Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P69853 (DMSD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tat proofreading chaperone DmsD
Alternative name(s):
DMSO reductase maturation protein
Twin-arginine leader-binding protein DmsD
Gene names
Name:dmsD
Synonyms:ynfI
Ordered Locus Names:b1591, JW5262
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length204 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.5 Ref.6 Ref.8

Subunit structure

Monomer and homodimer. Binds to the twin-arginine signal peptide of DmsA and TorA (Ref.4), although the latter binding is controversial (Ref.9). 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. Ref.4 Ref.6 Ref.7 Ref.8 Ref.9

Subcellular location

Cell inner membrane; Peripheral membrane protein. Cytoplasm. Note: Mainly cytoplasmic under aerobic conditions, and found in the inner membrane under anaerobic conditions. Ref.6

Sequence similarities

Belongs to the TorD/DmsD family. DmsD subfamily.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 204203Tat proofreading chaperone DmsD HAMAP-Rule MF_00940
PRO_0000211649

Experimental info

Mutagenesis72 – 754WQRL → HQRY: 1.5-fold increased binding to DmsA signal sequence. Ref.9
Sequence conflict71Missing AA sequence Ref.4

Secondary structure

........................... 204
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P69853 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: CB4273F4B6539D47

FASTA20423,345
        10         20         30         40         50         60 
MTHFSQQDNF SVAARVLGAL FYYAPESAEA APLVAVLTSD GWETQWPLPE ASLAPLVTAF 

        70         80         90        100        110        120 
QTQCEETHAQ AWQRLFVGPW ALPSPPWGSV WLDRESVLFG DSTLALRQWM REKGIQFEMK 

       130        140        150        160        170        180 
QNEPEDHFGS LLLMAAWLAE NGRQTECEEL LAWHLFPWST RFLDVFIEKA EHPFYRALGE 

       190        200 
LARLTLAQWQ SQLLIPVAVK PLFR 

« Hide

References

« Hide 'large scale' references
[1]"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map."
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. expand/collapse author list , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00096 Genomic DNA. Translation: AAC74663.2.
AP009048 Genomic DNA. Translation: BAA15315.1.
PIRA64915.
RefSeqNP_416108.2. NC_000913.3.
YP_489854.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP69853.
SMRP69853. Positions 1-204.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-47840N.
IntActP69853. 6 interactions.
MINTMINT-8046358.
STRING511145.b1591.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74663; AAC74663; b1591.
BAA15315; BAA15315; BAA15315.
GeneID12930123.
945987.
KEGGecj:Y75_p1567.
eco:b1591.
PATRIC32118484. VBIEscCol129921_1662.

Organism-specific databases

EchoBASEEB3608.
EcoGeneEG13847. dmsD.

Phylogenomic databases

eggNOGCOG3381.
HOGENOMHOG000120828.
OMAEDHIGLM.
OrthoDBEOG6FZ4BH.
PhylomeDBP69853.
ProtClustDBPRK11621.

Enzyme and pathway databases

BioCycEcoCyc:G6849-MONOMER.
ECOL316407:JW5262-MONOMER.

Gene expression databases

GenevestigatorP69853.

Family and domain databases

HAMAPMF_00940. DmsD_chaperone.
InterProIPR026269. DmsD-type.
IPR028611. DmsD_chaperone.
IPR020945. DMSO/NO3_reduct_chaperone.
[Graphical view]
PfamPF02613. Nitrate_red_del. 1 hit.
[Graphical view]
PIRSFPIRSF004690. DmsD. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP69853.
PROP69853.

Entry information

Entry nameDMSD_ECOLI
AccessionPrimary (citable) accession number: P69853
Secondary accession number(s): P76174, P77270
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene