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   24-JAN-2024, entry version 130.
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; Pseudomonadota; 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; 511145-b1591; -.
DR   EnsemblBacteria; AAC74663; AAC74663; b1591.
DR   GeneID; 75204434; -.
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   OrthoDB; 3174863at2; -.
DR   PhylomeDB; P69853; -.
DR   BioCyc; EcoCyc:G6849-MONOMER; -.
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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005048; F:signal sequence binding; IEA:InterPro.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.3480.10; TorD-like; 1.
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   PANTHER; PTHR34227; CHAPERONE PROTEIN YCDY; 1.
DR   PANTHER; PTHR34227:SF6; TAT PROOFREADING CHAPERONE DMSD; 1.
DR   Pfam; PF02613; Nitrate_red_del; 1.
DR   PIRSF; PIRSF004690; DmsD; 1.
DR   SUPFAM; SSF89155; TorD-like; 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
//