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Protein

Thiol:disulfide interchange protein DsbE

Gene

dsbE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in disulfide bond formation. Catalyzes a late, reductive step in the assembly of periplasmic c-type cytochromes, probably the reduction of disulfide bonds of the apocytochrome c to allow covalent linkage with the heme. Possible subunit of a heme lyase. DsbE is maintained in a reduced state by DsbD.

GO - Molecular functioni

  • disulfide oxidoreductase activity Source: EcoCyc

GO - Biological processi

  • cell redox homeostasis Source: InterPro
  • cytochrome complex assembly Source: EcoCyc
  • oxidation-reduction process Source: EcoCyc
Complete GO annotation...

Keywords - Biological processi

Cytochrome c-type biogenesis

Enzyme and pathway databases

BioCyciEcoCyc:EG12053-MONOMER.
ECOL316407:JW2183-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Thiol:disulfide interchange protein DsbE
Alternative name(s):
Cytochrome c biogenesis protein CcmG
Gene namesi
Name:dsbE
Synonyms:ccmG, yejQ
Ordered Locus Names:b2195, JW2183
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12053. dsbE.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 44CytoplasmicSequence analysis
Transmembranei5 – 2521HelicalSequence analysisAdd
BLAST
Topological domaini26 – 185160PeriplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi80 – 801C → S: Drastic decrease in activity. 1 Publication
Mutagenesisi83 – 831C → S: Drastic decrease in activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 185185Thiol:disulfide interchange protein DsbEPRO_0000201293Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi80 ↔ 83Redox-activeCurated

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP0AA86.

Interactioni

Protein-protein interaction databases

BioGridi4263405. 11 interactions.
DIPiDIP-48446N.
STRINGi511145.b2195.

Structurei

Secondary structure

1
185
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi36 – 383Combined sources
Turni39 – 424Combined sources
Beta strandi49 – 557Combined sources
Beta strandi59 – 613Combined sources
Helixi62 – 654Combined sources
Beta strandi67 – 693Combined sources
Beta strandi71 – 766Combined sources
Helixi81 – 9515Combined sources
Beta strandi100 – 1067Combined sources
Helixi109 – 11911Combined sources
Beta strandi124 – 1296Combined sources
Helixi133 – 1386Combined sources
Beta strandi142 – 1498Combined sources
Beta strandi153 – 1619Combined sources
Helixi165 – 1706Combined sources
Helixi173 – 18311Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z5YX-ray1.94E43-185[»]
2B1KX-ray1.90A19-185[»]
2B1LX-ray1.90A/B58-185[»]
2G0FX-ray2.20A19-185[»]
3K8NX-ray2.30A1-185[»]
ProteinModelPortaliP0AA86.
SMRiP0AA86. Positions 36-184.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AA86.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 177139ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the thioredoxin family. DsbE subfamily.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4107QX9. Bacteria.
COG0526. LUCA.
HOGENOMiHOG000097218.
InParanoidiP0AA86.
KOiK02199.
OMAiKWLAEFH.
OrthoDBiEOG6WX4Q5.
PhylomeDBiP0AA86.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR004799. Periplasmic_diS_OxRdtase_DsbE.
IPR013740. Redoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF08534. Redoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR00385. dsbE. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AA86-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRKVLLIPL IIFLAIAAAL LWQLARNAEG DDPTNLESAL IGKPVPKFRL
60 70 80 90 100
ESLDNPGQFY QADVLTQGKP VLLNVWATWC PTCRAEHQYL NQLSAQGIRV
110 120 130 140 150
VGMNYKDDRQ KAISWLKELG NPYALSLFDG DGMLGLDLGV YGAPETFLID
160 170 180
GNGIIRYRHA GDLNPRVWEE EIKPLWEKYS KEAAQ
Length:185
Mass (Da):20,809
Last modified:September 13, 2005 - v1
Checksum:iA599F7B77806A6B5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00008 Genomic DNA. Translation: AAA16387.1.
U00096 Genomic DNA. Translation: AAC75255.1.
AP009048 Genomic DNA. Translation: BAE76658.1.
PIRiA64989.
RefSeqiNP_416699.1. NC_000913.3.
WP_000824439.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75255; AAC75255; b2195.
BAE76658; BAE76658; BAE76658.
GeneIDi949073.
KEGGiecj:JW2183.
eco:b2195.
PATRICi32119749. VBIEscCol129921_2284.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00008 Genomic DNA. Translation: AAA16387.1.
U00096 Genomic DNA. Translation: AAC75255.1.
AP009048 Genomic DNA. Translation: BAE76658.1.
PIRiA64989.
RefSeqiNP_416699.1. NC_000913.3.
WP_000824439.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z5YX-ray1.94E43-185[»]
2B1KX-ray1.90A19-185[»]
2B1LX-ray1.90A/B58-185[»]
2G0FX-ray2.20A19-185[»]
3K8NX-ray2.30A1-185[»]
ProteinModelPortaliP0AA86.
SMRiP0AA86. Positions 36-184.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263405. 11 interactions.
DIPiDIP-48446N.
STRINGi511145.b2195.

