ID A0A085GET3_9ENTR Unreviewed; 212 AA.
AC A0A085GET3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 21.
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:KFC82228.1};
GN ORFNames=GBAG_1734 {ECO:0000313|EMBL:KFC82228.1};
OS Buttiauxella agrestis ATCC 33320.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Buttiauxella.
OX NCBI_TaxID=1006004 {ECO:0000313|EMBL:KFC82228.1, ECO:0000313|Proteomes:UP000028653};
RN [1] {ECO:0000313|EMBL:KFC82228.1, ECO:0000313|Proteomes:UP000028653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33320 {ECO:0000313|EMBL:KFC82228.1,
RC ECO:0000313|Proteomes:UP000028653};
RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT the evolutionary history of the Enterobacteriaceae.";
RL Submitted (MAY-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFC82228.1}.
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DR EMBL; JMPI01000024; KFC82228.1; -; Genomic_DNA.
DR RefSeq; WP_051873668.1; NZ_JMPI01000024.1.
DR AlphaFoldDB; A0A085GET3; -.
DR STRING; 1006004.GBAG_1734; -.
DR eggNOG; COG3381; Bacteria.
DR OrthoDB; 3174863at2; -.
DR Proteomes; UP000028653; Unassembled WGS sequence.
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:UP000028653}.
SQ SEQUENCE 212 AA; 24094 MW; 673445E32E7C4FC4 CRC64;
MSKSTSATTQ RLATIALTGR VLGALYYQEP KSRDVASLYA SLADPKWAEQ WPVQHDELAA
IAQRMTDGLD YSQESLSEAW QRLFIGPYAL PASPWGSVYL DKESVLFGDS MLELRRWMRK
NDISNEQESN EPEDHIGLLL MLAAWLAEEG LQQKVDELLA WHILPWSGRF LELFIAHAEH
PFYQALGELT QITLAEWRTD LLIPVATKEL HA
//
