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Q15ZS2 (DSBD_PSEA6) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 49. 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:Patl_0084
OrganismPseudoalteromonas atlantica (strain T6c / ATCC BAA-1087) [Complete proteome] [HAMAP]
Taxonomic identifier342610 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Pseudoalteromonadaceae › Pseudoalteromonas

Protein attributes

Sequence length592 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 – 1919 Potential
Chain20 – 592573Thiol:disulfide interchange protein DsbD HAMAP MF_00399
PRO_0000304392

Regions

Transmembrane186 – 20621Helical; Potential
Transmembrane229 – 24921Helical; Potential
Transmembrane265 – 28521Helical; Potential
Transmembrane318 – 33821Helical; Potential
Transmembrane345 – 36521Helical; Potential
Transmembrane379 – 39921Helical; Potential
Transmembrane406 – 42621Helical; Potential
Transmembrane440 – 46021Helical; Potential
Domain443 – 592150Thioredoxin

Amino acid modifications

Disulfide bond130 ↔ 136Redox-active By similarity
Disulfide bond204 ↔ 326Redox-active By similarity
Disulfide bond508 ↔ 511Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q15ZS2 [UniParc].

Last modified July 25, 2006. Version 1.
Checksum: 02B96FA996BA1AB3

FASTA59264,665
        10         20         30         40         50         60 
MKLIASFSIF MLMSIWSFAS LGQSNSFDSL FSNEPEFLKV DQAFVFDYVQ NGDQLVVTWD 

        70         80         90        100        110        120 
IADDYYLYQQ QFKAVSKNAS LGEPIFPTGK MKEDEFFDEP QEVYYHKVSV TYPILQSQDD 

       130        140        150        160        170        180 
SAVKIRYQGC AEAGLCYPPT TQVVYLNAVN ASDDLSNTDE ASVESSGSVS QQFELADLLT 

       190        200        210        220        230        240 
GDQSLIWVLL IFLALGVGLA FTPCVFPMYP ILSGIVIGQG KSISTSRAFV LSFVYVQGMA 

       250        260        270        280        290        300 
LTYSLLGLVV ASAGVQFQAA LQHPIILGAL IVVFALLALV MFGAWEFQLP SSWQEKLNGV 

       310        320        330        340        350        360 
SNQQKSGSYL GVLLMGAISG LVASPCTTAP LTGILLYIAQ TSDLLLGFSA LYALSLGMGI 

       370        380        390        400        410        420 
PLILFGITGG KLLPKAGAWM NIIKVTFGFM MLAVALMFVE RLVSHMATDI LWSLLGLVTF 

       430        440        450        460        470        480 
SYFYVMNQAS SVTFGKGVRA LVIFIGLFAS AMYGYQTIFG QTSSVAGHTE QSHPRFEVVK 

       490        500        510        520        530        540 
NLDDFEQKLA AANAQGKTVM VDLYADWCVA CKEFEKYTFP DTQVVDALSN TVWMQIDLTD 

       550        560        570        580        590 
NTATNIAFQE HFSILGLPTI LFFDLQGKEI SGSRVTGFMQ ASAFAAHAKN IL

« Hide

References

[1]"Complete sequence of Pseudoalteromonas atlantica T6c."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Karls A.C., Bartlett D., Higgins B.P., Richardson P.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: T6c / ATCC BAA-1087.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000388 Genomic DNA. Translation: ABG38616.1.
RefSeqYP_659670.1. NC_008228.1.

3D structure databases

ProteinModelPortalQ15ZS2.
SMRQ15ZS2. Positions 470-591.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ15ZS2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4171785.
GenomeReviewsGene locus Patl_0084 in contig CP000388_GR.
KEGGpat:Patl_0084.
NMPDRfig|342610.3.peg.394.
PATRIC23044954. VBIPseAtl25434_0088.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4232.
HOGENOMHBG640883.
OMATHILWAG.
PhylomeDBQ15ZS2.
ProtClustDBPRK00293.

Enzyme and pathway databases

BioCycPATL342610:PATL_0084-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_PSEA6
AccessionPrimary (citable) accession number: Q15ZS2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: July 25, 2006
Last modified: January 25, 2012
This is version 49 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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