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P36655

- DSBD_ECOLI

UniProt

P36655 - DSBD_ECOLI

Protein

Thiol:disulfide interchange protein DsbD

Gene

dsbD

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 156 (01 Oct 2014)
      Sequence version 4 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm, thereby maintaining the active site of DsbC, DsbE and DsbG in a reduced state. This transfer involves a cascade of disulfide bond formation and reduction steps.

    Catalytic activityi

    Protein dithiol + NAD(P)+ = protein disulfide + NAD(P)H.

    GO - Molecular functioni

    1. electron carrier activity Source: UniProtKB-HAMAP
    2. oxidoreductase activity Source: EcoliWiki
    3. protein disulfide oxidoreductase activity Source: EcoCyc
    4. protein-disulfide reductase activity Source: UniProtKB-HAMAP
    5. transmembrane electron transfer carrier Source: EcoCyc

    GO - Biological processi

    1. cell redox homeostasis Source: EcoCyc
    2. cellular response to temperature stimulus Source: EcoliWiki
    3. cytochrome complex assembly Source: EcoliWiki
    4. oxidation-reduction process Source: EcoCyc
    5. response to drug Source: EcoliWiki
    6. transmembrane transport Source: GOC

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Cytochrome c-type biogenesis, Electron transport, Transport

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciEcoCyc:DSBD-MONOMER.
    ECOL316407:JW5734-MONOMER.
    MetaCyc:DSBD-MONOMER.

    Protein family/group databases

    TCDBi5.A.1.1.1. the disulfide bond oxidoreductase d (dsbd) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thiol:disulfide interchange protein DsbD (EC:1.8.1.8)
    Alternative name(s):
    C-type cytochrome biogenesis protein CycZ
    Inner membrane copper tolerance protein
    Protein-disulfide reductase
    Short name:
    Disulfide reductase
    Gene namesi
    Name:dsbD
    Synonyms:cutA2, cycZ, dipZ
    Ordered Locus Names:b4136, JW5734
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG12178. dipZ.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasmic side of plasma membrane Source: EcoCyc
    2. integral component of plasma membrane Source: EcoliWiki

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi13 – 131C → A: No loss of activity. 1 Publication
    Mutagenesisi122 – 1221C → A: Loss of activity. 3 Publications
    Mutagenesisi128 – 1281C → A: Loss of activity. 3 Publications
    Mutagenesisi182 – 1821C → A: Loss of activity. 3 Publications
    Mutagenesisi301 – 3011C → A: No loss of activity. 3 Publications
    Mutagenesisi304 – 3041C → A: Loss of activity. 3 Publications
    Mutagenesisi480 – 4801C → A: Loss of activity; when associated with A-483. 3 Publications
    Mutagenesisi483 – 4831C → A: Loss of activity; when associated with A-480. 3 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 19191 PublicationAdd
    BLAST
    Chaini20 – 565546Thiol:disulfide interchange protein DsbDPRO_0000007373Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi122 ↔ 128Redox-activeCurated
    Disulfide bondi182 ↔ 304Redox-activeCurated
    Disulfide bondi480 ↔ 483Redox-activeCurated

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PRIDEiP36655.

    Expressioni

    Gene expression databases

    GenevestigatoriP36655.

    Interactioni

    Protein-protein interaction databases

    DIPiDIP-9476N.
    STRINGi511145.b4136.

    Structurei

    Secondary structure

    1
    565
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi25 – 284
    Helixi33 – 364
    Beta strandi37 – 448
    Beta strandi47 – 548
    Beta strandi58 – 614
    Helixi62 – 643
    Beta strandi66 – 749
    Beta strandi83 – 875
    Turni88 – 903
    Beta strandi91 – 966
    Beta strandi98 – 11922
    Beta strandi121 – 1233
    Turni124 – 1263
    Beta strandi132 – 1376
    Helixi456 – 46611
    Beta strandi471 – 4766
    Helixi481 – 4899
    Turni490 – 4923
    Helixi494 – 4996
    Turni500 – 5023
    Beta strandi503 – 5097
    Helixi515 – 5239
    Beta strandi528 – 5358
    Helixi543 – 5453
    Beta strandi547 – 5493
    Helixi553 – 56210

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JPEX-ray1.90A20-151[»]
    1JZDX-ray2.30C20-151[»]
    1L6PX-ray1.65A20-144[»]
    1VRSX-ray2.85A/B/C20-162[»]
    D/E/F438-565[»]
    1Z5YX-ray1.94D20-162[»]
    2FWEX-ray1.65A438-565[»]
    2FWFX-ray1.30A438-565[»]
    2FWGX-ray1.10A438-565[»]
    2FWHX-ray0.99A438-565[»]
    3PFUX-ray1.80A21-151[»]
    4IP1X-ray2.47A444-565[»]
    4IP6X-ray2.23A444-565[»]
    ProteinModelPortaliP36655.
    SMRiP36655. Positions 23-143, 447-563.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP36655.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini20 – 162143PeriplasmicSequence AnalysisAdd
    BLAST
    Topological domaini184 – 20724CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini229 – 24214PeriplasmicSequence AnalysisAdd
    BLAST
    Topological domaini264 – 29532CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini317 – 3226PeriplasmicSequence Analysis
    Topological domaini344 – 35613CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini378 – 3836PeriplasmicSequence Analysis
    Topological domaini405 – 41713CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini439 – 565127PeriplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei163 – 18321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei208 – 22821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei243 – 26321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei296 – 31621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei323 – 34321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei357 – 37721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei384 – 40421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei418 – 43821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini434 – 565132ThioredoxinAdd
    BLAST

    Sequence similaritiesi

    Belongs to the thioredoxin family. DsbD subfamily.Curated
    Contains 1 thioredoxin domain.Curated

    Keywords - Domaini

    Redox-active center, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG4232.
    HOGENOMiHOG000254981.
    KOiK04084.
    OMAiTHILWAG.
    OrthoDBiEOG69D3B9.
    PhylomeDBiP36655.

    Family and domain databases

    Gene3Di2.60.40.1250. 1 hit.
    3.40.30.10. 1 hit.
    HAMAPiMF_00399. DbsD.
    InterProiIPR003834. Cyt_c_assmbl_TM_dom.
    IPR028250. DsbDN.
    IPR022910. Thiol_diS_interchange_DbsD.
    IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    [Graphical view]
    PANTHERiPTHR32234. PTHR32234. 1 hit.
    PfamiPF11412. DsbC. 1 hit.
    PF02683. DsbD. 1 hit.
    [Graphical view]
    SUPFAMiSSF52833. SSF52833. 1 hit.
    SSF74863. SSF74863. 1 hit.
    PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
    PS51352. THIOREDOXIN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P36655-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAQRIFTLIL LLCSTSVFAG LFDAPGRSQF VPADQAFAFD FQQNQHDLNL    50
    TWQIKDGYYL YRKQIRITPE HAKIADVQLP QGVWHEDEFY GKSEIYRDRL 100
    TLPVTINQAS AGATLTVTYQ GCADAGFCYP PETKTVPLSE VVANNAAPQP 150
    VSVPQQEQPT AQLPFSALWA LLIGIGIAFT PCVLPMYPLI SGIVLGGKQR 200
    LSTARALLLT FIYVQGMALT YTALGLVVAA AGLQFQAALQ HPYVLIGLAI 250
    VFTLLAMSMF GLFTLQLPSS LQTRLTLMSN RQQGGSPGGV FVMGAIAGLI 300
    CSPCTTAPLS AILLYIAQSG NMWLGGGTLY LYALGMGLPL MLITVFGNRL 350
    LPKSGPWMEQ VKTAFGFVIL ALPVFLLERV IGDVWGLRLW SALGVAFFGW 400
    AFITSLQAKR GWMRIVQIIL LAAALVSVRP LQDWAFGATH TAQTQTHLNF 450
    TQIKTVDELN QALVEAKGKP VMLDLYADWC VACKEFEKYT FSDPQVQKAL 500
    ADTVLLQANV TANDAQDVAL LKHLNVLGLP TILFFDGQGQ EHPQARVTGF 550
    MDAETFSAHL RDRQP 565
    Length:565
    Mass (Da):61,795
    Last modified:June 1, 2001 - v4
    Checksum:i41EFAA1C9EAC6C5F
    GO

