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P0A6M2

- DSBB_ECOLI

UniProt

P0A6M2 - DSBB_ECOLI

Protein

Disulfide bond formation protein B

Gene

dsbB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (10 May 2005)
      Previous versions | rss
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    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
    2. response to heat Source: EcoCyc

    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 2 Publications; Multi-pass membrane protein 2 Publications

    GO - Cellular componenti

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

    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 – 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A6M2.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1414CytoplasmicCuratedAdd
    BLAST
    Topological domaini32 – 4918PeriplasmicCuratedAdd
    BLAST
    Topological domaini66 – 716CytoplasmicCurated
    Topological domaini90 – 14455PeriplasmicCuratedAdd
    BLAST
    Topological domaini164 – 17613CytoplasmicCuratedAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei15 – 3117HelicalCuratedAdd
    BLAST
    Transmembranei50 – 6516HelicalCuratedAdd
    BLAST
    Transmembranei72 – 8918HelicalCuratedAdd
    BLAST
    Transmembranei145 – 16319HelicalCuratedAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the DsbB family.Curated

    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

    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: October 1, 2014
    This is version 88 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