Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Disulfide bond formation protein B

Gene

dsbB

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

Functioni

Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by oxidizing the DsbA protein. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway.3 Publications

GO - Molecular functioni

  1. electron carrier activity Source: UniProtKB-HAMAP
  2. protein disulfide oxidoreductase activity Source: EcoCyc

GO - Biological processi

  1. electron transport chain Source: EcoCyc
  2. response to heat Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Enzyme and pathway databases

BioCyciEcoCyc:DSBBPROT-MONOMER.
ECOL316407:JW5182-MONOMER.
MetaCyc:DSBBPROT-MONOMER.

Protein family/group databases

TCDBi5.A.2.1.1. the disulfide bond oxidoreductase b (dsbb) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Disulfide bond formation protein B
Alternative name(s):
Disulfide oxidoreductase
Gene namesi
Name:dsbB
Synonyms:roxB, ycgA
Ordered Locus Names:b1185, JW5182
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11393. dsbB.

Subcellular locationi

Cell inner membrane 2 Publications; Multi-pass membrane protein 2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1414CytoplasmicCuratedAdd
BLAST
Transmembranei15 – 3117HelicalCuratedAdd
BLAST
Topological domaini32 – 4918PeriplasmicCuratedAdd
BLAST
Transmembranei50 – 6516HelicalCuratedAdd
BLAST
Topological domaini66 – 716CytoplasmicCurated
Transmembranei72 – 8918HelicalCuratedAdd
BLAST
Topological domaini90 – 14455PeriplasmicCuratedAdd
BLAST
Transmembranei145 – 16319HelicalCuratedAdd
BLAST
Topological domaini164 – 17613CytoplasmicCuratedAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Induction of the PhoP/PhoQ two-component regulatory system.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 176176Disulfide bond formation protein BPRO_0000059342Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi41 ↔ 44Redox-active1 Publication
Disulfide bondi104 ↔ 130Redox-active1 Publication

Keywords - PTMi

Disulfide bond

Expressioni

Gene expression databases

GenevestigatoriP0A6M2.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
dsbAP0AEG45EBI-1170740,EBI-549711

Protein-protein interaction databases

IntActiP0A6M2. 1 interaction.
MINTiMINT-6742413.
STRINGi511145.b1185.

Structurei

Secondary structure

1
176
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 98Combined sources
Helixi13 – 219Combined sources
Helixi23 – 3412Combined sources
Helixi44 – 6219Combined sources
Beta strandi66 – 694Combined sources
Helixi70 – 9627Combined sources
Helixi115 – 1184Combined sources
Turni122 – 1243Combined sources
Beta strandi138 – 1403Combined sources
Helixi142 – 15716Combined sources
Turni158 – 1614Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HI7X-ray3.70B1-176[»]
2K73NMR-A1-176[»]
2K74NMR-A1-176[»]
2LEGNMR-B1-176[»]
2LTQNMR-A/D1-176[»]
2ZUPX-ray3.70B1-176[»]
2ZUQX-ray3.30A/D1-176[»]
3E9JX-ray3.70C/F1-176[»]
ProteinModelPortaliP0A6M2.
SMRiP0A6M2. Positions 1-176.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6M2.

Family & Domainsi

Sequence similaritiesi

Belongs to the DsbB family.Curated

Keywords - Domaini

Redox-active center, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1495.
HOGENOMiHOG000218135.
InParanoidiP0A6M2.
KOiK03611.
OMAiPSPFVTC.
OrthoDBiEOG6CCH7H.

Family and domain databases

Gene3Di1.20.1550.10. 1 hit.
HAMAPiMF_00286. DsbB.
InterProiIPR003752. DiS_bond_form_DsbB/BdbC.
IPR022920. Disulphide_bond_form_DsbB.
IPR023380. DsbB-like_dom.
[Graphical view]
PfamiPF02600. DsbB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A6M2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRFLNQCSQ GRGAWLLMAF TALALELTAL WFQHVMLLKP CVLCIYERCA
60 70 80 90 100
LFGVLGAALI GAIAPKTPLR YVAMVIWLYS AFRGVQLTYE HTMLQLYPSP
110 120 130 140 150
FATCDFMVRF PEWLPLDKWV PQVFVASGDC AERQWDFLGL EMPQWLLGIF
160 170
IAYLIVAVLV VISQPFKAKK RDLFGR
Length:176
Mass (Da):20,142
Last modified:May 9, 2005 - v1
Checksum:i9CBD673D51E9F09B
GO

