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Tat proofreading chaperone DmsD (DMSO reductase maturation protein) (Twin-arginine leader-binding protein DmsD)

 DMSD_ECOLI              Reviewed;         204 AA.
P69853; P76174; P77270;
07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
10-OCT-2018, entry version 100.
RecName: Full=Tat proofreading chaperone DmsD {ECO:0000255|HAMAP-Rule:MF_00940};
AltName: Full=DMSO reductase maturation protein {ECO:0000255|HAMAP-Rule:MF_00940};
AltName: Full=Twin-arginine leader-binding protein DmsD {ECO:0000255|HAMAP-Rule:MF_00940};
Name=dmsD {ECO:0000255|HAMAP-Rule:MF_00940}; Synonyms=ynfI;
OrderedLocusNames=b1591, JW5262;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9097039; DOI=10.1093/dnares/3.6.363;
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.;
"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.";
DNA Res. 3:363-377(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
PROTEIN SEQUENCE OF 2-11, FUNCTION, AND INTERACTION WITH SIGNAL
PEPTIDES OF DMSA AND TORA.
PubMed=11309116; DOI=10.1046/j.1365-2958.2001.02391.x;
Oresnik I.J., Ladner C.L., Turner R.J.;
"Identification of a twin-arginine leader-binding protein.";
Mol. Microbiol. 40:323-331(2001).
[5]
FUNCTION.
PubMed=12527378; DOI=10.1016/S0014-5793(02)03839-5;
Ray N., Oates J., Turner R.J., Robinson C.;
"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.";
FEBS Lett. 534:156-160(2003).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TATB AND TATC.
PubMed=12813051; DOI=10.1074/jbc.M301076200;
Papish A.L., Ladner C.L., Turner R.J.;
"The twin-arginine leader-binding protein, DmsD, interacts with the
TatB and TatC subunits of the Escherichia coli twin-arginine
translocase.";
J. Biol. Chem. 278:32501-32506(2003).
[7]
SUBUNIT.
PubMed=14766221; DOI=10.1016/j.bbrc.2004.01.070;
Sarfo K.J., Winstone T.L., Papish A.L., Howell J.M., Kadir H.,
Vogel H.J., Turner R.J.;
"Folding forms of Escherichia coli DmsD, a twin-arginine leader
binding protein.";
Biochem. Biophys. Res. Commun. 315:397-403(2004).
[8]
FUNCTION, AND INTERACTION WITH CHAPERONES AND MOCO BIOSYNTHESIS
PROTEINS.
PubMed=20153451; DOI=10.1016/j.bbapap.2010.01.022;
Li H., Chang L., Howell J.M., Turner R.J.;
"DmsD, a Tat system specific chaperone, interacts with other general
chaperones and proteins involved in the molybdenum cofactor
biosynthesis.";
Biochim. Biophys. Acta 1804:1301-1309(2010).
[9]
INTERACTION WITH DMSA; TATB AND TATC, AND MUTAGENESIS OF
72-TRP--LEU-75.
PubMed=20169075; DOI=10.1371/journal.pone.0009225;
Kostecki J.S., Li H., Turner R.J., DeLisa M.P.;
"Visualizing interactions along the Escherichia coli twin-arginine
translocation pathway using protein fragment complementation.";
PLoS ONE 5:E9225-E9225(2010).
[10]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS).
PubMed=19652330; DOI=10.1107/S1744309109023811;
Ramasamy S.K., Clemons W.M. Jr.;
"Structure of the twin-arginine signal-binding protein DmsD from
Escherichia coli.";
Acta Crystallogr. F 65:746-750(2009).
[11]
X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS).
PubMed=19361518; DOI=10.1016/j.jmb.2009.03.069;
Stevens C.M., Winstone T.M., Turner R.J., Paetzel M.;
"Structural analysis of a monomeric form of the twin-arginine leader
peptide binding chaperone Escherichia coli DmsD.";
J. Mol. Biol. 389:124-133(2009).
-!- 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. {ECO:0000255|HAMAP-Rule:MF_00940,
ECO:0000269|PubMed:11309116, ECO:0000269|PubMed:12527378,
ECO:0000269|PubMed:12813051, ECO:0000269|PubMed:20153451}.
-!- SUBUNIT: 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.
{ECO:0000269|PubMed:11309116, ECO:0000269|PubMed:12813051,
ECO:0000269|PubMed:14766221, ECO:0000269|PubMed:20153451,
ECO:0000269|PubMed:20169075}.
-!- INTERACTION:
P18775:dmsA; NbExp=8; IntAct=EBI-4406374, EBI-4411104;
C5A1D5:groL (xeno); NbExp=5; IntAct=EBI-4406374, EBI-4406290;
C4ZYN1:grpE (xeno); NbExp=4; IntAct=EBI-4406374, EBI-4407105;
C4ZTJ3:tig (xeno); NbExp=3; IntAct=EBI-4406374, EBI-4407188;
P77374:ynfE; NbExp=3; IntAct=EBI-4406374, EBI-556186;
P77783:ynfF; NbExp=3; IntAct=EBI-4406374, EBI-6406285;
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000269|PubMed:12813051}; Peripheral membrane protein
{ECO:0000269|PubMed:12813051}. Cytoplasm
{ECO:0000269|PubMed:12813051}. Note=Mainly cytoplasmic under
aerobic conditions, and found in the inner membrane under
anaerobic conditions.
