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P69853

- DMSD_ECOLI

UniProt

P69853 - DMSD_ECOLI

Protein

Tat proofreading chaperone DmsD

Gene

dmsD

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 81 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Required for biogenesis/assembly of DMSO reductase, but not for the interaction of the DmsA signal peptide with the Tat system. May be part of a chaperone cascade complex that facilitates a folding-maturation pathway for the substrate protein.4 PublicationsUniRule annotation

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. signal sequence binding Source: InterPro

    GO - Biological processi

    1. chaperone-mediated protein folding Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Chaperone

    Enzyme and pathway databases

    BioCyciEcoCyc:G6849-MONOMER.
    ECOL316407:JW5262-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tat proofreading chaperone DmsDUniRule annotation
    Alternative name(s):
    DMSO reductase maturation proteinUniRule annotation
    Twin-arginine leader-binding protein DmsDUniRule annotation
    Gene namesi
    Name:dmsDUniRule annotation
    Synonyms:ynfI
    Ordered Locus Names:b1591, JW5262
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG13847. dmsD.

    Subcellular locationi

    Cell inner membrane 1 Publication; Peripheral membrane protein 1 Publication. Cytoplasm 1 Publication
    Note: Mainly cytoplasmic under aerobic conditions, and found in the inner membrane under anaerobic conditions.

    GO - Cellular componenti

    1. cytoplasm Source: EcoCyc
    2. extrinsic component of cytoplasmic side of plasma membrane Source: EcoCyc

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi72 – 754WQRL → HQRY: 1.5-fold increased binding to DmsA signal sequence. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 204203Tat proofreading chaperone DmsDPRO_0000211649Add
    BLAST

    Expressioni

    Gene expression databases

    GenevestigatoriP69853.

    Interactioni

    Subunit structurei

    Monomer and homodimer. Binds to the twin-arginine signal peptide of DmsA and TorA (PubMed:11309116), although the latter binding is controversial (PubMed:20169075). Interacts with the TatB and TatC subunits of the Tat translocase complex. Interacts also with other general chaperones, such as GroEL, and proteins involved in the molybdenum cofactor biosynthesis.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    dmsAP187757EBI-4406374,EBI-4411104
    dnaKC4ZPU05EBI-4406374,EBI-4406497From a different organism.
    groLC5A1D55EBI-4406374,EBI-4406290From a different organism.
    grpEC4ZYN14EBI-4406374,EBI-4407105From a different organism.
    moeBC4ZXZ85EBI-4406374,EBI-4407215From a different organism.
    tigC4ZTJ33EBI-4406374,EBI-4407188From a different organism.
    tufAC4ZUJ44EBI-4406374,EBI-4407165From a different organism.
    ynfEP773743EBI-4406374,EBI-556186
    ynfFP777832EBI-4406374,EBI-6406285

    Protein-protein interaction databases

    DIPiDIP-47840N.
    IntActiP69853. 18 interactions.
    MINTiMINT-8046358.
    STRINGi511145.b1591.

    Structurei

    Secondary structure

    1
    204
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 63
    Helixi10 – 2213
    Turni28 – 303
    Helixi31 – 377
    Helixi42 – 454
    Beta strandi46 – 483
    Helixi50 – 6011
    Helixi68 – 769
    Helixi88 – 925
    Helixi101 – 11212
    Helixi128 – 14013
    Helixi144 – 15411
    Helixi156 – 16914
    Helixi173 – 19119

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3CW0X-ray2.40A/B/C/D1-204[»]
    3EFPX-ray2.01A/B1-204[»]
    3U41X-ray2.50A/B/C/D/E/F/G/H1-204[»]
    ProteinModelPortaliP69853.
    SMRiP69853. Positions 1-204.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP69853.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the TorD/DmsD family. DmsD subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG3381.
    HOGENOMiHOG000120828.
    OMAiEDHIGLM.
    OrthoDBiEOG6FZ4BH.
    PhylomeDBiP69853.

    Family and domain databases

    HAMAPiMF_00940. DmsD_chaperone.
    InterProiIPR026269. DmsD-type.
    IPR028611. DmsD_chaperone.
    IPR020945. DMSO/NO3_reduct_chaperone.
    [Graphical view]
    PfamiPF02613. Nitrate_red_del. 1 hit.
    [Graphical view]
    PIRSFiPIRSF004690. DmsD. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P69853-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTHFSQQDNF SVAARVLGAL FYYAPESAEA APLVAVLTSD GWETQWPLPE    50
    ASLAPLVTAF QTQCEETHAQ AWQRLFVGPW ALPSPPWGSV WLDRESVLFG 100
    DSTLALRQWM REKGIQFEMK QNEPEDHFGS LLLMAAWLAE NGRQTECEEL 150
    LAWHLFPWST RFLDVFIEKA EHPFYRALGE LARLTLAQWQ SQLLIPVAVK 200
    PLFR 204
    Length:204
    Mass (Da):23,345
    Last modified:January 23, 2007 - v2
    Checksum:iCB4273F4B6539D47
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti7 – 71Missing AA sequence (PubMed:11309116)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00096 Genomic DNA. Translation: AAC74663.2.
    AP009048 Genomic DNA. Translation: BAA15315.1.
    PIRiA64915.
    RefSeqiNP_416108.2. NC_000913.3.
    YP_489854.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74663; AAC74663; b1591.
    BAA15315; BAA15315; BAA15315.
    GeneIDi12930123.
    945987.
    KEGGiecj:Y75_p1567.
    eco:b1591.
    PATRICi32118484. VBIEscCol129921_1662.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00096 Genomic DNA. Translation: AAC74663.2 .
    AP009048 Genomic DNA. Translation: BAA15315.1 .
    PIRi A64915.
    RefSeqi NP_416108.2. NC_000913.3.
    YP_489854.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3CW0 X-ray 2.40 A/B/C/D 1-204 [» ]
    3EFP X-ray 2.01 A/B 1-204 [» ]
    3U41 X-ray 2.50 A/B/C/D/E/F/G/H 1-204 [» ]
    ProteinModelPortali P69853.
    SMRi P69853. Positions 1-204.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-47840N.
    IntActi P69853. 18 interactions.
    MINTi MINT-8046358.
    STRINGi 511145.b1591.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC74663 ; AAC74663 ; b1591 .
    BAA15315 ; BAA15315 ; BAA15315 .
    GeneIDi 12930123.
    945987.
    KEGGi ecj:Y75_p1567.
    eco:b1591.
    PATRICi 32118484. VBIEscCol129921_1662.

    Organism-specific databases

    EchoBASEi EB3608.
    EcoGenei EG13847. dmsD.

    Phylogenomic databases

    eggNOGi COG3381.
    HOGENOMi HOG000120828.
    OMAi EDHIGLM.
    OrthoDBi EOG6FZ4BH.
    PhylomeDBi P69853.

    Enzyme and pathway databases

    BioCyci EcoCyc:G6849-MONOMER.
    ECOL316407:JW5262-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P69853.
    PROi P69853.

    Gene expression databases

    Genevestigatori P69853.

    Family and domain databases

    HAMAPi MF_00940. DmsD_chaperone.
    InterProi IPR026269. DmsD-type.
    IPR028611. DmsD_chaperone.
    IPR020945. DMSO/NO3_reduct_chaperone.
    [Graphical view ]
    Pfami PF02613. Nitrate_red_del. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF004690. DmsD. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "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.
    4. "Identification of a twin-arginine leader-binding protein."
      Oresnik I.J., Ladner C.L., Turner R.J.
      Mol. Microbiol. 40:323-331(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-11, FUNCTION, INTERACTION WITH SIGNAL PEPTIDES OF DMSA AND TORA.
    5. "DmsD is required for the biogenesis of DMSO reductase in Escherichia coli but not for the interaction of the DmsA signal peptide with the Tat apparatus."
      Ray N., Oates J., Turner R.J., Robinson C.
      FEBS Lett. 534:156-160(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "The twin-arginine leader-binding protein, DmsD, interacts with the TatB and TatC subunits of the Escherichia coli twin-arginine translocase."
      Papish A.L., Ladner C.L., Turner R.J.
      J. Biol. Chem. 278:32501-32506(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TATB AND TATC.
    7. "Folding forms of Escherichia coli DmsD, a twin-arginine leader binding protein."
      Sarfo K.J., Winstone T.L., Papish A.L., Howell J.M., Kadir H., Vogel H.J., Turner R.J.
      Biochem. Biophys. Res. Commun. 315:397-403(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    8. "DmsD, a Tat system specific chaperone, interacts with other general chaperones and proteins involved in the molybdenum cofactor biosynthesis."
      Li H., Chang L., Howell J.M., Turner R.J.
      Biochim. Biophys. Acta 1804:1301-1309(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CHAPERONES AND MOCO BIOSYNTHESIS PROTEINS.
    9. "Visualizing interactions along the Escherichia coli twin-arginine translocation pathway using protein fragment complementation."
      Kostecki J.S., Li H., Turner R.J., DeLisa M.P.
      PLoS ONE 5:E9225-E9225(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DMSA; TATB AND TATC, MUTAGENESIS OF 72-TRP--LEU-75.
    10. "Structure of the twin-arginine signal-binding protein DmsD from Escherichia coli."
      Ramasamy S.K., Clemons W.M. Jr.
      Acta Crystallogr. F 65:746-750(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS).
    11. "Structural analysis of a monomeric form of the twin-arginine leader peptide binding chaperone Escherichia coli DmsD."
      Stevens C.M., Winstone T.M., Turner R.J., Paetzel M.
      J. Mol. Biol. 389:124-133(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS).

    Entry informationi

    Entry nameiDMSD_ECOLI
    AccessioniPrimary (citable) accession number: P69853
    Secondary accession number(s): P76174, P77270
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 81 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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