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P0A6M2 (DSBB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Disulfide bond formation protein B
Alternative name(s):
Disulfide oxidoreductase
Gene names
Name:dsbB
Synonyms:roxB, ycgA
Ordered Locus Names:b1185, JW5182
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length176 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2 Ref.10

Subcellular location

Cell inner membrane; Multi-pass membrane protein Ref.1 Ref.7.

Disruption phenotype

Induction of the PhoP/PhoQ two-component regulatory system. Ref.10

Sequence similarities

Belongs to the DsbB family.

Sequence caution

The sequence AAA23711.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAA24220.1 differs from that shown. Reason: Frameshift at position 130.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

dsbAP0AEG45EBI-1170740,EBI-549711

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 176176Disulfide bond formation protein B HAMAP-Rule MF_00286
PRO_0000059342

Regions

Topological domain1 – 1414Cytoplasmic Probable
Transmembrane15 – 3117Helical; Probable
Topological domain32 – 4918Periplasmic Probable
Transmembrane50 – 6516Helical; Probable
Topological domain66 – 716Cytoplasmic Probable
Transmembrane72 – 8918Helical; Probable
Topological domain90 – 14455Periplasmic Probable
Transmembrane145 – 16319Helical; Probable
Topological domain164 – 17613Cytoplasmic Probable

Amino acid modifications

Disulfide bond41 ↔ 44Redox-active Ref.8
Disulfide bond104 ↔ 130Redox-active Ref.8

Secondary structure

..................... 176
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A6M2 [UniParc].

Last modified May 10, 2005. Version 1.
Checksum: 9CBD673D51E9F09B

FASTA17620,142
        10         20         30         40         50         60 
MLRFLNQCSQ GRGAWLLMAF TALALELTAL WFQHVMLLKP CVLCIYERCA LFGVLGAALI 

        70         80         90        100        110        120 
GAIAPKTPLR YVAMVIWLYS AFRGVQLTYE HTMLQLYPSP FATCDFMVRF PEWLPLDKWV 

       130        140        150        160        170 
PQVFVASGDC AERQWDFLGL EMPQWLLGIF IAYLIVAVLV VISQPFKAKK RDLFGR 

« Hide

References

« Hide 'large scale' references
[1]"A pathway for disulfide bond formation in vivo."
Bardwell J.C.A., Lee J.-O., Jander G., Martin N., Belin D., Beckwith J.
Proc. Natl. Acad. Sci. U.S.A. 90:1038-1042(1993) [PubMed] [Europe PMC] [Abstract]
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(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[3]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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(2006) [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(1992) [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(1994) [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(1999) [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(2005) [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(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOP/PHOQ REGULATION, DISRUPTION PHENOTYPE.
Strain: K12 / MG1655 / ATCC 47076.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRF64864.
RefSeqNP_415703.3. NC_000913.3.
YP_489452.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP0A6M2.
SMRP0A6M2. Positions 1-176.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP0A6M2. 1 interaction.
MINTMINT-6742413.
STRING511145.b1185.

Chemistry

BindingDBP0A6M2.

Protein family/group databases

TCDB5.A.2.1.1. the disulfide bond oxidoreductase b (dsbb) family.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74269; AAC74269; b1185.
BAA36032; BAA36032; BAA36032.
GeneID12932821.
946344.
KEGGecj:Y75_p1157.
eco:b1185.
PATRIC32117616. VBIEscCol129921_1230.

Organism-specific databases

EchoBASEEB1366.
EcoGeneEG11393. dsbB.

Phylogenomic databases

eggNOGCOG1495.
HOGENOMHOG000218135.
KOK03611.
OMAVLIAQPF.
OrthoDBEOG6CCH7H.
ProtClustDBPRK01749.

Enzyme and pathway databases

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

Gene expression databases

GenevestigatorP0A6M2.

Family and domain databases

Gene3D1.20.1550.10. 1 hit.
HAMAPMF_00286. DsbB.
InterProIPR003752. DiS_bond_form_DsbB/BdbC.
IPR022920. Disulphide_bond_form_DsbB.
IPR023380. DsbB-like_dom.
[Graphical view]
PfamPF02600. DsbB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A6M2.
PROP0A6M2.

Entry information

Entry nameDSBB_ECOLI
AccessionPrimary (citable) accession number: P0A6M2
Secondary accession number(s): P30018, Q47408
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: May 10, 2005
Last modified: March 19, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene