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A4TRR6 (DSBD_YERPP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 43. 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:YPDSF_3628
OrganismYersinia pestis (strain Pestoides F) [Complete proteome] [HAMAP]
Taxonomic identifier386656 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Yersinia

Protein attributes

Sequence length595 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 – 2424 Potential
Chain25 – 595571Thiol:disulfide interchange protein DsbD HAMAP MF_00399
PRO_5000237106

Regions

Transmembrane197 – 21721Helical; Potential
Transmembrane233 – 25321Helical; Potential
Transmembrane270 – 29021Helical; Potential
Transmembrane311 – 33121Helical; Potential
Transmembrane332 – 35221Helical; Potential
Transmembrane353 – 37321Helical; Potential
Transmembrane384 – 40421Helical; Potential
Transmembrane411 – 43121Helical; Potential
Transmembrane435 – 45521Helical; Potential
Domain452 – 592141Thioredoxin

Amino acid modifications

Disulfide bond134 ↔ 140Redox-active By similarity
Disulfide bond209 ↔ 331Redox-active By similarity
Disulfide bond507 ↔ 510Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
A4TRR6 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: D91ABB96DD6686C5

FASTA59564,506
        10         20         30         40         50         60 
MAQRFITLIL LLCSVLLAPH SAQSSLFGEN ASFGTKNSQS RFIPVDQAFA FDFHQQGDQL 

        70         80         90        100        110        120 
NLSWQIHPGY YLYRQQIKIV PQQAALGAFT LPEGITHHDE FYGEVEIFKQ QLTLKIPITQ 

       130        140        150        160        170        180 
AAEQASVSVT YQGCAEAGFC YPPETRVIPL DVVVAASTAS GTAAVNSSAT VNPPATTQPE 

       190        200        210        220        230        240 
GDATPVPSTL PFSPLWALLI GIGIAFTPCV LPMYPLISAV ILGREKPHSQ RRILILAVVY 

       250        260        270        280        290        300 
VQGMALTYTL LGLVVAAAGL QFQAALQHPY VLIGLSVLFV LLALSMFGLY SLQLPSSLQT 

       310        320        330        340        350        360 
RLTQWSNSQR GGSLAGVFAM GALAGLICSP CTTAPLSAIL LYIAQSGNML AGGGTLYLYA 

       370        380        390        400        410        420 
LGMGIPLVVV TLFGNKLIPR SGPWMQYVKE AFGFVILALP VFLLERVLGD VWGLRLWSLL 

       430        440        450        460        470        480 
AVAFFGWAFV LSLKAHAGWV RVCQLLLLAA LLIVARPLQD WAFNGNTQQN AVKHINFQPV 

       490        500        510        520        530        540 
ANLPQLQAVL AQAQGKPVML DLYADWCVAC KEFEKYTFSD DKVQRQLANT LLLQADVTAN 

       550        560        570        580        590 
NAEHATLLKK FNVLGLPTIL FFDSQGNEIT AARVTGFMDA AQFLQHLQNT PAVTK

« Hide

References

[1]"Complete sequence of chromosome of Yersinia pestis Pestoides F."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Di Bartolo G., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Worsham P., Chu M., Bearden S., Garcia E., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Pestoides F.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000668 Genomic DNA. Translation: ABP41978.1.
RefSeqYP_001164951.1. NC_009381.1.

3D structure databases

ProteinModelPortalA4TRR6.
SMRA4TRR6. Positions 41-155, 474-589.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4TRR6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5062962.
GenomeReviewsGene locus YPDSF_3628 in contig CP000668_GR.
KEGGypp:YPDSF_3628.
PATRIC18617313. VBIYerPes122972_4513.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4232.
HOGENOMHBG640883.
OMAKPHTDEY.
ProtClustDBPRK00293.

Enzyme and pathway databases

BioCycYPES386656:YPDSF_3628-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_YERPP
AccessionPrimary (citable) accession number: A4TRR6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: May 15, 2007
Last modified: January 25, 2012
This is version 43 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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