Proteomic databases

PaxDbiP0AA86.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75255; AAC75255; b2195.
BAE76658; BAE76658; BAE76658.
GeneIDi949073.
KEGGiecj:JW2183.
eco:b2195.
PATRICi32119749. VBIEscCol129921_2284.

Organism-specific databases

EchoBASEiEB1984.
EcoGeneiEG12053. dsbE.

Phylogenomic databases

eggNOGiENOG4107QX9. Bacteria.
COG0526. LUCA.
HOGENOMiHOG000097218.
InParanoidiP0AA86.
KOiK02199.
OMAiKWLAEFH.
OrthoDBiEOG6WX4Q5.
PhylomeDBiP0AA86.

Enzyme and pathway databases

BioCyciEcoCyc:EG12053-MONOMER.
ECOL316407:JW2183-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AA86.
PROiP0AA86.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR004799. Periplasmic_diS_OxRdtase_DsbE.
IPR013740. Redoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF08534. Redoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR00385. dsbE. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K., Church G.M.
    Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / BHB2600.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "The Escherichia coli CcmG protein fulfils a specific role in cytochrome c assembly."
    Reid E., Cole J., Eaves D.J.
    Biochem. J. 355:51-58(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-6, CHARACTERIZATION.
    Strain: K12.
  5. "Escherichia coli genes required for cytochrome c maturation."
    Thoeny-Meyer L., Fischer F., Kunzler P., Ritz D., Hennecke H.
    J. Bacteriol. 177:4321-4326(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  6. Missiakas D., Georgopoulos C., Raina S.
    Submitted (NOV-1994) to UniProtKB
    Cited for: CHARACTERIZATION.
  7. "The active-site cysteines of the periplasmic thioredoxin-like protein CcmG of Escherichia coli are important but not essential for cytochrome c maturation in vivo."
    Fabianek R.A., Hennecke H., Thoeny-Meyer L.
    J. Bacteriol. 180:1947-1950(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-80 AND CYS-83.
  8. "Biochemical characterization of the thioredoxin domain of Escherichia coli DsbE protein reveals a weak reductant."
    Li Q., Hu H.-Y., Xu G.-J.
    Biochem. Biophys. Res. Commun. 283:849-853(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  9. "Structural and redox properties of the leaderless DsbE (CcmG) protein: both active-site cysteines of the reduced form are involved in its function in the Escherichia coli periplasm."
    Li Q., Hu H.-Y., Wang W.-Q., Xu G.-J.
    Biol. Chem. 382:1679-1686(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: BL21-DE3.

Entry informationi

Entry nameiDSBE_ECOLI
AccessioniPrimary (citable) accession number: P0AA86
Secondary accession number(s): P33926, Q2MAP8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: September 13, 2005
Last modified: July 6, 2016
This is version 93 of the entry and version 1 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.