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Protein

Thiol:disulfide interchange protein DsbG

Gene

dsbG

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in disulfide bond formation. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins such as ErfK, YbiS and YnhG. Probably also functions as a disulfide isomerase with a narrower substrate specificity than DsbC. DsbG is maintained in a reduced state by DsbD. Displays chaperone activity in both redox states in vitro.1 Publication

GO - Molecular functioni

  • protein disulfide isomerase activity Source: EcoliWiki
  • protein disulfide oxidoreductase activity Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Enzyme and pathway databases

BioCyciEcoCyc:DSBG-MONOMER.
ECOL316407:JW0597-MONOMER.
MetaCyc:DSBG-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Thiol:disulfide interchange protein DsbG
Gene namesi
Name:dsbG
Synonyms:ybdP
Ordered Locus Names:b0604, JW0597
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13535. dsbG.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Disruption phenotypei

No visible phenotype.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi126C → A: Complete loss of redox activity. 1 Publication1
Mutagenesisi126C → S: No loss of chaperone activity; when associated with S-129. 1 Publication1
Mutagenesisi129C → A: Partial loss of redox activity. Traps the protein in complex with ErfK, YbiS and YnhG. 2 Publications1
Mutagenesisi129C → S: No loss of chaperone activity; when associated with S-126. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 171 PublicationAdd BLAST17
ChainiPRO_000003427818 – 248Thiol:disulfide interchange protein DsbGAdd BLAST231

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi126 ↔ 129Redox-active1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP77202.
PRIDEiP77202.

Interactioni

Subunit structurei

Homodimer. Interacts with ErfK, YbiS and YnhG.2 Publications

Protein-protein interaction databases

BioGridi4260900. 172 interactors.
DIPiDIP-9478N.
IntActiP77202. 11 interactors.
MINTiMINT-1232069.
STRINGi511145.b0604.

Structurei

Secondary structure

1248
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi22 – 28Combined sources7
Turni29 – 31Combined sources3
Beta strandi32 – 39Combined sources8
Helixi41 – 43Combined sources3
Beta strandi45 – 51Combined sources7
Beta strandi54 – 60Combined sources7
Beta strandi67 – 70Combined sources4
Helixi80 – 88Combined sources9
Helixi92 – 94Combined sources3
Helixi95 – 102Combined sources8
Beta strandi107 – 110Combined sources4
Beta strandi115 – 122Combined sources8
Helixi127 – 141Combined sources15
Beta strandi144 – 151Combined sources8
Helixi159 – 168Combined sources10
Beta strandi169 – 171Combined sources3
Helixi172 – 181Combined sources10
Turni182 – 184Combined sources3
Helixi196 – 212Combined sources17
Beta strandi219 – 224Combined sources6
Turni225 – 227Combined sources3
Beta strandi228 – 235Combined sources8
Helixi238 – 244Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1V57X-ray2.00A/B18-248[»]
1V58X-ray1.70A/B18-248[»]
2H0GX-ray2.30A/B18-248[»]
2H0HX-ray1.80A/B18-248[»]
2H0IX-ray2.40A/B18-248[»]
2IY2X-ray1.90A/B19-89[»]
5G1KX-ray1.96A/B1-248[»]
5G1LX-ray1.70A/B1-248[»]
ProteinModelPortaliP77202.
SMRiP77202.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP77202.

Family & Domainsi

Sequence similaritiesi

Belongs to the thioredoxin family. DsbC subfamily.Curated

Keywords - Domaini

Redox-active center, Signal

Phylogenomic databases

eggNOGiENOG4108KHN. Bacteria.
COG1651. LUCA.
HOGENOMiHOG000117889.
InParanoidiP77202.
KOiK03805.
OMAiKLVYAPM.
PhylomeDBiP77202.

Family and domain databases

CDDicd03020. DsbA_DsbC_DsbG. 1 hit.
Gene3Di3.40.30.10. 1 hit.
InterProiIPR033954. DiS-bond_Isoase_DsbC/G.
IPR018950. DiS-bond_isomerase_DsbC/G_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF13098. Thioredoxin_2. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
SSF54423. SSF54423. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P77202-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKKILLLAL LPAIAFAEEL PAPVKAIEKQ GITIIKTFDA PGGMKGYLGK
60 70 80 90 100
YQDMGVTIYL TPDGKHAISG YMYNEKGENL SNTLIEKEIY APAGREMWQR
110 120 130 140 150
MEQSHWLLDG KKDAPVIVYV FADPFCPYCK QFWQQARPWV DSGKVQLRTL
160 170 180 190 200
LVGVIKPESP ATAAAILASK DPAKTWQQYE ASGGKLKLNV PANVSTEQMK
210 220 230 240
VLSDNEKLMD DLGANVTPAI YYMSKENTLQ QAVGLPDQKT LNIIMGNK
Length:248
Mass (Da):27,495
Last modified:November 1, 1997 - v2
Checksum:i73D57BF7DBF52A06
GO

Sequence cautioni

The sequence AAB40805 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF000956 Genomic DNA. Translation: AAC45785.1.
U82598 Genomic DNA. Translation: AAB40805.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73705.2.
AP009048 Genomic DNA. Translation: BAA35234.2.
PIRiB64794.
RefSeqiNP_415137.2. NC_000913.3.
WP_000913829.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73705; AAC73705; b0604.
BAA35234; BAA35234; BAA35234.
GeneIDi945224.
KEGGiecj:JW0597.
eco:b0604.
PATRICi32116386. VBIEscCol129921_0633.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF000956 Genomic DNA. Translation: AAC45785.1.
U82598 Genomic DNA. Translation: AAB40805.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73705.2.
AP009048 Genomic DNA. Translation: BAA35234.2.
PIRiB64794.
RefSeqiNP_415137.2. NC_000913.3.
WP_000913829.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1V57X-ray2.00A/B18-248[»]
1V58X-ray1.70A/B18-248[»]
2H0GX-ray2.30A/B18-248[»]
2H0HX-ray1.80A/B18-248[»]
2H0IX-ray2.40A/B18-248[»]
2IY2X-ray1.90A/B19-89[»]
5G1KX-ray1.96A/B1-248[»]
5G1LX-ray1.70A/B1-248[»]
ProteinModelPortaliP77202.
SMRiP77202.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260900. 172 interactors.
DIPiDIP-9478N.
IntActiP77202. 11 interactors.
MINTiMINT-1232069.
STRINGi511145.b0604.

Proteomic databases

PaxDbiP77202.
PRIDEiP77202.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73705; AAC73705; b0604.
BAA35234; BAA35234; BAA35234.
GeneIDi945224.
KEGGiecj:JW0597.
eco:b0604.
PATRICi32116386. VBIEscCol129921_0633.

Organism-specific databases

EchoBASEiEB3306.
EcoGeneiEG13535. dsbG.

Phylogenomic databases

eggNOGiENOG4108KHN. Bacteria.
COG1651. LUCA.
HOGENOMiHOG000117889.
InParanoidiP77202.
KOiK03805.
OMAiKLVYAPM.
PhylomeDBiP77202.

Enzyme and pathway databases

BioCyciEcoCyc:DSBG-MONOMER.
ECOL316407:JW0597-MONOMER.
MetaCyc:DSBG-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP77202.
PROiP77202.

Family and domain databases

CDDicd03020. DsbA_DsbC_DsbG. 1 hit.
Gene3Di3.40.30.10. 1 hit.
InterProiIPR033954. DiS-bond_Isoase_DsbC/G.
IPR018950. DiS-bond_isomerase_DsbC/G_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF13098. Thioredoxin_2. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
SSF54423. SSF54423. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDSBG_ECOLI
AccessioniPrimary (citable) accession number: P77202
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 30, 2016
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.