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Reviewed, UniProtKB/Swiss-Prot A8AMR4 (DSBD_CITK8)

Last modified June 16, 2009. Version 16. 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: CKO_03700
OrganismCitrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696) [Complete proteome] [HAMAP]
Taxonomic identifier290338 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCitrobacter

Protein attributes

Sequence length569 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 – 569550Thiol:disulfide interchange protein dsbD HAMAP MF_00399
PRO_1000049607

Regions

Transmembrane168 – 18821 Potential
Transmembrane213 – 23321 Potential
Transmembrane248 – 26821 Potential
Transmembrane301 – 32121 Potential
Transmembrane328 – 34821 Potential
Transmembrane362 – 38221 Potential
Transmembrane391 – 41121 Potential
Domain430 – 569140Thioredoxin

Amino acid modifications

Disulfide bond122 ↔ 128Redox-active By similarity
Disulfide bond187 ↔ 309Redox-active By similarity
Disulfide bond484 ↔ 487Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
A8AMR4-1 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: A4D4AC331EC56094

FASTA56961,756
        10         20         30         40         50         60 
MAQRILTLIL LLCSTSAFAG LFDAPGRSQF VPADQAFSFD FQQNQHDLNL SWQVKDGYYL 

        70         80         90        100        110        120 
YRKQISITPS QAEIAEVRLP AGVWHEDEFY GKSEIYRKRL NIPLIVNQAA SGATLTVTYQ 

       130        140        150        160        170        180 
GCADAGFCYP PETKTVPLSE VSASTVAKST PSPVAAQTEE TPQPAARLPF SALWALLIGI 

       190        200        210        220        230        240 
GIAFTPCVLP MYPLISGIVL GGKQRLSTGR ALLLTFIYVQ GMALTYTALG LVVAAAGLQF 

       250        260        270        280        290        300 
QAALQHPYVL IGLALVFTLL ALSMFGLFTL QLPSSLQTRL TLMSNRQQGG SPGGVFVMGA 

       310        320        330        340        350        360 
IAGLICSPCT TAPLSAILLY IAQSGNMWLG GGTLYLYALG MGLPLILITV FGNRLLPKSG 

       370        380        390        400        410        420 
PWMEHVKTAF GFVILALPVF LLERVIGDEW GLRLWSLLGV AFFGWAFITS LHARRSGMRI 

       430        440        450        460        470        480 
VQIILLAAAL VSVRPLQDWA FGATTAQTQA HLNFKPITTV DALNQALAEA KGKPIMLDLY 

       490        500        510        520        530        540 
ADWCVACKEF EKYTFSDPQV QQTLGDTVLL QANVTANNAQ DVALLRHLNV LGLPTILFFD 

       550        560 
AQGHEHPNAR VTGFMDATTF SAHLRDRQP 

« Hide

References

[1]McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W., Johnson M., Thiruvilangam P., Wilson R.
Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000822 Genomic DNA. Translation: ABV14777.1.
RefSeqYP_001455213.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5583492.
GenomeReviewsGene locus CKO_03700 in contig CP000822_GR.
KEGGcko:CKO_03700.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAA8AMR4. TITHILW.

Family and domain databases

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

Entry information

Entry nameDSBD_CITK8
AccessionPrimary (citable) accession number: A8AMR4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 23, 2007
Last modified: June 16, 2009
This is version 16 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