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.
SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein (By similarity).
SIMILARITY: Belongs to the thioredoxin family. DsbD subfamily.
SIMILARITY: Contains 1 thioredoxin domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

CP000668; ABP41978.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001164951.1; -.

3D structure databases

ModBase

A4TRR6.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from HAMAP).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from HAMAP).
GO:0047134;	Molecular function: protein-disulfide reductase activity (inferred from electronic annotation from HAMAP).
GO:0045454;	Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0017004;	Biological process: cytochrome complex assembly (inferred from electronic annotation from HAMAP).
GO:0022900;	Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0006810;	Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_00399; -; 1.
PBIL [Tree]

InterPro

IPR003834; Cyt_c_assmbl_TM.
IPR006662; Thioredoxin-like.
IPR013766; Thioredoxin_dom.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.30.10; Thioredoxin_fold; 1.

Pfam

PF02683; DsbD; 1.
PF00085; Thioredoxin; 1.
Pfam graphical view of domain structure.

PRINTS

PR00421; THIOREDOXIN.

PROSITE

PS00194; THIOREDOXIN_1; 1.
PS51352; THIOREDOXIN_2; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

5062962; -.

GenomeReviews

CP000668_GR; YPDSF_3628.

KEGG

ypp:YPDSF_3628; -.

CMR

A4TRR6; YPDSF_3628.

Other

ProtoNet

A4TRR6.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cell inner membrane; Cell membrane; Complete proteome; Cytochrome c-type biogenesis; Electron transport; Membrane; NAD; Oxidoreductase; Redox-active center; Signal; Transmembrane; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 24`	`24`	`Potential.`
`CHAIN`	`25 595`	`571`	`Thiol:disulfide interchange protein dsbD.`	`PRO_5000237106`
`TRANSMEM`	`197 217`	`21`	`Potential.`
`TRANSMEM`	`233 253`	`21`	`Potential.`
`TRANSMEM`	`270 290`	`21`	`Potential.`
`TRANSMEM`	`311 331`	`21`	`Potential.`
`TRANSMEM`	`332 352`	`21`	`Potential.`
`TRANSMEM`	`353 373`	`21`	`Potential.`
`TRANSMEM`	`384 404`	`21`	`Potential.`
`TRANSMEM`	`411 431`	`21`	`Potential.`
`TRANSMEM`	`435 455`	`21`	`Potential.`
`DOMAIN`	`452 592`	`141`	`Thioredoxin.`
`DISULFID`	`134 140`		`Redox-active (By similarity).`
`DISULFID`	`209 331`		`Redox-active (By similarity).`
`DISULFID`	`507 510`		`Redox-active (By similarity).`

Sequence information

Length: 595 AA [This is the length of the unprocessed precursor]

Molecular weight: 64506 Da [This is the MW of the unprocessed precursor]

CRC64: D91ABB96DD6686C5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAQRFITLIL LLCSVLLAPH SAQSSLFGEN ASFGTKNSQS RFIPVDQAFA FDFHQQGDQL 

        70         80         90        100        110        120 
NLSWQIHPGY YLYRQQIKIV PQQAALGAFT LPEGITHHDE FYGEVEIFKQ QLTLKIPITQ 

       130        140        150        160        170        180 
AAEQASVSVT YQGCAEAGFC YPPETRVIPL DVVVAASTAS GTAAVNSSAT VNPPATTQPE 

       190        200        210        220        230        240 
GDATPVPSTL PFSPLWALLI GIGIAFTPCV LPMYPLISAV ILGREKPHSQ RRILILAVVY 

       250        260        270        280        290        300 
VQGMALTYTL LGLVVAAAGL QFQAALQHPY VLIGLSVLFV LLALSMFGLY SLQLPSSLQT 

       310        320        330        340        350        360 
RLTQWSNSQR GGSLAGVFAM GALAGLICSP CTTAPLSAIL LYIAQSGNML AGGGTLYLYA 

       370        380        390        400        410        420 
LGMGIPLVVV TLFGNKLIPR SGPWMQYVKE AFGFVILALP VFLLERVLGD VWGLRLWSLL 

       430        440        450        460        470        480 
AVAFFGWAFV LSLKAHAGWV RVCQLLLLAA LLIVARPLQD WAFNGNTQQN AVKHINFQPV 

       490        500        510        520        530        540 
ANLPQLQAVL AQAQGKPVML DLYADWCVAC KEFEKYTFSD DKVQRQLANT LLLQADVTAN 

       550        560        570        580        590 
NAEHATLLKK FNVLGLPTIL FFDSQGNEIT AARVTGFMDA AQFLQHLQNT PAVTK

A4TRR6 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools