ID   DMSD_SALTI              Reviewed;         204 AA.
AC   Q8Z6Y5; Q7C9V2;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
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};
GN   OrderedLocusNames=STY1569, t1416;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
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}.
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DR   EMBL; AL513382; CAD01818.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO69060.1; -; Genomic_DNA.
DR   RefSeq; NP_455984.1; NC_003198.1.
DR   RefSeq; WP_000206559.1; NZ_WSUR01000006.1.
DR   AlphaFoldDB; Q8Z6Y5; -.
DR   SMR; Q8Z6Y5; -.
DR   STRING; 220341.16502662; -.
DR   EnsemblBacteria; AAO69060; AAO69060; t1416.
DR   KEGG; stt:t1416; -.
DR   KEGG; sty:STY1569; -.
DR   PATRIC; fig|220341.7.peg.1578; -.
DR   eggNOG; COG3381; Bacteria.
DR   HOGENOM; CLU_077650_7_1_6; -.
DR   OMA; AWHLLPW; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; 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   CHAIN           1..204
FT                   /note="Tat proofreading chaperone DmsD"
FT                   /id="PRO_0000211653"
SQ   SEQUENCE   204 AA;  23417 MW;  EFB0571FAF625E17 CRC64;
     MTTFLQRDDF AVTARVLGAL FYYSPESHET APLVQALLND DWQAQWPLDA EALAPVAAMF
     KTHSEESLPQ AWQRLFIGPY ALPSPPWGSV WLDRESVLFG DSTLALRQWM RENGIQFEMQ
     QNEPEDHFGA LLLLAAWLAE NGRHHECEQL LAWHLFPWSP RFLDVFIDHA GHPFYQALGQ
     LARLTLAQWQ AQLIIPVAVK PLFR