ID   DMSD_SALPA              Reviewed;         204 AA.
AC   Q5PHH8;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 69.
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=SPA1359;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV77304.1; -; Genomic_DNA.
DR   RefSeq; WP_000206563.1; NC_006511.1.
DR   AlphaFoldDB; Q5PHH8; -.
DR   SMR; Q5PHH8; -.
DR   EnsemblBacteria; AAV77304; AAV77304; SPA1359.
DR   KEGG; spt:SPA1359; -.
DR   HOGENOM; CLU_077650_7_1_6; -.
DR   OMA; AWHLLPW; -.
DR   Proteomes; UP000008185; 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_0000211652"
SQ   SEQUENCE   204 AA;  23451 MW;  F9C1281559300DF2 CRC64;
     MTTFLQRDDF AVTARVLGAL FYYSPESHET APLVQALLND DWQAQWPLDA EALAPVAVMF
     KTHSEESLPQ AWQRLFIGPY ALPSPPWGSV WLDRESVLFG DSTLALRQWM RENGIQFEMQ
     QNEPEDHFGS LLLLAAWLAE NGRHHECEQL LAWHLFPWSS RFLDVFIDHA GHPFYQALGQ
     LARLTLAQWQ AQLIIPVAVK PLFR