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Tat proofreading chaperone DmsD (DMSO reductase maturation protein) (Twin-arginine leader-binding protein DmsD)

 DMSD_SALTY              Reviewed;         204 AA.
Q8ZPK0;
07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
28-FEB-2018, entry version 76.
RecName: Full=Tat proofreading chaperone DmsD {ECO:0000255|HAMAP-Rule:MF_00940};
AltName: Full=DMSO reductase maturation protein {ECO:0000255|HAMAP-Rule:MF_00940};
AltName: Full=Twin-arginine leader-binding protein DmsD {ECO:0000255|HAMAP-Rule:MF_00940};
Name=dmsD {ECO:0000255|HAMAP-Rule:MF_00940};
OrderedLocusNames=STM1495;
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Salmonella.
NCBI_TaxID=99287;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=LT2 / SGSC1412 / ATCC 700720;
PubMed=11677609; DOI=10.1038/35101614;
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M.,
Waterston R., Wilson R.K.;
"Complete genome sequence of Salmonella enterica serovar Typhimurium
LT2.";
Nature 413:852-856(2001).
[2]
X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS), AND SUBUNIT.
PubMed=18175314; DOI=10.1002/prot.21828;
Qiu Y., Zhang R., Binkowski T.A., Tereshko V., Joachimiak A.,
Kossiakoff A.;
"The 1.38 A crystal structure of DmsD protein from Salmonella
typhimurium, a proofreading chaperone on the Tat pathway.";
Proteins 71:525-533(2008).
-!- FUNCTION: Required for biogenesis/assembly of DMSO reductase, but
not for the interaction of the DmsA signal peptide with the Tat
system. May be part of a chaperone cascade complex that
facilitates a folding-maturation pathway for the substrate
protein. {ECO:0000255|HAMAP-Rule:MF_00940}.
-!- SUBUNIT: Monomer in solution. {ECO:0000269|PubMed:18175314}.
-!- SIMILARITY: Belongs to the TorD/DmsD family. DmsD subfamily.
{ECO:0000255|HAMAP-Rule:MF_00940}.
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EMBL; AE006468; AAL20414.1; -; Genomic_DNA.
RefSeq; NP_460455.1; NC_003197.2.
RefSeq; WP_000206561.1; NC_003197.2.
PDB; 1S9U; X-ray; 1.38 A; A=1-204.
PDBsum; 1S9U; -.
ProteinModelPortal; Q8ZPK0; -.
SMR; Q8ZPK0; -.
STRING; 99287.STM1495; -.
PaxDb; Q8ZPK0; -.
EnsemblBacteria; AAL20414; AAL20414; STM1495.
GeneID; 1253013; -.
KEGG; stm:STM1495; -.
PATRIC; fig|99287.12.peg.1580; -.
eggNOG; ENOG4108NEM; Bacteria.
eggNOG; COG3381; LUCA.
HOGENOM; HOG000120828; -.
OMA; AWHLLPW; -.
PhylomeDB; Q8ZPK0; -.
BioCyc; SENT99287:G1FZD-1512-MONOMER; -.
EvolutionaryTrace; Q8ZPK0; -.
Proteomes; UP000001014; Chromosome.
GO; GO:0005048; F:signal sequence binding; IEA:InterPro.
HAMAP; MF_00940; DmsD_chaperone; 1.
InterPro; IPR026269; DmsD-type.
InterPro; IPR028611; DmsD_chaperone.
InterPro; IPR020945; DMSO/NO3_reduct_chaperone.
InterPro; IPR036411; TorD-like_sf.
Pfam; PF02613; Nitrate_red_del; 1.
PIRSF; PIRSF004690; DmsD; 1.
SUPFAM; SSF89155; SSF89155; 1.
1: Evidence at protein level;
3D-structure; Chaperone; Complete proteome; Reference proteome.
CHAIN 1 204 Tat proofreading chaperone DmsD.
/FTId=PRO_0000211654.
HELIX 1 5 {ECO:0000244|PDB:1S9U}.
TURN 6 8 {ECO:0000244|PDB:1S9U}.
HELIX 9 22 {ECO:0000244|PDB:1S9U}.
TURN 28 30 {ECO:0000244|PDB:1S9U}.
HELIX 31 39 {ECO:0000244|PDB:1S9U}.
HELIX 43 45 {ECO:0000244|PDB:1S9U}.
STRAND 46 48 {ECO:0000244|PDB:1S9U}.
HELIX 50 60 {ECO:0000244|PDB:1S9U}.
HELIX 68 76 {ECO:0000244|PDB:1S9U}.
HELIX 88 92 {ECO:0000244|PDB:1S9U}.
HELIX 101 112 {ECO:0000244|PDB:1S9U}.
HELIX 128 140 {ECO:0000244|PDB:1S9U}.
HELIX 144 154 {ECO:0000244|PDB:1S9U}.
HELIX 156 169 {ECO:0000244|PDB:1S9U}.
HELIX 173 192 {ECO:0000244|PDB:1S9U}.
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


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