ID B2U1Q1_SHIB3 Unreviewed; 204 AA.
AC B2U1Q1;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 62.
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 ECO:0000313|EMBL:ACD06379.1};
GN OrderedLocusNames=SbBS512_E1777 {ECO:0000313|EMBL:ACD06379.1};
OS Shigella boydii serotype 18 (strain CDC 3083-94 / BS512).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=344609 {ECO:0000313|EMBL:ACD06379.1, ECO:0000313|Proteomes:UP000001030};
RN [1] {ECO:0000313|Proteomes:UP000001030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 3083-94 / BS512 {ECO:0000313|Proteomes:UP000001030};
RA Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R.,
RA Jiang L., Ravel J., Sebastian Y.;
RT "Complete sequence of Shigella boydii serotype 18 strain BS512.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001063; ACD06379.1; -; Genomic_DNA.
DR RefSeq; WP_000148717.1; NC_010658.1.
DR AlphaFoldDB; B2U1Q1; -.
DR STRING; 344609.SbBS512_E1777; -.
DR KEGG; sbc:SbBS512_E1777; -.
DR HOGENOM; CLU_077650_7_1_6; -.
DR Proteomes; UP000001030; 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:UP000001030}.
SQ SEQUENCE 204 AA; 23410 MW; 3E426B5B511B2CA1 CRC64;
MTHFSQQDNF SVAARVLGAL FYYAPESAEA APLVAVLTSD GWETQWPLPE ASLAPLVTAF
QTQCEETHAQ AWQRLFVGPW ALPSPPWGSV WLDRESVLFG DSTLALRQWM REKGIQFEMK
QYEPEDHFGS LLLMAAWLAE NGRQTECEEL LAWHLFPWST RFLDVFIEKA EHPFYRALGE
LSRLTLAQWQ SQLLIPVAVK PLFR
//