-!- SIMILARITY: Belongs to the TorD/DmsD family. DmsD subfamily.
{ECO:0000255|HAMAP-Rule:MF_00940}.
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EMBL; U00096; AAC74663.2; -; Genomic_DNA.
EMBL; AP009048; BAA15315.1; -; Genomic_DNA.
PIR; A64915; A64915.
RefSeq; NP_416108.2; NC_000913.3.
RefSeq; WP_000148710.1; NZ_LN832404.1.
PDB; 3CW0; X-ray; 2.40 A; A/B/C/D=1-204.
PDB; 3EFP; X-ray; 2.01 A; A/B=1-204.
PDB; 3U41; X-ray; 2.50 A; A/B/C/D/E/F/G/H=1-204.
PDBsum; 3CW0; -.
PDBsum; 3EFP; -.
PDBsum; 3U41; -.
ProteinModelPortal; P69853; -.
SMR; P69853; -.
BioGrid; 4259117; 3.
DIP; DIP-47840N; -.
IntAct; P69853; 11.
MINT; P69853; -.
STRING; 316385.ECDH10B_1724; -.
PaxDb; P69853; -.
PRIDE; P69853; -.
EnsemblBacteria; AAC74663; AAC74663; b1591.
EnsemblBacteria; BAA15315; BAA15315; BAA15315.
GeneID; 945987; -.
KEGG; ecj:JW5262; -.
KEGG; eco:b1591; -.
PATRIC; fig|1411691.4.peg.671; -.
EchoBASE; EB3608; -.
EcoGene; EG13847; dmsD.
eggNOG; ENOG4108NEM; Bacteria.
eggNOG; COG3381; LUCA.
HOGENOM; HOG000120828; -.
InParanoid; P69853; -.
OMA; AWHLLPW; -.
PhylomeDB; P69853; -.
BioCyc; EcoCyc:G6849-MONOMER; -.
EvolutionaryTrace; P69853; -.
PRO; PR:P69853; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005737; C:cytoplasm; IMP:EcoCyc.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IMP:EcoCyc.
GO; GO:0005048; F:signal sequence binding; IEA:InterPro.
GO; GO:0061077; P:chaperone-mediated protein folding; IEA:UniProtKB-UniRule.
HAMAP; MF_00940; DmsD_chaperone; 1.
InterPro; IPR026269; DmsD-type.
InterPro; IPR028611; DmsD_chaperone.
InterPro; IPR020945; DMSO/NO3_reduct_chaperone.
InterPro; IPR036411; TorD-like_sf.
Pfam; PF02613; Nitrate_red_del; 1.
PIRSF; PIRSF004690; DmsD; 1.
SUPFAM; SSF89155; SSF89155; 1.
1: Evidence at protein level;
3D-structure; Cell inner membrane; Cell membrane; Chaperone;
Complete proteome; Cytoplasm; Direct protein sequencing; Membrane;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:11309116}.
CHAIN 2 204 Tat proofreading chaperone DmsD.
/FTId=PRO_0000211649.
MUTAGEN 72 75 WQRL->HQRY: 1.5-fold increased binding to
DmsA signal sequence.
{ECO:0000269|PubMed:20169075}.
CONFLICT 7 7 Missing (in Ref. 4; AA sequence).
{ECO:0000305}.
HELIX 4 6 {ECO:0000244|PDB:3EFP}.
HELIX 10 22 {ECO:0000244|PDB:3EFP}.
TURN 28 30 {ECO:0000244|PDB:3EFP}.
HELIX 31 37 {ECO:0000244|PDB:3EFP}.
HELIX 42 45 {ECO:0000244|PDB:3EFP}.
STRAND 46 48 {ECO:0000244|PDB:3EFP}.
HELIX 50 60 {ECO:0000244|PDB:3EFP}.
HELIX 68 76 {ECO:0000244|PDB:3EFP}.
HELIX 88 92 {ECO:0000244|PDB:3EFP}.
HELIX 101 112 {ECO:0000244|PDB:3EFP}.
HELIX 128 140 {ECO:0000244|PDB:3EFP}.
HELIX 144 154 {ECO:0000244|PDB:3EFP}.
HELIX 156 169 {ECO:0000244|PDB:3EFP}.
HELIX 173 191 {ECO:0000244|PDB:3EFP}.
SEQUENCE 204 AA; 23345 MW; CB4273F4B6539D47 CRC64;
MTHFSQQDNF SVAARVLGAL FYYAPESAEA APLVAVLTSD GWETQWPLPE ASLAPLVTAF
QTQCEETHAQ AWQRLFVGPW ALPSPPWGSV WLDRESVLFG DSTLALRQWM REKGIQFEMK
QNEPEDHFGS LLLMAAWLAE NGRQTECEEL LAWHLFPWST RFLDVFIEKA EHPFYRALGE
LARLTLAQWQ SQLLIPVAVK PLFR


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