    Sequence cautioni

    The sequence CAA54781.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAA85375.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z36905 Genomic DNA. Translation: CAA85375.1. Different initiation.
    X77707 Genomic DNA. Translation: CAA54781.1. Different initiation.
    U14003 Genomic DNA. Translation: AAA97035.1.
    U00096 Genomic DNA. Translation: AAC77096.1.
    AP009048 Genomic DNA. Translation: BAE78138.1.
    PIRiS56364.
    RefSeqiNP_418559.1. NC_000913.3.
    YP_492279.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC77096; AAC77096; b4136.
    BAE78138; BAE78138; BAE78138.
    GeneIDi12933697.
    948649.
    KEGGiecj:Y75_p4023.
    eco:b4136.
    PATRICi32123839. VBIEscCol129921_4267.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z36905 Genomic DNA. Translation: CAA85375.1 . Different initiation.
    X77707 Genomic DNA. Translation: CAA54781.1 . Different initiation.
    U14003 Genomic DNA. Translation: AAA97035.1 .
    U00096 Genomic DNA. Translation: AAC77096.1 .
    AP009048 Genomic DNA. Translation: BAE78138.1 .
    PIRi S56364.
    RefSeqi NP_418559.1. NC_000913.3.
    YP_492279.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JPE X-ray 1.90 A 20-151 [» ]
    1JZD X-ray 2.30 C 20-151 [» ]
    1L6P X-ray 1.65 A 20-144 [» ]
    1VRS X-ray 2.85 A/B/C 20-162 [» ]
    D/E/F 438-565 [» ]
    1Z5Y X-ray 1.94 D 20-162 [» ]
    2FWE X-ray 1.65 A 438-565 [» ]
    2FWF X-ray 1.30 A 438-565 [» ]
    2FWG X-ray 1.10 A 438-565 [» ]
    2FWH X-ray 0.99 A 438-565 [» ]
    3PFU X-ray 1.80 A 21-151 [» ]
    4IP1 X-ray 2.47 A 444-565 [» ]
    4IP6 X-ray 2.23 A 444-565 [» ]
    ProteinModelPortali P36655.
    SMRi P36655. Positions 23-143, 447-563.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-9476N.
    STRINGi 511145.b4136.

    Protein family/group databases

    TCDBi 5.A.1.1.1. the disulfide bond oxidoreductase d (dsbd) family.

    Proteomic databases

    PRIDEi P36655.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC77096 ; AAC77096 ; b4136 .
    BAE78138 ; BAE78138 ; BAE78138 .
    GeneIDi 12933697.
    948649.
    KEGGi ecj:Y75_p4023.
    eco:b4136.
    PATRICi 32123839. VBIEscCol129921_4267.

    Organism-specific databases

    EchoBASEi EB2095.
    EcoGenei EG12178. dipZ.

    Phylogenomic databases

    eggNOGi COG4232.
    HOGENOMi HOG000254981.
    KOi K04084.
    OMAi THILWAG.
    OrthoDBi EOG69D3B9.
    PhylomeDBi P36655.

    Enzyme and pathway databases

    BioCyci EcoCyc:DSBD-MONOMER.
    ECOL316407:JW5734-MONOMER.
    MetaCyc:DSBD-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P36655.
    PROi P36655.

