Reviewed, UniProtKB/Swiss-Prot Q66FE1 (DSBD_YERPS)

Names and origin

Protein names

Recommended 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:	YPTB0399

Organism

Yersinia pseudotuberculosis [Complete proteome] [HAMAP]

Taxonomic identifier

633 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Yersinia

Protein attributes

Sequence length	595 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred 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.

Ontologies

Keywords
Biological process	Cytochrome c-type biogenesis Electron transport Transport
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Redox-active center Signal Transmembrane
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro cytochrome complex assembly Inferred from electronic annotation. Source: HAMAP electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	electron carrier activity Inferred from electronic annotation. Source: HAMAP protein-disulfide reductase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24	Potential
	Chain	25 – 595	571	Thiol:disulfide interchange protein dsbD HAMAP MF_00399		PRO_5000098386
Regions
	Transmembrane	197 – 217	21	Potential
	Transmembrane	233 – 253	21	Potential
	Transmembrane	270 – 290	21	Potential
	Transmembrane	311 – 331	21	Potential
	Transmembrane	332 – 352	21	Potential
	Transmembrane	353 – 373	21	Potential
	Transmembrane	384 – 404	21	Potential
	Transmembrane	411 – 431	21	Potential
	Transmembrane	435 – 455	21	Potential
	Domain	452 – 592	141	Thioredoxin
Amino acid modifications
	Disulfide bond	134 ↔ 140		Redox-active By similarity
	Disulfide bond	209 ↔ 331		Redox-active By similarity
	Disulfide bond	507 ↔ 510		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q66FE1-1 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 4DBC4E2277788265	FASTA	595	64,492
	10 20 30 40 50 60 MAQRFITLIL LLCSVLLAPH SAQSSLFGEN TSFGAKNSQS 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 NAEHATLLNK FNVLGLPTIL FFDSQGNEIT AARVTGFMDA AQFLQHLQNT PAVTK

References

[1]

"Insights into the evolution of Yersinia pestis through whole-genome comparison with Yersinia pseudotuberculosis." Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O., Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L., Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C., Simonet M., Chenal-Francisque V., Souza B. , Dacheux D., Elliott J.M., Derbise A., Hauser L.J., Garcia E. Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004) [PubMed: 15358858] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: IP32953 / Serotype I.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX936398 Genomic DNA. Translation: CAH19639.1.
RefSeq	YP_068942.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2955489.
GenomeReviews	Gene locus YPTB0399 in contig BX936398_GR.
KEGG	yps:YPTB0399.
NMPDR	fig|273123.1.peg.526.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q66FE1.
OMA	Q66FE1. DIQMENG.
Enzyme and pathway databases
BioCyc	YPSE273123:YPTB0399-MON.
BRENDA	1.8.1.8. 20871.
Family and domain databases
HAMAP	MF_00399. [Tree]
InterPro	IPR003834. Cyt_c_assmbl_TM. IPR017936. Thioredoxin-like. IPR017937. Thioredoxin_CS. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
Pfam	PF02683. DsbD. 1 hit. [Graphical view]
PROSITE	PS00194. THIOREDOXIN_1. 1 hit. PS51352. THIOREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DSBD_YERPS

Accession

Primary (citable) accession number: Q66FE1

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	October 11, 2004
Last modified:	June 16, 2009
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)