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Reviewed, UniProtKB/Swiss-Prot Q5PIQ0 (DSBD_SALPA)

Last modified June 16, 2009. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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

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: SPA4139
OrganismSalmonella paratyphi A [Complete proteome] [HAMAP]
Taxonomic identifier54388 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length567 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.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 567548Thiol:disulfide interchange protein dsbD HAMAP MF_00399
PRO_0000304395

Regions

Transmembrane166 – 18621 Potential
Transmembrane211 – 23121 Potential
Transmembrane246 – 26621 Potential
Transmembrane299 – 31921 Potential
Transmembrane326 – 34621 Potential
Transmembrane360 – 38021 Potential
Transmembrane387 – 40721 Potential
Transmembrane418 – 43821 Potential
Domain435 – 567133Thioredoxin

Amino acid modifications

Disulfide bond122 ↔ 128Redox-active By similarity
Disulfide bond185 ↔ 307Redox-active By similarity
Disulfide bond482 ↔ 485Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5PIQ0-1 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: FF6A6526EB405CBA

FASTA56761,314
        10         20         30         40         50         60 
MAQRIFTLIL LLCSTSAFAG LFDAPGRSQF VPADRAFVFD FQQNQHDLTL SWQVKEGYYL 

        70         80         90        100        110        120 
YRKQISITPT KADIAAVQLP AGVWHEDEFY GKSEIYRKRL NVPVTVNQAA AGATLTVTYQ 

       130        140        150        160        170        180 
GCADAGFCYP PETKTVPLSE VAAAIDATPT PAVTQTGETS KPAAQLPFSA LWALLIGIGI 

       190        200        210        220        230        240 
AFTPCVLPMY PLISGIVLGG RQRLSTGRAL LLAFIYVQGM ALTYTALGLV VAAAGLQFQA 

       250        260        270        280        290        300 
ALQHPYVLIG LAIVFTLLAL SMFGLFTLQL PSSLQTRLTL MSNRQQGGSP GGVFVMGAIA 

       310        320        330        340        350        360 
GLICSPCTTA PLSAILLYIA QSGNMWLGGG TLYLYALGMG LPLMLVTVFG NRLLPKSGPW 

       370        380        390        400        410        420 
MAHVKTAFGF VILALPVFLL ERIIGEAWGL RLWSLLGVAF FGWAFITSLQ ARRAWMRIVQ 

       430        440        450        460        470        480 
IILLAAALIS VRPLQDWAFG SPSAQAPAHL NFTAISTVDE LNQALAQAKG KPVMLDFYAD 

       490        500        510        520        530        540 
WCVACKEFEK YTFSDPRVQQ ALGDTVLLQA NVTANNAQDV ALLKHLQVLG LPTILFFDAQ 

       550        560 
GQEQPQARVT GFMDAATFSA HLHDRQP 

« Hide

References

[1]"Comparison of genome degradation in Paratyphi A and Typhi, human-restricted serovars of Salmonella enterica that cause typhoid."
McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S., Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R., Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F. expand/collapse author list , Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W., Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M., Warren W., Florea L., Spieth J., Wilson R.K.
Nat. Genet. 36:1268-1274(2004) [PubMed: 15531882] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 9150 / SARB42.

Cross-references

Sequence databases

CP000026 Genomic DNA. Translation: AAV79880.1.
RefSeqYP_153192.1.

3D structure databases

SMRQ5PIQ0. Positions 23-143, 449-567.
ModBaseSearch...

Genome annotation databases

GeneID3176146.
GenomeReviewsGene locus SPA4139 in contig CP000026_GR.
KEGGspt:SPA4139.
NMPDRfig|295319.3.peg.3423.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ5PIQ0.
OMAQ5PIQ0. TITHILW.

Enzyme and pathway databases

BioCycSENT295319:SPA4139-MON.

Family and domain databases

HAMAPMF_00399.
[Tree]
InterProIPR003834. Cyt_c_assmbl_TM.
IPR017936. Thioredoxin-like.
IPR015467. Thioredoxin_core.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PANTHERPTHR10438. Trx. 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...

Entry information

Entry nameDSBD_SALPA
AccessionPrimary (citable) accession number: Q5PIQ0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: January 4, 2005
Last modified: June 16, 2009
This is version 41 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)

Relevant documents

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