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ECOLI:DSBB

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) dsbB (synonyms: roxB, ycgA)
Protein Name(s) Disulfide bond formation protein B

Disulfide oxidoreductase

External Links
UniProt P0A6M2
EMBL L03721
U00096
AP009048
M83655
PIR F64864
RefSeq NP_415703.3
YP_489452.1
PDB 2HI7
2K73
2K74
2LEG
2LTQ
2ZUP
2ZUQ
3E9J
PDBsum 2HI7
2K73
2K74
2LEG
2LTQ
2ZUP
2ZUQ
3E9J
ProteinModelPortal P0A6M2
SMR P0A6M2
IntAct P0A6M2
MINT MINT-6742413
STRING 511145.b1185
BindingDB P0A6M2
TCDB 5.A.2.1.1
EnsemblBacteria AAC74269
BAA36032
GeneID 12932821
946344
KEGG ecj:Y75_p1157
eco:b1185
PATRIC 32117616
EchoBASE EB1366
EcoGene EG11393
eggNOG COG1495
HOGENOM HOG000218135
InParanoid P0A6M2
KO K03611
OMA PSPFVTC
OrthoDB EOG6CCH7H
BioCyc EcoCyc:DSBBPROT-MONOMER
ECOL316407:JW5182-MONOMER
MetaCyc:DSBBPROT-MONOMER
EvolutionaryTrace P0A6M2
PRO PR:P0A6M2
Proteomes UP000000318
UP000000625
Genevestigator P0A6M2
GO GO:0016021
GO:0005886
GO:0009055
GO:0015035
GO:0022900
GO:0009408
Gene3D 1.20.1550.10
HAMAP MF_00286
InterPro IPR003752
IPR022920
IPR023380
Pfam PF02600

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0003756

protein disulfide isomerase activity

PMID:17110337[1]

ECO:0000315

F

Fig 4 shows how dsbB/dsbA complex forms a disulfide bond.

complete
CACAO 9615

enables

GO:0015035

protein disulfide oxidoreductase activity

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11393
PANTHER:PTN002195183

F

Seeded From UniProt

complete

involved_in

GO:0006457

protein folding

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN002195183
UniProtKB:P21482
UniProtKB:P57701

P

Seeded From UniProt

complete

involved_in

GO:0022900

electron transport chain

PMID:12006488[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

PMID:8430071[4]

ECO:0000245

automatically integrated combinatorial evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0015035

protein disulfide oxidoreductase activity

PMID:8430071[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0009408

response to heat

PMID:24580753[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0015035

protein disulfide oxidoreductase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003752

F

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003752

C

Seeded From UniProt

complete

enables

GO:0015035

protein disulfide oxidoreductase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000083131

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:UR000083131

P

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:UR000083131

C

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:UR000083131

F

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

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

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

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-0560
UniProtKB-KW:KW-0249

P

Seeded From UniProt

complete

Notes

References

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

  1. Inaba, K et al. (2006) Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation. Cell 127 789-801 PubMed GONUTS page
  2. 2.0 2.1 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  3. Kadokura, H & Beckwith, J (2002) Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA. EMBO J. 21 2354-63 PubMed GONUTS page
  4. 4.0 4.1 Bardwell, JC et al. (1993) A pathway for disulfide bond formation in vivo. Proc. Natl. Acad. Sci. U.S.A. 90 1038-42 PubMed GONUTS page
  5. Krisko, A et al. (2014) Inferring gene function from evolutionary change in signatures of translation efficiency. Genome Biol. 15 R44 PubMed GONUTS page