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P69853

- DMSD_ECOLI

UniProt

P69853 - DMSD_ECOLI

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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

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. signal sequence binding Source: InterPro

GO - Biological processi

  1. chaperone-mediated protein folding Source: UniProtKB-HAMAP
Complete GO annotation...

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
Complete GO annotation...

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.
InParanoidiP69853.
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

        10         20         30         40         50
MTHFSQQDNF SVAARVLGAL FYYAPESAEA APLVAVLTSD GWETQWPLPE
60 70 80 90 100
ASLAPLVTAF QTQCEETHAQ AWQRLFVGPW ALPSPPWGSV WLDRESVLFG
110 120 130 140 150
DSTLALRQWM REKGIQFEMK QNEPEDHFGS LLLMAAWLAE NGRQTECEEL
160 170 180 190 200
LAWHLFPWST RFLDVFIEKA EHPFYRALGE LARLTLAQWQ SQLLIPVAVK

PLFR
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.
InParanoidi P69853.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 82 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