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A3N207 (DSBD_ACTP2) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. 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:APL_1359
OrganismActinobacillus pleuropneumoniae serotype 5b (strain L20) [Complete proteome] [HAMAP]
Taxonomic identifier416269 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Actinobacillus

Protein attributes

Sequence length583 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 – 2020 Potential
Chain21 – 583563Thiol:disulfide interchange protein DsbD HAMAP MF_00399
PRO_0000304382

Regions

Transmembrane185 – 20521Helical; Potential
Transmembrane237 – 25721Helical; Potential
Transmembrane261 – 28121Helical; Potential
Transmembrane302 – 32221Helical; Potential
Transmembrane344 – 36421Helical; Potential
Transmembrane375 – 39521Helical; Potential
Transmembrane405 – 42521Helical; Potential
Transmembrane433 – 45321Helical; Potential
Domain440 – 583144Thioredoxin

Amino acid modifications

Disulfide bond123 ↔ 128Redox-active By similarity
Disulfide bond200 ↔ 322Redox-active By similarity
Disulfide bond500 ↔ 503Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
A3N207 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: 46DC55D0A23EA722

FASTA58364,037
        10         20         30         40         50         60 
MLKRFIFLLV GITLTLSAHA GLFGNDQPKY LSGAEAFAFS ATPKSDKQIE LNWQIADGYY 

        70         80         90        100        110        120 
LYKKEIQVTP QNAEIQPLAF PAAENYHDEF FGEVEIFRNQ LTLPITFSAE QANASLSVHY 

       130        140        150        160        170        180 
QGCTKGFCYP PETVTVSLDG QQAVDSAQNV AKNRENSTAS QPLANAPKAE QDQLAENLAN 

       190        200        210        220        230        240 
NRLSIFWFFL LGIGLAFTPC VLPMLPLLSA IVIGNKQRPN TFKALLLSFA YVQGMALTYT 

       250        260        270        280        290        300 
LLGLVVAAIG LPFQVALQSP PVLISLAILF TILAASMFGL FEIRLPNSWQ QKLNAMSQKQ 

       310        320        330        340        350        360 
QGGAFGSVFV MGMIAGLVAS PCTSAPLSGA LLYVAQSGDL LTGGLALYLL ALGMGIPLIL 

       370        380        390        400        410        420 
ITLFGNRILP KSGDWLLKVK TAFGFVMLAL PVFLLSRILP SHYEPLMWSA LAMVFVGWLI 

       430        440        450        460        470        480 
SVIPTQGVIK QAVRIVLFLT FAVASYPWAN LVWNQGNSSH SAQVSNHLAF ERVQSLAELQ 

       490        500        510        520        530        540 
EKLTASQGKK VMLDLYADWC VACKEFEKYT FTDQAVQQKL AEMVVLQVDM TNNSAQNDEL 

       550        560        570        580 
MKHFNVLGLP TILFFDESGK ELTQSRVTGF LEANQFLNWL NQL

« Hide

References

[1]"The complete genome sequence of Actinobacillus pleuropneumoniae L20 (serotype 5b)."
Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M., Nash J.H.E.
J. Bacteriol. 190:1495-1496(2008) [PubMed: 18065534] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: L20.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000569 Genomic DNA. Translation: ABN74443.1.
RefSeqYP_001054048.1. NC_009053.1.

3D structure databases

ProteinModelPortalA3N207.
SMRA3N207. Positions 467-576.
ModBaseSearch...

Protein-protein interaction databases

STRINGA3N207.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4849875.
GenomeReviewsGene locus APL_1359 in contig CP000569_GR.
KEGGapl:APL_1359.
PATRIC20747685. VBIActPle94089_1416.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4232.
HOGENOMHBG640883.
OMARILPEVW.
PhylomeDBA3N207.
ProtClustDBPRK00293.

Enzyme and pathway databases

BioCycAPLE416269:APL_1359-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_ACTP2
AccessionPrimary (citable) accession number: A3N207
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: April 3, 2007
Last modified: December 14, 2011
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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