ID   DMSD_ECOL6              Reviewed;         204 AA.
AC   Q8CW16;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 94.
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}; OrderedLocusNames=c1982;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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}.
CC   -!- SIMILARITY: Belongs to the TorD/DmsD family. DmsD subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00940}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN80442.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE014075; AAN80442.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000148699.1; NC_004431.1.
DR   AlphaFoldDB; Q8CW16; -.
DR   BMRB; Q8CW16; -.
DR   SMR; Q8CW16; -.
DR   STRING; 199310.c1982; -.
DR   EnsemblBacteria; AAN80442; AAN80442; c1982.
DR   KEGG; ecc:c1982; -.
DR   eggNOG; COG3381; Bacteria.
DR   HOGENOM; CLU_077650_7_1_6; -.
DR   OMA; AWHLLPW; -.
DR   Proteomes; UP000001410; Chromosome.
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   3: Inferred from homology;
KW   Chaperone.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..204
FT                   /note="Tat proofreading chaperone DmsD"
FT                   /id="PRO_0000211651"
SQ   SEQUENCE   204 AA;  23398 MW;  C3777B42EEF16649 CRC64;
     MTHFSQQDNF SVAARVLGAL FYYAPESAEA APLVAVLTRD GWETQWPLPE ASLAPLVTAF
     QTQSEETHAQ AWQRLFVGPW ALPSPPWGSV WLDRESVLFG DSTLALRQWM REKGIQFEMK
     QNEPEDHFGS LLLMAAWLAE NGRQTECEEL LAWHLFPWST RFLDVFIEKA EHPFYRALGE
     LARLTLAQWQ SQLLIPVAVK PLFR