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Q9PHR3 (DSBD_CAMJE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 81. 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:Cj0603c
OrganismCampylobacter jejuni
Taxonomic identifier197 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

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. 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 – 1616 Potential
Chain17 – 567551Thiol:disulfide interchange protein DsbD HAMAP MF_00399
PRO_0000007372

Regions

Topological domain17 – 166150Periplasmic Potential
Transmembrane167 – 18721Helical; Potential
Topological domain188 – 21124Cytoplasmic Potential
Transmembrane212 – 23221Helical; Potential
Topological domain233 – 24715Periplasmic Potential
Transmembrane248 – 26821Helical; Potential
Topological domain269 – 28921Cytoplasmic Potential
Transmembrane290 – 31021Helical; Potential
Topological domain311 – 33222Periplasmic Potential
Transmembrane333 – 35321Helical; Potential
Topological domain354 – 3618Cytoplasmic Potential
Transmembrane362 – 38221Helical; Potential
Topological domain383 – 3853Periplasmic Potential
Transmembrane386 – 40621Helical; Potential
Topological domain407 – 41711Cytoplasmic Potential
Transmembrane418 – 43821Helical; Potential
Topological domain439 – 567129Periplasmic Potential
Domain430 – 567138Thioredoxin

Amino acid modifications

Disulfide bond111 ↔ 117Redox-active By similarity
Disulfide bond186 ↔ 307Redox-active By similarity
Disulfide bond488 ↔ 491Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9PHR3 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: CBEE897144D24852

FASTA56763,786
        10         20         30         40         50         60 
MRIFGIILLS FCLCFASILS LNEAFNVKSN SYNNSISIDI ELGKDIYLYS NKLKLYINEK 

        70         80         90        100        110        120 
DISSLINLPQ SSTRGNENVY YQKLNLALPN LLLERFAKNT TNLIKLEFQG CSEQGLCYNP 

       130        140        150        160        170        180 
QTWYFDLISK KDAFEISKPY KAQKTDKKTK IESEESSIAN FLATDNFFWI LLSFFGYGLL 

       190        200        210        220        230        240 
LSLTPCILPM IPILSSLIVA KSNAKFSKKY SFFLSFIYVF FMSLAYAIAG VIASFLGASI 

       250        260        270        280        290        300 
QGILQKPIIL ILFALIFIAF AFAMFGAFRF ELPLRFQTFI HKKSEKGKGV VGIAIMGFLS 

       310        320        330        340        350        360 
ALIVGPCVAA PLAGALIYIA NTGNALLGGS ALFIMSFGMG IPLLFIGLGL GFIKPGFWME 

       370        380        390        400        410        420 
KVKIFFGFVM LAMAIWILSR IIEENYILIA YGILGVFFSV FMGIFEKSFT IISKIKKSIL 

       430        440        450        460        470        480 
ILILAYSLSI FLGGLFGAKN FLNPLNFNTI SASKHALSYD YINNFEQLKQ EIQTNTKPIM 

       490        500        510        520        530        540 
LDFTASWCEN CKLLDELTFS DERIIQKMQN YKLIKVDVSE NNNEQIKTMK EFNVFGPPVL 

       550        560 
IFFENGKEKL KITGFISADD LLKKIEP 

« Hide

References

[1]"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences."
Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. expand/collapse author list , van Vliet A.H.M., Whitehead S., Barrell B.G.
Nature 403:665-668(2000) [PubMed: 10688204] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 11168 / Serotype O:2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL111168 Genomic DNA. Translation: CAL34749.1.
PIRB81408.
RefSeqYP_002344033.1. NC_002163.1.

3D structure databases

ProteinModelPortalQ9PHR3.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9PHR3. 3 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID904931.
GenomeReviewsGene locus Cj0603c in contig AL111168_GR.
KEGGcje:Cj0603c.
PATRIC20058150. VBICamJej33762_0595.

Phylogenomic databases

HOGENOMHBG640883.
OMARNGHEIG.
PhylomeDBQ9PHR3.
ProtClustDBCLSK878853.

Enzyme and pathway databases

BioCycCJEJ192222:CJ0603C-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.
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. False negative.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDSBD_CAMJE
AccessionPrimary (citable) accession number: Q9PHR3
Secondary accession number(s): Q0PAR4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 81 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