Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot A7MMC7 (DSBD_ENTS8)

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: ESA_00148
OrganismEnterobacter sakazakii (strain ATCC BAA-894) [Complete proteome] [HAMAP]
Taxonomic identifier290339 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCronobacter

Protein attributes

Sequence length574 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 – 574555Thiol:disulfide interchange protein dsbD HAMAP MF_00399
PRO_1000049608

Regions

Transmembrane173 – 19321 Potential
Transmembrane218 – 23821 Potential
Transmembrane253 – 27321 Potential
Transmembrane306 – 32621 Potential
Transmembrane333 – 35321 Potential
Transmembrane367 – 38721 Potential
Transmembrane399 – 41921 Potential
Domain430 – 574145Thioredoxin

Amino acid modifications

Disulfide bond122 ↔ 128Redox-active By similarity
Disulfide bond192 ↔ 314Redox-active By similarity
Disulfide bond489 ↔ 492Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
A7MMC7-1 [UniParc].

Last modified October 2, 2007. Version 1.
Checksum: 9063912E6842813A

FASTA57461,676
        10         20         30         40         50         60 
MAHRILTLIL LFCSAHASAS LFGQQNASQF VPADQAFAFD FQQQQHQLTL NWQIKPGYYL 

        70         80         90        100        110        120 
YRQQIRVTPA NASVAPPALP TGEPHEDEFF GKSEIYRDAL SVPVTVEQAA PGATLSVTYQ 

       130        140        150        160        170        180 
GCAEAGFCYP PETRTVPLSA VEPTESVKAN AATPSAATGE QTRVNSDSPS ATLPFSAFWA 

       190        200        210        220        230        240 
LLIGIGVAFT PCVLPMYPLI SGIVLGGDKR LSTRRALLLA FIYVQGMALT YTALGLVVAA 

       250        260        270        280        290        300 
AGLQFQAALQ SPWVLVTLSA VFVLLALSMF GLFTLQLPAS LQTRLTLMSN RQRGGSPGGV 

       310        320        330        340        350        360 
FAMGAIAGLI CSPCTTAPLS AILLYIAQSG NLWLGGGTLY LYALGMGLPL ILVTVFGNRL 

       370        380        390        400        410        420 
LPKSGPWMEQ VKTAFGFVIL ALPVFLLERV LGEPWGVRLW SVLGVAFFGW AFVTSLNATR 

       430        440        450        460        470        480 
SWMRAVQIVL LGAAMICARP LQDWVFGAPV AESQAHLAFT RIATVDDLDR ALAQAKGKPV 

       490        500        510        520        530        540 
MLDLYADWCV ACKEFEKYTF SAPEVQRALD GAVLLQADVT ANSAADVALL KRLNVLGLPT 

       550        560        570 
IIFFDAQGNE IPNGRVTGFM DAPAFATHLH NRLR 

« Hide

References

[1]McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., Fulton B., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W., Johnson M., Thiruvilangam P., Wilson R.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000783 Genomic DNA. Translation: ABU75452.1.
RefSeqYP_001436288.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5549371.
GenomeReviewsGene locus ESA_00148 in contig CP000783_GR.
KEGGesa:ESA_00148.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAA7MMC7. HTDEYFG.

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_ENTS8
AccessionPrimary (citable) accession number: A7MMC7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 2, 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