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ECOLI:DSBD

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) dsbD (synonyms: cutA2, cycZ, dipZ)
Protein Name(s) Thiol:disulfide interchange protein DsbD

C-type cytochrome biogenesis protein CycZ Inner membrane copper tolerance protein Protein-disulfide reductase Disulfide reductase

External Links
UniProt P36655
EMBL Z36905
X77707
U14003
U00096
AP009048
PIR S56364
RefSeq NP_418559.1
YP_492279.1
PDB 1JPE
1JZD
1L6P
1VRS
1Z5Y
2FWE
2FWF
2FWG
2FWH
3PFU
4IP1
4IP6
PDBsum 1JPE
1JZD
1L6P
1VRS
1Z5Y
2FWE
2FWF
2FWG
2FWH
3PFU
4IP1
4IP6
ProteinModelPortal P36655
SMR P36655
DIP DIP-9476N
STRING 511145.b4136
TCDB 5.A.1.1.1
PRIDE P36655
EnsemblBacteria AAC77096
BAE78138
GeneID 12933697
948649
KEGG ecj:Y75_p4023
eco:b4136
PATRIC 32123839
EchoBASE EB2095
EcoGene EG12178
eggNOG COG4232
HOGENOM HOG000254981
InParanoid P36655
KO K04084
OMA QSAVENM
OrthoDB EOG69D3B9
PhylomeDB P36655
BioCyc EcoCyc:DSBD-MONOMER
ECOL316407:JW5734-MONOMER
MetaCyc:DSBD-MONOMER
EvolutionaryTrace P36655
PRO PR:P36655
Proteomes UP000000318
UP000000625
Genevestigator P36655
GO GO:0009898
GO:0005887
GO:0009055
GO:0016491
GO:0015035
GO:0047134
GO:0022865
GO:0045454
GO:0071502
GO:0017004
GO:0055114
GO:0042493
GO:0055085
Gene3D 2.60.40.1250
3.40.30.10
HAMAP MF_00399
InterPro IPR003834
IPR028250
IPR022910
IPR012336
IPR017937
PANTHER PTHR32234:SF0
Pfam PF11412
PF02683
SUPFAM SSF52833
SSF74863
PROSITE PS00194
PS51352

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

involved_in

GO:0055114

oxidation-reduction process

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG12178
PANTHER:PTN001283383

P

Seeded From UniProt

complete

involved_in

GO:0045454

cell redox homeostasis

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG12178
PANTHER:PTN001283383

P

Seeded From UniProt

complete

involved_in

GO:0017004

cytochrome complex assembly

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG12178
PANTHER:PTN001283383

P

Seeded From UniProt

complete

enables

GO:0015035

protein disulfide oxidoreductase activity

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG12178
PANTHER:PTN001283383

F

Seeded From UniProt

complete

part_of

GO:0005887

integral component of plasma membrane

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG12178
PANTHER:PTN001283383

C

Seeded From UniProt

complete

involved_in

GO:0071502

cellular response to temperature stimulus

PMID:7628442[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0042493

response to drug

PMID:7628442[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0017004

cytochrome complex assembly

PMID:7957865[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

PMID:7628442[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005887

integral component of plasma membrane

PMID:19258316[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

PMID:7628442[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0045454

cell redox homeostasis

PMID:7628442[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

PMID:8917542[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

PMID:7628442[2]

ECO:0000245

automatically integrated combinatorial evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0015035

protein disulfide oxidoreductase activity

PMID:8917542[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0009898

cytoplasmic side of plasma membrane

PMID:10712691[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0022900

electron transport chain

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0009055

P

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003834

C

Seeded From UniProt

complete

involved_in

GO:0017004

cytochrome complex assembly

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003834

P

Seeded From UniProt

complete

involved_in

GO:0045454

cell redox homeostasis

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR013766
InterPro:IPR017937

P

Seeded From UniProt

complete

enables

GO:0047134

protein-disulfide reductase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR022910

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003834
InterPro:IPR022910

P

Seeded From UniProt

complete

enables

GO:0047134

protein-disulfide reductase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.8.1.8

F

Seeded From UniProt

complete

involved_in

GO:0017004

cytochrome complex assembly

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000085087

P

Seeded From UniProt

complete

enables

GO:0009055

electron transfer activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000085087

F

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000085087

C

Seeded From UniProt

complete

enables

GO:0047134

protein-disulfide reductase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000085087

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000085087

P

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

GO_REF:0000037
GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1003
UniProtKB-KW:KW-0997
UniProtKB-SubCell:SL-0037

C

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037
GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0249
UniProtKB-KW:KW-0560

P

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0812

C

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

complete

involved_in

GO:0017004

cytochrome complex assembly

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0201

P

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

edit table

Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ 1.0 1.1 1.2 1.3 1.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  2. ↑ 2.0 2.1 2.2 2.3 2.4 2.5 Missiakas, D et al. (1995) Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli. EMBO J. 14 3415-24 PubMed GONUTS page
  3. ↑ Sambongi, Y & Ferguson, SJ (1994) Specific thiol compounds complement deficiency in c-type cytochrome biogenesis in Escherichia coli carrying a mutation in a membrane-bound disulphide isomerase-like protein. FEBS Lett. 353 235-8 PubMed GONUTS page
  4. ↑ Cho, SH & Beckwith, J (2009) Two snapshots of electron transport across the membrane: insights into the structure and function of DsbD. J. Biol. Chem. 284 11416-24 PubMed GONUTS page
  5. ↑ 5.0 5.1 Rietsch, A et al. (1996) An in vivo pathway for disulfide bond isomerization in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 93 13048-53 PubMed GONUTS page
  6. ↑ Chung, J et al. (2000) Transfer of electrons across the cytoplasmic membrane by DsbD, a membrane protein involved in thiol-disulphide exchange and protein folding in the bacterial periplasm. Mol. Microbiol. 35 1099-109 PubMed GONUTS page
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