Sequence cautioni

The sequence AAA23711.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAA24220.1 differs from that shown. Reason: Frameshift at position 130. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L03721 Genomic DNA. Translation: AAA23711.1. Different initiation.
U00096 Genomic DNA. Translation: AAC74269.1.
AP009048 Genomic DNA. Translation: BAA36032.2.
M83655 Genomic DNA. Translation: AAA24220.1. Frameshift.
PIRiF64864.
RefSeqiNP_415703.3. NC_000913.3.
YP_489452.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74269; AAC74269; b1185.
BAA36032; BAA36032; BAA36032.
GeneIDi12932821.
946344.
KEGGiecj:Y75_p1157.
eco:b1185.
PATRICi32117616. VBIEscCol129921_1230.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L03721 Genomic DNA. Translation: AAA23711.1. Different initiation.
U00096 Genomic DNA. Translation: AAC74269.1.
AP009048 Genomic DNA. Translation: BAA36032.2.
M83655 Genomic DNA. Translation: AAA24220.1. Frameshift.
PIRiF64864.
RefSeqiNP_415703.3. NC_000913.3.
YP_489452.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HI7X-ray3.70B1-176[»]
2K73NMR-A1-176[»]
2K74NMR-A1-176[»]
2LEGNMR-B1-176[»]
2LTQNMR-A/D1-176[»]
2ZUPX-ray3.70B1-176[»]
2ZUQX-ray3.30A/D1-176[»]
3E9JX-ray3.70C/F1-176[»]
ProteinModelPortaliP0A6M2.
SMRiP0A6M2. Positions 1-176.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP0A6M2. 1 interaction.
MINTiMINT-6742413.
STRINGi511145.b1185.

Chemistry

BindingDBiP0A6M2.

Protein family/group databases

TCDBi5.A.2.1.1. the disulfide bond oxidoreductase b (dsbb) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74269; AAC74269; b1185.
BAA36032; BAA36032; BAA36032.
GeneIDi12932821.
946344.
KEGGiecj:Y75_p1157.
eco:b1185.
PATRICi32117616. VBIEscCol129921_1230.

Organism-specific databases

EchoBASEiEB1366.
EcoGeneiEG11393. dsbB.

Phylogenomic databases

eggNOGiCOG1495.
HOGENOMiHOG000218135.
InParanoidiP0A6M2.
KOiK03611.
OMAiPSPFVTC.
OrthoDBiEOG6CCH7H.

Enzyme and pathway databases

BioCyciEcoCyc:DSBBPROT-MONOMER.
ECOL316407:JW5182-MONOMER.
MetaCyc:DSBBPROT-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A6M2.
PROiP0A6M2.

Gene expression databases

GenevestigatoriP0A6M2.

Family and domain databases

Gene3Di1.20.1550.10. 1 hit.
HAMAPiMF_00286. DsbB.
InterProiIPR003752. DiS_bond_form_DsbB/BdbC.
IPR022920. Disulphide_bond_form_DsbB.
IPR023380. DsbB-like_dom.
[Graphical view]
PfamiPF02600. DsbB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
  2. "Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo."
    Missiakas D., Georgopoulos C., Raina S.
    Proc. Natl. Acad. Sci. U.S.A. 90:7084-7088(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Cloning, sequencing, and expression of the nhaB gene, encoding a Na+/H+ antiporter in Escherichia coli."
    Pinner E., Padan E., Schuldiner S.
    J. Biol. Chem. 267:11064-11068(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-169.
    Strain: K12.
  7. "Two cysteines in each periplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formation."
    Jander G., Martin N.L., Beckwith J.
    EMBO J. 13:5121-5127(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF CYSTEINE RESIDUES.
  8. "Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway."
    Kobayashi T., Ito K.
    EMBO J. 18:1192-1198(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: REDOX-ACTIVE SITES, DISULFIDE BONDS.
  9. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: K12 / MG1655 / ATCC 47076.
  10. "Perturbation of the oxidizing environment of the periplasm stimulates the PhoQ/PhoP system in Escherichia coli."
    Lippa A.M., Goulian M.
    J. Bacteriol. 194:1457-1463(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOP/PHOQ REGULATION, DISRUPTION PHENOTYPE.
    Strain: K12 / MG1655 / ATCC 47076.

Entry informationi

Entry nameiDSBB_ECOLI
AccessioniPrimary (citable) accession number: P0A6M2
Secondary accession number(s): P30018, Q47408
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 9, 2005
Last sequence update: May 9, 2005
Last modified: January 6, 2015
This is version 91 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, 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

External Data

Dasty 3

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 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.