DMSD_SHIFL
ID DMSD_SHIFL Reviewed; 204 AA.
AC P69855; P76174; P77270;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 89.
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=SF1612, S1744;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(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; AE005674; AAN43196.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP17084.1; -; Genomic_DNA.
DR RefSeq; NP_707489.2; NC_004337.2.
DR RefSeq; WP_000148710.1; NZ_WPGW01000024.1.
DR AlphaFoldDB; P69855; -.
DR BMRB; P69855; -.
DR SMR; P69855; -.
DR STRING; 198214.SF1612; -.
DR EnsemblBacteria; AAN43196; AAN43196; SF1612.
DR EnsemblBacteria; AAP17084; AAP17084; S1744.
DR GeneID; 1024778; -.
DR GeneID; 66674519; -.
DR KEGG; sfl:SF1612; -.
DR KEGG; sfx:S1744; -.
DR PATRIC; fig|198214.7.peg.1905; -.
DR HOGENOM; CLU_077650_7_1_6; -.
DR OMA; AWHLLPW; -.
DR OrthoDB; 1995553at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..204
FT /note="Tat proofreading chaperone DmsD"
FT /id="PRO_0000211655"
SQ SEQUENCE 204 AA; 23345 MW; CB4273F4B6539D47 CRC64;
MTHFSQQDNF SVAARVLGAL FYYAPESAEA APLVAVLTSD GWETQWPLPE ASLAPLVTAF
QTQCEETHAQ AWQRLFVGPW ALPSPPWGSV WLDRESVLFG DSTLALRQWM REKGIQFEMK
QNEPEDHFGS LLLMAAWLAE NGRQTECEEL LAWHLFPWST RFLDVFIEKA EHPFYRALGE
LARLTLAQWQ SQLLIPVAVK PLFR