DMSD_ECOLI
ID DMSD_ECOLI Reviewed; 204 AA.
AC P69853; P76174; P77270;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Tat proofreading chaperone DmsD {ECO:0000255|HAMAP-Rule:MF_00940};
DE AltName: Full=DMSO reductase maturation protein {ECO:0000255|HAMAP-Rule:MF_00940};
DE AltName: Full=Twin-arginine leader-binding protein DmsD {ECO:0000255|HAMAP-Rule:MF_00940};
GN Name=dmsD {ECO:0000255|HAMAP-Rule:MF_00940}; Synonyms=ynfI;
GN OrderedLocusNames=b1591, JW5262;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP PROTEIN SEQUENCE OF 2-11, FUNCTION, AND INTERACTION WITH SIGNAL PEPTIDES OF
RP DMSA AND TORA.
RX PubMed=11309116; DOI=10.1046/j.1365-2958.2001.02391.x;
RA Oresnik I.J., Ladner C.L., Turner R.J.;
RT "Identification of a twin-arginine leader-binding protein.";
RL Mol. Microbiol. 40:323-331(2001).
RN [5]
RP FUNCTION.
RX PubMed=12527378; DOI=10.1016/s0014-5793(02)03839-5;
RA Ray N., Oates J., Turner R.J., Robinson C.;
RT "DmsD is required for the biogenesis of DMSO reductase in Escherichia coli
RT but not for the interaction of the DmsA signal peptide with the Tat
RT apparatus.";
RL FEBS Lett. 534:156-160(2003).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TATB AND TATC.
RX PubMed=12813051; DOI=10.1074/jbc.m301076200;
RA Papish A.L., Ladner C.L., Turner R.J.;
RT "The twin-arginine leader-binding protein, DmsD, interacts with the TatB
RT and TatC subunits of the Escherichia coli twin-arginine translocase.";
RL J. Biol. Chem. 278:32501-32506(2003).
RN [7]
RP SUBUNIT.
RX PubMed=14766221; DOI=10.1016/j.bbrc.2004.01.070;
RA Sarfo K.J., Winstone T.L., Papish A.L., Howell J.M., Kadir H., Vogel H.J.,
RA Turner R.J.;
RT "Folding forms of Escherichia coli DmsD, a twin-arginine leader binding
RT protein.";
RL Biochem. Biophys. Res. Commun. 315:397-403(2004).
RN [8]
RP FUNCTION, AND INTERACTION WITH CHAPERONES AND MOCO BIOSYNTHESIS PROTEINS.
RX PubMed=20153451; DOI=10.1016/j.bbapap.2010.01.022;
RA Li H., Chang L., Howell J.M., Turner R.J.;
RT "DmsD, a Tat system specific chaperone, interacts with other general
RT chaperones and proteins involved in the molybdenum cofactor biosynthesis.";
RL Biochim. Biophys. Acta 1804:1301-1309(2010).
RN [9]
RP INTERACTION WITH DMSA; TATB AND TATC, AND MUTAGENESIS OF 72-TRP--LEU-75.
RX PubMed=20169075; DOI=10.1371/journal.pone.0009225;
RA Kostecki J.S., Li H., Turner R.J., DeLisa M.P.;
RT "Visualizing interactions along the Escherichia coli twin-arginine
RT translocation pathway using protein fragment complementation.";
RL PLoS ONE 5:E9225-E9225(2010).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS).
RX PubMed=19652330; DOI=10.1107/s1744309109023811;
RA Ramasamy S.K., Clemons W.M. Jr.;
RT "Structure of the twin-arginine signal-binding protein DmsD from
RT Escherichia coli.";
RL Acta Crystallogr. F 65:746-750(2009).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS).
RX PubMed=19361518; DOI=10.1016/j.jmb.2009.03.069;
RA Stevens C.M., Winstone T.M., Turner R.J., Paetzel M.;
RT "Structural analysis of a monomeric form of the twin-arginine leader
RT peptide binding chaperone Escherichia coli DmsD.";
RL J. Mol. Biol. 389:124-133(2009).
CC -!- FUNCTION: Required for biogenesis/assembly of DMSO reductase, but not
CC for the interaction of the DmsA signal peptide with the Tat system. May
CC be part of a chaperone cascade complex that facilitates a folding-
CC maturation pathway for the substrate protein. {ECO:0000255|HAMAP-
CC Rule:MF_00940, ECO:0000269|PubMed:11309116,
CC ECO:0000269|PubMed:12527378, ECO:0000269|PubMed:12813051,
CC ECO:0000269|PubMed:20153451}.
CC -!- SUBUNIT: Monomer and homodimer. Binds to the twin-arginine signal
CC peptide of DmsA and TorA (PubMed:11309116), although the latter binding
CC is controversial (PubMed:20169075). Interacts with the TatB and TatC
CC subunits of the Tat translocase complex. Interacts also with other
CC general chaperones, such as GroEL, and proteins involved in the
CC molybdenum cofactor biosynthesis. {ECO:0000269|PubMed:11309116,
CC ECO:0000269|PubMed:12813051, ECO:0000269|PubMed:14766221,
CC ECO:0000269|PubMed:20153451, ECO:0000269|PubMed:20169075}.
