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P0A6M2

- DSBB_ECOLI

UniProt

P0A6M2 - DSBB_ECOLI

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Protein
Disulfide bond formation protein B
Gene
dsbB, roxB, ycgA, b1185, JW5182
Organism
Escherichia coli (strain K12)
Status
Reviewed - 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 binding Source: IntAct
  3. protein disulfide oxidoreductase activity Source: EcoCyc

GO - Biological processi

  1. electron transport chain 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: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11393. dsbB.

Subcellular locationi

Cell inner membrane; Multi-pass membrane protein 2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1414Cytoplasmic Inferred
Add
BLAST
Transmembranei15 – 3117Helical; Inferred
Add
BLAST
Topological domaini32 – 4918Periplasmic Inferred
Add
BLAST
Transmembranei50 – 6516Helical; Inferred
Add
BLAST
Topological domaini66 – 716Cytoplasmic Inferred
Transmembranei72 – 8918Helical; Inferred
Add
BLAST
Topological domaini90 – 14455Periplasmic Inferred
Add
BLAST
Transmembranei145 – 16319Helical; Inferred
Add
BLAST
Topological domaini164 – 17613Cytoplasmic Inferred
Add
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 BUniRule annotation
PRO_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

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP0A6M2.

Family & Domainsi

Sequence similaritiesi

Belongs to the DsbB family.

Keywords - Domaini

Redox-active center, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1495.
HOGENOMiHOG000218135.
KOiK03611.
OMAiVLIAQPF.
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

MLRFLNQCSQ GRGAWLLMAF TALALELTAL WFQHVMLLKP CVLCIYERCA    50
LFGVLGAALI GAIAPKTPLR YVAMVIWLYS AFRGVQLTYE HTMLQLYPSP 100
FATCDFMVRF PEWLPLDKWV PQVFVASGDC AERQWDFLGL EMPQWLLGIF 150
IAYLIVAVLV VISQPFKAKK RDLFGR 176
Length:176
Mass (Da):20,142
Last modified:May 10, 2005 - v1
Checksum:i9CBD673D51E9F09B
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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.
PIRi F64864.
RefSeqi NP_415703.3. NC_000913.3.
YP_489452.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2HI7 X-ray 3.70 B 1-176 [» ]
2K73 NMR - A 1-176 [» ]
2K74 NMR - A 1-176 [» ]
2LEG NMR - B 1-176 [» ]
2LTQ NMR - A/D 1-176 [» ]
2ZUP X-ray 3.70 B 1-176 [» ]
2ZUQ X-ray 3.30 A/D 1-176 [» ]
3E9J X-ray 3.70 C/F 1-176 [» ]
ProteinModelPortali P0A6M2.
SMRi P0A6M2. Positions 1-176.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P0A6M2. 1 interaction.
MINTi MINT-6742413.
STRINGi 511145.b1185.

Chemistry

BindingDBi P0A6M2.

Protein family/group databases

TCDBi 5.A.2.1.1. the disulfide bond oxidoreductase b (dsbb) family.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74269 ; AAC74269 ; b1185 .
BAA36032 ; BAA36032 ; BAA36032 .
GeneIDi 12932821.
946344.
KEGGi ecj:Y75_p1157.
eco:b1185.
PATRICi 32117616. VBIEscCol129921_1230.

Organism-specific databases

EchoBASEi EB1366.
EcoGenei EG11393. dsbB.

Phylogenomic databases

eggNOGi COG1495.
HOGENOMi HOG000218135.
KOi K03611.
OMAi VLIAQPF.
OrthoDBi EOG6CCH7H.

Enzyme and pathway databases

BioCyci EcoCyc:DSBBPROT-MONOMER.
ECOL316407:JW5182-MONOMER.
MetaCyc:DSBBPROT-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A6M2.
PROi P0A6M2.

Gene expression databases

Genevestigatori P0A6M2.

Family and domain databases

Gene3Di 1.20.1550.10. 1 hit.
HAMAPi MF_00286. DsbB.
InterProi IPR003752. DiS_bond_form_DsbB/BdbC.
IPR022920. Disulphide_bond_form_DsbB.
IPR023380. DsbB-like_dom.
[Graphical view ]
Pfami PF02600. DsbB. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1993) [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(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.

Entry informationi

Entry nameiDSBB_ECOLI
AccessioniPrimary (citable) accession number: P0A6M2
Secondary accession number(s): P30018, Q47408
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: May 10, 2005
Last modified: June 11, 2014
This is version 87 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

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