Reviewed, UniProtKB/Swiss-Prot Q15ZS2 (DSBD_PSEA6)

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:	Patl_0084

Organism

Pseudoalteromonas atlantica (strain T6c / BAA-1087) [Complete proteome] [HAMAP]

Taxonomic identifier

342610 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Pseudoalteromonadaceae › Pseudoalteromonas

Protein attributes

Sequence length	592 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 – 592	573	Thiol:disulfide interchange protein dsbD HAMAP MF_00399		PRO_0000304392
Regions
	Transmembrane	186 – 206	21	Potential
	Transmembrane	229 – 249	21	Potential
	Transmembrane	265 – 285	21	Potential
	Transmembrane	318 – 338	21	Potential
	Transmembrane	345 – 365	21	Potential
	Transmembrane	379 – 399	21	Potential
	Transmembrane	406 – 426	21	Potential
	Transmembrane	440 – 460	21	Potential
	Domain	443 – 592	150	Thioredoxin
Amino acid modifications
	Disulfide bond	130 ↔ 136		Redox-active By similarity
	Disulfide bond	204 ↔ 326		Redox-active By similarity
	Disulfide bond	508 ↔ 511		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q15ZS2-1 [UniParc]. Last modified July 25, 2006. Version 1. Checksum: 02B96FA996BA1AB3	FASTA	592	64,665
	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

References

[1]

"Complete sequence of Pseudoalteromonas atlantica T6c." 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. , 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].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000388 Genomic DNA. Translation: ABG38616.1.
RefSeq	YP_659670.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4171785.
GenomeReviews	Gene locus Patl_0084 in contig CP000388_GR.
KEGG	pat:Patl_0084.
NMPDR	fig|342610.3.peg.394.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q15ZS2.
OMA	Q15ZS2. TITHILW.
Enzyme and pathway databases
BioCyc	PATL342610:PATL_0084-MON.
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_PSEA6

Accession

Primary (citable) accession number: Q15ZS2

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	July 25, 2006
Last modified:	June 16, 2009
This is version 29 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)