ID Q65Q18_MANSM Unreviewed; 224 AA.
AC Q65Q18;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Probable 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=torD {ECO:0000313|EMBL:AAU38942.1};
GN Synonyms=dmsD {ECO:0000256|HAMAP-Rule:MF_00940};
GN OrderedLocusNames=MS2335 {ECO:0000313|EMBL:AAU38942.1};
OS Mannheimia succiniciproducens (strain MBEL55E).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Basfia.
OX NCBI_TaxID=221988 {ECO:0000313|EMBL:AAU38942.1, ECO:0000313|Proteomes:UP000000607};
RN [1] {ECO:0000313|EMBL:AAU38942.1, ECO:0000313|Proteomes:UP000000607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBEL55E {ECO:0000313|EMBL:AAU38942.1,
RC ECO:0000313|Proteomes:UP000000607};
RX PubMed=15378067; DOI=10.1038/nbt1010;
RA Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA Jeong H., Hur C.G., Kim J.J.;
RT "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT succiniciproducens.";
RL Nat. Biotechnol. 22:1275-1281(2004).
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; AE016827; AAU38942.1; -; Genomic_DNA.
DR AlphaFoldDB; Q65Q18; -.
DR STRING; 221988.MS2335; -.
DR KEGG; msu:MS2335; -.
DR eggNOG; COG3381; Bacteria.
DR HOGENOM; CLU_077650_7_1_6; -.
DR Proteomes; UP000000607; 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:SF1; TAT PROOFREADING CHAPERONE DMSD-RELATED; 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|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00940}.
SQ SEQUENCE 224 AA; 25994 MW; 98204EED02797AB2 CRC64;
MVKNTALLSL KQQKSAMNFK EILMDNALLQ WISTGGRLLG AVFYYEPKDK RVQPVLDFFR
QPDWTKDWAT LANPALINAL IEKSAQQDLS QAYQYLFIGP NELPAPPWGS VYLDKESVIF
GDSLLALRDF LTVHQIEFIQ TQNEPEDHLG LMLMLAAYLA ENKPELLEEF LTKHLFSWVY
RCLDLIFAQT DYPFYQAMAL LARQTLKGWQ QQLDLQVDQP QLYR
//