    Gene expression databases

    Genevestigatori P36655.

    Family and domain databases

    Gene3Di 2.60.40.1250. 1 hit.
    3.40.30.10. 1 hit.
    HAMAPi MF_00399. DbsD.
    InterProi IPR003834. Cyt_c_assmbl_TM_dom.
    IPR028250. DsbDN.
    IPR022910. Thiol_diS_interchange_DbsD.
    IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    [Graphical view ]
    PANTHERi PTHR32234. PTHR32234. 1 hit.
    Pfami PF11412. DsbC. 1 hit.
    PF02683. DsbD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52833. SSF52833. 1 hit.
    SSF74863. SSF74863. 1 hit.
    PROSITEi PS00194. THIOREDOXIN_1. 1 hit.
    PS51352. THIOREDOXIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli."
      Missiakas D., Schwager F., Raina S.
      EMBO J. 14:3415-3424(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
    2. "Molecular genetics of a chromosomal locus involved in copper tolerance in Escherichia coli K-12."
      Fong S.-T., Camakaris J., Lee B.T.O.
      Mol. Microbiol. 15:1127-1137(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. "The biogenesis of c-type cytochromes in Escherichia coli requires a membrane-bound protein, DipZ, with a protein disulphide isomerase-like domain."
      Crooke H.R., Cole J.A.
      Mol. Microbiol. 15:1139-1150(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    4. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
      Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
      Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    6. "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.
    7. "Escherichia coli DipZ: anatomy of a transmembrane protein disulphide reductase in which three pairs of cysteine residues, one in each of three domains, contribute differentially to function."
      Gordon E.H.J., Page M.D., Willis A.C., Ferguson S.J.
      Mol. Microbiol. 35:1360-1374(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-8 AND 20-34, TOPOLOGY, MUTAGENESIS OF CYS-122; CYS-128; CYS-182; CYS-301; CYS-304; CYS-480 AND CYS-483.
    8. "Transfer of electrons across the cytoplasmic membrane by DsbD, a membrane protein involved in thiol-disulphide exchange and protein folding in the bacterial periplasm."
      Chung J., Chen T., Missiakas D.
      Mol. Microbiol. 35:1099-1109(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-27, TOPOLOGY, MUTAGENESIS OF CYS-122; CYS-128; CYS-182; CYS-301; CYS-304; CYS-480 AND CYS-483.
      Strain: BL21-DE3.
    9. Missiakas D., Hughes G.J., Frutiger S., Paquet N., Raina S.
      Submitted (MAY-1995) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 78-82.
    10. "Specific thiol compounds complement deficiency in c-type cytochrome biogenesis in Escherichia coli carrying a mutation in a membrane-bound disulphide isomerase-like protein."
      Sambongi Y., Ferguson S.J.
      FEBS Lett. 353:235-238(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    11. "Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli."
      Stewart E.J., Katzen F., Beckwith J.
      EMBO J. 18:5963-5971(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: TOPOLOGY, MUTAGENESIS OF CYS-13; CYS-122; CYS-128; CYS-182; CYS-301; CYS-304; CYS-480 AND CYS-483.
      Strain: DHB4 and RI242.
    12. "Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade."
      Katzen F., Beckwith J.
      Cell 103:769-779(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    13. "DsbD-catalyzed transport of electrons across the membrane of Escherichia coli."
      Krupp R., Chan C., Missiakas D.
      J. Biol. Chem. 276:3696-3701(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
      Strain: K38.
    14. "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.

    Entry informationi

    Entry nameiDSBD_ECOLI
    AccessioniPrimary (citable) accession number: P36655
    Secondary accession number(s): P76796, Q2M6G8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 156 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The consequences of replacement of the cysteines with alanines were found to depend on the conditions tested and on the reporter system used for the analysis, and then differ depending on the references.

    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

    External Data

    Dasty 3