Reviewed, UniProtKB/Swiss-Prot Q9KJZ3 (DSBD_PSEUK)

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

Organism

Pseudomonas sp. (strain JR1 / K1)

Taxonomic identifier

269087 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	578 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
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 – 18	18	Potential
	Chain	19 – 578	560	Thiol:disulfide interchange protein dsbD HAMAP MF_00399		PRO_0000007383
Regions
	Topological domain	19 – 158	140	Periplasmic Potential
	Transmembrane	159 – 179	21	Potential
	Topological domain	180 – 207	28	Cytoplasmic Potential
	Transmembrane	208 – 228	21	Potential
	Topological domain	229 – 237	9	Periplasmic Potential
	Transmembrane	238 – 258	21	Potential
	Topological domain	259 – 281	23	Cytoplasmic Potential
	Transmembrane	282 – 302	21	Potential
	Topological domain	303 – 321	19	Periplasmic Potential
	Transmembrane	322 – 342	21	Potential
	Topological domain	343 – 351	9	Cytoplasmic Potential
	Transmembrane	352 – 372	21	Potential
	Topological domain	373	1	Periplasmic Potential
	Transmembrane	374 – 394	21	Potential
	Topological domain	395 – 408	14	Cytoplasmic Potential
	Transmembrane	409 – 429	21	Potential
	Topological domain	430 – 578	149	Periplasmic Potential
	Domain	433 – 576	144	Thioredoxin
Amino acid modifications
	Disulfide bond	118 ↔ 124		Redox-active By similarity
	Disulfide bond	179 ↔ 299		Redox-active By similarity
	Disulfide bond	491 ↔ 494		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9KJZ3-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 7473FC17A9BF7284	FASTA	578	62,181
	10 20 30 40 50 60 MRRLFLFFAL LISGVAQAGT NPFETKPDFL PVGKAFVFTS ERLESGETQL YWQIADGYYL 70 80 90 100 110 120 YQKRLKFDGL PAEQHPALPE GETHSDEFFG EQQVYRQGLE LKIAAGATGQ IKVGFQGCAD 130 140 150 160 170 180 AGLCYPPHTQ VVDLGGYLRY RCDRRSTGPS PGQRLQQRAL GWSLLVFFGL GLLLAFTPCS 190 200 210 220 230 240 LPMLPILAGL IVGSGATPKR GFALATSYVV SMALVYAAMG VLAAMLGANL QALLQNPWLL 250 260 270 280 290 300 GSFAAVFVLL ALPMFGFFEL QLPVAVRDRL ENVSRNQRGG SLFGAGVLGA LSGLLVGPCM 310 320 330 340 350 360 TAPLAGALLY IAQSGNALHG GLILFAMGIG IGVPLLLLVT VGNRFLPKPG AWMNLLKGVF 370 380 390 400 410 420 GFLFLATALL MLRPVLDESL WIGLCGGLLL IAAYSAWKQS EGFGRVAHVF GASSLLLGVW 430 440 450 460 470 480 GSLLMIGAAG GSDDLMKPLQ VYSASNSSSA ANPVSHDAFT TIKDPAALQR ELDEAQAQGQ 490 500 510 520 530 540 WVLLDYYADW CVSCKVMEKQ VFGKAHVMEA LSDVRLLRLD VTADNAASRE LLGRYKVPGP 550 560 570 PSLLWIGADG IERRSQRITG EVDAGTFLQR WTTTRDAH

References

[1]

"The two-component signal transduction system ArmRS is involved in deregulation of 3-isopropylcatechol dioxygenase in the mutant strain Pseudomonas sp. K1." Johann A., Michel J., Averhoff B., Gottschalk G. Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF155506 Genomic DNA. Translation: AAF80267.1.
3D structure databases
HSSP	HSSP built from PDB template 1JPE based on UniProtKB P36655.
ModBase	Search...
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_PSEUK

Accession

Primary (citable) accession number: Q9KJZ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	October 1, 2000
Last modified:	June 16, 2009
This is version 54 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)