P69853 (DMSD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	204 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cell inner membrane Cell membrane Cytoplasm Membrane
Molecular function	Chaperone
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular_component	cytoplasm Inferred from mutant phenotype Ref.6. Source: EcoCyc extrinsic to internal side of plasma membrane Inferred from mutant phenotype Ref.6. Source: EcoCyc
Molecular_function	signal sequence binding Inferred from physical interaction Ref.4PubMed 19151138. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
dmsA	P18775	6	EBI-4406374,EBI-4411104
ynfE	P77374	3	EBI-4406374,EBI-556186
ynfF	P77783	2	EBI-4406374,EBI-6406285

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.4

Chain

2 – 204

203

Tat proofreading chaperone DmsD HAMAP-Rule MF_00940

PRO_0000211649

Experimental info

Mutagenesis

72 – 75

4

WQRL → HQRY: 1.5-fold increased binding to DmsA signal sequence. Ref.9

Sequence conflict

7

1

Missing AA sequence Ref.4

Secondary structure

1

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204

Helix Strand Turn

Details...

Helix

4 – 6

3

Helix

10 – 22

13

Turn

28 – 30

3

Helix

31 – 37

7

Helix

42 – 45

4

Beta strand

46 – 48

3

Helix

50 – 60

11

Helix

68 – 76

9

Helix

88 – 92

5

Helix

101 – 112

12

Helix

128 – 140

13

Helix

144 – 154

11

Helix

156 – 169

14

Helix

173 – 191

19

Sequences

	Sequence		Length	Mass (Da)
	P69853 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: CB4273F4B6539D47	FASTA	204	23,345
	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

References

	« Hide 'large scale' referencesShow '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. , 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 277:1453-1474(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 SIGNAL PEPTIDE; 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.

PIR

A64915.

RefSeq

NP_416108.2. NC_000913.2.
YP_489854.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P69853.

SMR

P69853. Positions 1-204.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-47840N.

IntAct

P69853. 6 interactions.

STRING

511145.b1591.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74663; AAC74663; b1591.
BAA15315; BAA15315; BAA15315.

GeneID

12930123.
945987.

KEGG

ecj:Y75_p1567.
eco:b1591.

PATRIC

32118484. VBIEscCol129921_1662.

Organism-specific databases

EchoBASE

EB3608.

EcoGene

EG13847. dmsD.

Phylogenomic databases

eggNOG

COG3381.

HOGENOM

HOG000120828.

OMA

EDHIGLM.

ProtClustDB

PRK11621.

Enzyme and pathway databases

BioCyc

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

Gene expression databases

Genevestigator

P69853.

Family and domain databases

HAMAP

MF_00940. DmsD_chaperone.

InterPro

IPR026269. DmsD-type.
IPR020945. DMSO/NO3_reduct_chaperone.
[Graphical view]

Pfam

PF02613. Nitrate_red_del. 1 hit.
[Graphical view]

PIRSF

PIRSF004690. DmsD. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P69853.

Entry information

Entry name

DMSD_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program