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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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi126 – 1261C → A: Complete loss of redox activity. 1 Publication
Mutagenesisi126 – 1261C → S: No loss of chaperone activity; when associated with S-129. 1 Publication
Mutagenesisi129 – 1291C → A: Partial loss of redox activity. Traps the protein in complex with ErfK, YbiS and YnhG. 2 Publications
Mutagenesisi129 – 1291C → S: No loss of chaperone activity; when associated with S-126. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 17171 PublicationAdd
BLAST
Chaini18 – 248231Thiol:disulfide interchange protein DsbGPRO_0000034278Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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 interactions.
DIPiDIP-9478N.
IntActiP77202. 11 interactions.
MINTiMINT-1232069.
STRINGi511145.b0604.

Structurei

Secondary structure

1
248
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi22 – 287Combined sources
Turni29 – 313Combined sources
Beta strandi32 – 398Combined sources
Helixi41 – 433Combined sources
Beta strandi45 – 517Combined sources
Beta strandi54 – 607Combined sources
Beta strandi67 – 704Combined sources
Helixi80 – 889Combined sources
Helixi92 – 943Combined sources
Helixi95 – 1028Combined sources
Beta strandi107 – 1104Combined sources
Beta strandi115 – 1228Combined sources
Helixi127 – 14115Combined sources
Beta strandi144 – 1518Combined sources
Helixi159 – 16810Combined sources
Beta strandi169 – 1713Combined sources
Helixi172 – 18110Combined sources
Turni182 – 1843Combined sources
Helixi196 – 21217Combined sources
Beta strandi219 – 2246Combined sources
Turni225 – 2273Combined sources
Beta strandi228 – 2358Combined sources
Helixi238 – 2447Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 19-247.
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

Gene3Di3.40.30.10. 1 hit.
InterProiIPR018950. 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
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. Positions 19-247.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260900. 172 interactions.
DIPiDIP-9478N.
IntActiP77202. 11 interactions.
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

Gene3Di3.40.30.10. 1 hit.
InterProiIPR018950. 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: September 7, 2016
This is version 132 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.