CC -!- INTERACTION:
CC P69853; P18775: dmsA; NbExp=8; IntAct=EBI-4406374, EBI-4411104;
CC P69853; P77374: ynfE; NbExp=3; IntAct=EBI-4406374, EBI-556186;
CC P69853; P77783: ynfF; NbExp=3; IntAct=EBI-4406374, EBI-6406285;
CC P69853; C5A1D5: groEL; Xeno; NbExp=5; IntAct=EBI-4406374, EBI-4406290;
CC P69853; C4ZYN1: grpE; Xeno; NbExp=4; IntAct=EBI-4406374, EBI-4407105;
CC P69853; C4ZTJ3: tig; Xeno; NbExp=3; IntAct=EBI-4406374, EBI-4407188;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:12813051}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12813051}. Cytoplasm {ECO:0000269|PubMed:12813051}.
CC Note=Mainly cytoplasmic under aerobic conditions, and found in the
CC inner membrane under anaerobic conditions.
CC -!- SIMILARITY: Belongs to the TorD/DmsD family. DmsD subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00940}.
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DR EMBL; U00096; AAC74663.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA15315.1; -; Genomic_DNA.
DR PIR; A64915; A64915.
DR RefSeq; NP_416108.2; NC_000913.3.
DR RefSeq; WP_000148710.1; NZ_STEB01000003.1.
DR PDB; 3CW0; X-ray; 2.40 A; A/B/C/D=1-204.
DR PDB; 3EFP; X-ray; 2.01 A; A/B=1-204.
DR PDB; 3U41; X-ray; 2.50 A; A/B/C/D/E/F/G/H=1-204.
DR PDBsum; 3CW0; -.
DR PDBsum; 3EFP; -.
DR PDBsum; 3U41; -.
DR AlphaFoldDB; P69853; -.
DR BMRB; P69853; -.
DR SMR; P69853; -.
DR BioGRID; 4259117; 3.
DR DIP; DIP-47840N; -.
DR IntAct; P69853; 11.
DR MINT; P69853; -.
DR STRING; 511145.b1591; -.
DR jPOST; P69853; -.
DR PaxDb; P69853; -.
DR PRIDE; P69853; -.
DR EnsemblBacteria; AAC74663; AAC74663; b1591.
DR EnsemblBacteria; BAA15315; BAA15315; BAA15315.
DR GeneID; 66674519; -.
DR GeneID; 945987; -.
DR KEGG; ecj:JW5262; -.
DR KEGG; eco:b1591; -.
DR PATRIC; fig|1411691.4.peg.671; -.
DR EchoBASE; EB3608; -.
DR eggNOG; COG3381; Bacteria.
DR HOGENOM; CLU_077650_7_1_6; -.
DR InParanoid; P69853; -.
DR OMA; AWHLLPW; -.
DR PhylomeDB; P69853; -.
DR BioCyc; EcoCyc:G6849-MON; -.
DR EvolutionaryTrace; P69853; -.
DR PRO; PR:P69853; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IMP:EcoCyc.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IMP:EcoCyc.
DR GO; GO:0005048; F:signal sequence binding; IEA:InterPro.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00940; DmsD_chaperone; 1.
DR InterPro; IPR026269; DmsD-type.
DR InterPro; IPR028611; DmsD_chaperone.
DR InterPro; IPR020945; DMSO/NO3_reduct_chaperone.
DR InterPro; IPR036411; TorD-like_sf.
DR Pfam; PF02613; Nitrate_red_del; 1.
DR PIRSF; PIRSF004690; DmsD; 1.
DR SUPFAM; SSF89155; SSF89155; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Chaperone; Cytoplasm;
KW Direct protein sequencing; Membrane; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11309116"
FT CHAIN 2..204
FT /note="Tat proofreading chaperone DmsD"
FT /id="PRO_0000211649"
FT MUTAGEN 72..75
FT /note="WQRL->HQRY: 1.5-fold increased binding to DmsA
FT signal sequence."
FT /evidence="ECO:0000269|PubMed:20169075"
FT CONFLICT 7
FT /note="Missing (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:3EFP"
FT HELIX 10..22
FT /evidence="ECO:0007829|PDB:3EFP"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:3EFP"
FT HELIX 31..37
FT /evidence="ECO:0007829|PDB:3EFP"
FT HELIX 42..45
FT /evidence="ECO:0007829|PDB:3EFP"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:3EFP"
FT HELIX 50..60
FT /evidence="ECO:0007829|PDB:3EFP"
FT HELIX 68..76
FT /evidence="ECO:0007829|PDB:3EFP"
FT HELIX 88..92
FT /evidence="ECO:0007829|PDB:3EFP"
FT HELIX 101..112
FT /evidence="ECO:0007829|PDB:3EFP"
FT HELIX 128..140
FT /evidence="ECO:0007829|PDB:3EFP"
FT HELIX 144..154
FT /evidence="ECO:0007829|PDB:3EFP"
FT HELIX 156..169
FT /evidence="ECO:0007829|PDB:3EFP"
FT HELIX 173..191
FT /evidence="ECO:0007829|PDB:3EFP"
SQ 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
