ID Q9X6B3_YERPE Unreviewed; 236 AA.
AC Q9X6B3; A0A0H2W2S8; A0A1U8QW19; A0A2U2H1Q7; A0A384KPC6; Q74XN7; Q7CKA4;
DT 01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 150.
DE RecName: Full=Tat proofreading chaperone DmsD {ECO:0000256|HAMAP-Rule:MF_00940};
DE AltName: Full=DMSO reductase maturation protein {ECO:0000256|HAMAP-Rule:MF_00940};
DE AltName: Full=Twin-arginine leader-binding protein DmsD {ECO:0000256|HAMAP-Rule:MF_00940};
GN Name=dmsD {ECO:0000256|HAMAP-Rule:MF_00940};
GN OrderedLocusNames=YPO3322 {ECO:0000313|EMBL:CAL21913.1};
OS Yersinia pestis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632 {ECO:0000313|EMBL:CAL21913.1, ECO:0000313|Proteomes:UP000000815};
RN [1] {ECO:0000313|EMBL:CAL21913.1, ECO:0000313|Proteomes:UP000000815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis {ECO:0000313|Proteomes:UP000000815};
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Leather S., Karlyshev A.V., Moule S.,
RA Oyston P.C.F., Quail M., Rutherford K., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
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:0000256|HAMAP-
CC Rule:MF_00940}.
CC -!- SIMILARITY: Belongs to the TorD/DmsD family. DmsD subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00940}.
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DR EMBL; AL590842; CAL21913.1; -; Genomic_DNA.
DR PIR; AF0403; AF0403.
DR RefSeq; WP_002209430.1; NZ_WUCM01000060.1.
DR RefSeq; YP_002348218.1; NC_003143.1.
DR STRING; 214092.YPO3322; -.
DR PaxDb; 214092-YPO3322; -.
DR DNASU; 1145814; -.
DR GeneID; 57975387; -.
DR KEGG; ype:YPO3322; -.
DR KEGG; ypj:CH55_1902; -.
DR KEGG; ypl:CH46_1773; -.
DR KEGG; ypv:BZ15_201; -.
DR KEGG; ypw:CH59_2727; -.
DR PATRIC; fig|1028802.3.peg.308; -.
DR eggNOG; COG3381; Bacteria.
DR HOGENOM; CLU_077650_7_1_6; -.
DR OMA; AWHLLPW; -.
DR OrthoDB; 3174863at2; -.
DR Proteomes; UP000000815; 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 3: Inferred from homology;
KW Chaperone {ECO:0000256|HAMAP-Rule:MF_00940};
KW Reference proteome {ECO:0000313|Proteomes:UP000000815}.
SQ SEQUENCE 236 AA; 26766 MW; 77467CD405EDE9B9 CRC64;
MIKTDMTYQD IVYKDTVYQD SVYQKIGLTG RVLGALFYCE PDSAECRDIV VQLRNGTWAA
EWPYGGADEL MPIATLLAAA QSDQYQSIAH QSAAAPLAET LEEAWQRLFI GPYALPAPPW
GSVYLDKDMV LFGDSTLKLR NWMQQRHVEV TLKQQEPEDH FGLLMMMAAW LAEHQPVDLP
VLLADHLLPW SYRYLALLQS DAGHPFYQGL AQLTTLTLAH WQHELQVTPA GVELYR
//
