Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q1C0X4 (DSBD_YERPA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:YPA_3937
OrganismYersinia pestis bv. Antiqua (strain Antiqua) [Complete proteome] [HAMAP]
Taxonomic identifier360102 [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-Rule MF_00399

Catalytic activity

Protein dithiol + NAD(P)+ = protein disulfide + NAD(P)H. HAMAP-Rule MF_00399

Subcellular location

Cell inner membrane; Multi-pass membrane protein By similarity HAMAP-Rule 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-Rule MF_00399
PRO_5000116349

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
Q1C0X4 [UniParc].

Last modified July 11, 2006. 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 genome sequence of Yersinia pestis strains Antiqua and Nepal516: evidence of gene reduction in an emerging pathogen."
Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M., Worsham P., Chu M.C., Andersen G.L.
J. Bacteriol. 188:4453-4463(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Antiqua.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000308 Genomic DNA. Translation: ABG15898.1.
RefSeqYP_653843.1. NC_008150.1.

3D structure databases

ProteinModelPortalQ1C0X4.
SMRQ1C0X4. Positions 41-155, 474-589.
ModBaseSearch...

Protein-protein interaction databases

STRING360102.YPA_3937.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG15898; ABG15898; YPA_3937.
GeneID4119501.
KEGGypa:YPA_3937.
PATRIC18587971. VBIYerPes1796_4760.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4232.
HOGENOMHOG000254981.
KOK04084.
OMAKPHTDEY.
ProtClustDBPRK00293.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
HAMAPMF_00399. DbsD.
InterProIPR003834. Cyt_c_assmbl_TM_dom.
IPR022910. Thiol_diS_interchange_DbsD.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
[Graphical view]
PANTHERPTHR32234:SF1. PTHR32234:SF1. 1 hit.
PfamPF02683. DsbD. 1 hit.
PF13098. Thioredoxin_2. 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_YERPA
AccessionPrimary (citable) accession number: Q1C0X4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: July 11, 2006
Last modified: May 1, 2013
This is version 62 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents