Reviewed, UniProtKB/Swiss-Prot Q8CVH5 (DSBD_ECOL6)

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:	c5218

Organism

Escherichia coli O6 [Complete proteome] [HAMAP]

Taxonomic identifier

217992 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	565 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 – 19	19	Potential
	Chain	20 – 565	546	Thiol:disulfide interchange protein dsbD HAMAP MF_00399		PRO_0000304387
Regions
	Transmembrane	163 – 183	21	Potential
	Transmembrane	208 – 228	21	Potential
	Transmembrane	243 – 263	21	Potential
	Transmembrane	289 – 309	21	Potential
	Transmembrane	323 – 343	21	Potential
	Transmembrane	357 – 377	21	Potential
	Transmembrane	384 – 404	21	Potential
	Domain	434 – 565	132	Thioredoxin
Amino acid modifications
	Disulfide bond	122 ↔ 128		Redox-active By similarity
	Disulfide bond	182 ↔ 304		Redox-active By similarity
	Disulfide bond	480 ↔ 483		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8CVH5-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 49AFB0911AFA8C7C	FASTA	565	61,889
	10 20 30 40 50 60 MAQRIFTLIL LLCSTSVFAG LFDAPGRSQF VPADQAFAFD FQQNQHDLNL TWQIKDGYYL 70 80 90 100 110 120 YRKQIRITPE HAKIADVQLP QGVWHEDEFY GKSEIYRDRL TLPVTINQAS AGATLTVTYQ 130 140 150 160 170 180 GCADAGFCYP PETKTVPLSE VVANNEASQP VSVPQQEQPT AQLPFSALWA LLIGIGIAFT 190 200 210 220 230 240 PCVLPMYPLI SGIVLGGKQR LSTARALLLT FIYVQGMALT YTALGLVVAA AGLQFQAALQ 250 260 270 280 290 300 HPYVLIGLAI VFTLLAMSMF GLFTLQLPSS LQTRLTLMSN RQQGGSPGGV FIMGAIAGLI 310 320 330 340 350 360 CSPCTTAPLS AILLYIAQSG NMWLGGGTLY LYALGMGLPL MLITVFGNRL LPKSGPWMEQ 370 380 390 400 410 420 VKTAFGFVIL ALPVFLLERV IGDIWGLRLW SALGVAFFGW AFITSLQAKR GWMRVVQIIL 430 440 450 460 470 480 LAAALVSVRP LQDWAFGATH TAQTQTHLNF TQIKTVDELN QALVEAKGKP VMLDLYADWC 490 500 510 520 530 540 VACKEFEKYT FSDPQVQKAL ADTVLLQANV TANDAQDMAL LKHLNVLGLP TILFFDGQGQ 550 560 EHPQARVTGF MDAETFSAHL RDRQP

References

[1]

"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli." Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R. Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE014075 Genomic DNA. Translation: AAN83640.1.
RefSeq	NP_757066.1.
3D structure databases
HSSP	HSSP built from PDB template 1L6P based on UniProtKB P36655.
SMR	Q8CVH5. Positions 23-143, 442-565.
ModBase	Search...
Genome annotation databases
GeneID	1037532.
GenomeReviews	Gene locus c5218 in contig AE014075_GR.
KEGG	ecc:c5218.
NMPDR	fig|199310.1.peg.5109.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8CVH5.
OMA	Q8CVH5. TITHILW.
Enzyme and pathway databases
BRENDA	1.8.1.8. 292881.
Family and domain databases
HAMAP	MF_00399. [Tree]
InterPro	IPR003834. Cyt_c_assmbl_TM. IPR017936. Thioredoxin-like. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
Pfam	PF02683. DsbD. 1 hit. PF00085. Thioredoxin. 1 hit. [Graphical view]
PROSITE	PS00194. THIOREDOXIN_1. 1 hit. PS51352. THIOREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DSBD_ECOL6

Accession

Primary (citable) accession number: Q8CVH5

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	March 1, 2003
Last modified:	June 16, 2009
This is version 53 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)