ID DMSD_SALTY Reviewed; 204 AA.
AC Q8ZPK0;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 98.
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=STM1495;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS), AND SUBUNIT.
RX PubMed=18175314; DOI=10.1002/prot.21828;
RA Qiu Y., Zhang R., Binkowski T.A., Tereshko V., Joachimiak A.,
RA Kossiakoff A.;
RT "The 1.38 A crystal structure of DmsD protein from Salmonella typhimurium,
RT a proofreading chaperone on the Tat pathway.";
RL Proteins 71:525-533(2008).
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 -!- SUBUNIT: Monomer in solution. {ECO:0000269|PubMed:18175314}.
CC -!- SIMILARITY: Belongs to the TorD/DmsD family. DmsD subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00940}.
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DR EMBL; AE006468; AAL20414.1; -; Genomic_DNA.
DR RefSeq; NP_460455.1; NC_003197.2.
DR RefSeq; WP_000206561.1; NC_003197.2.
DR PDB; 1S9U; X-ray; 1.38 A; A=1-204.
DR PDBsum; 1S9U; -.
DR AlphaFoldDB; Q8ZPK0; -.
DR SMR; Q8ZPK0; -.
DR STRING; 99287.STM1495; -.
DR PaxDb; 99287-STM1495; -.
DR GeneID; 1253013; -.
DR KEGG; stm:STM1495; -.
DR PATRIC; fig|99287.12.peg.1580; -.
DR HOGENOM; CLU_077650_7_1_6; -.
DR OMA; AWHLLPW; -.
DR PhylomeDB; Q8ZPK0; -.
DR BioCyc; SENT99287:STM1495-MONOMER; -.
DR EvolutionaryTrace; Q8ZPK0; -.
DR Proteomes; UP000001014; Chromosome.
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; Chaperone; Reference proteome.
FT CHAIN 1..204
FT /note="Tat proofreading chaperone DmsD"
FT /id="PRO_0000211654"
FT HELIX 1..5
FT /evidence="ECO:0007829|PDB:1S9U"
FT TURN 6..8
FT /evidence="ECO:0007829|PDB:1S9U"
FT HELIX 9..22
FT /evidence="ECO:0007829|PDB:1S9U"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:1S9U"
FT HELIX 31..39
FT /evidence="ECO:0007829|PDB:1S9U"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:1S9U"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:1S9U"
FT HELIX 50..60
FT /evidence="ECO:0007829|PDB:1S9U"
FT HELIX 68..76
FT /evidence="ECO:0007829|PDB:1S9U"
FT HELIX 88..92
FT /evidence="ECO:0007829|PDB:1S9U"
FT HELIX 101..112
FT /evidence="ECO:0007829|PDB:1S9U"
FT HELIX 128..140
FT /evidence="ECO:0007829|PDB:1S9U"
FT HELIX 144..154
FT /evidence="ECO:0007829|PDB:1S9U"
FT HELIX 156..169
FT /evidence="ECO:0007829|PDB:1S9U"
FT HELIX 173..192
FT /evidence="ECO:0007829|PDB:1S9U"
SQ SEQUENCE 204 AA; 23481 MW; EFB2930376875EF1 CRC64;
MTTFLQRDDF AVTARVLGAL FYYSPESHET APLVQALLND DWQAQWPLDA EALAPVAAMF
KTHSEESLPQ AWQRLFIGPY ALPSPPWGSV WLDRESVLFG DSTLALRQWM RENGIQFEMQ
QNEPEDHFGS LLLLAAWLAE NDRHHECEQL LAWHLFPWSS RFLDVFIDHA GHPFYQALGQ
LARLTLAQWQ AQLIIPVAVK PLFR
//
