genomic DNA. Translation: BAB38540.1.
PIRC86109.
E91268.
RefSeqNP_290769.1.
NP_313144.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1UC7X-ray1.90A/B441-565[»]
SMRP58162. Positions 23-143.
ModBaseSearch...

Genome annotation databases

GeneID914141.
959987.
GenomeReviewsGene locus Z5741 in contig AE005174_GR.
Gene locus ECs5117 in contig BA000007_GR.
KEGGece:Z5741.
ecs:ECs5117.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP58162.
OMAP58162. TITHILW.

Enzyme and pathway databases

BioCycECOL83334:ECS5117-MON.

Family and domain databases

HAMAPMF_00399.
[Tree]
InterProIPR003834. Cyt_c_assmbl_TM.
IPR017936. Thioredoxin-like.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PfamPF02683. DsbD. 1 hit.
PF00085. Thioredoxin. 1 hit.
[Graphical view]
PROSITEPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameDSBD_ECO57
AccessionPrimary (citable) accession number: P58162
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: June 1, 2001
Last modified: June 16, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents