ID A0A097R0W6_HAFAL Unreviewed; 204 AA.
AC A0A097R0W6;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
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 ORFNames=AT03_08230 {ECO:0000313|EMBL:AIU72378.1};
OS Hafnia alvei FB1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Hafnia.
OX NCBI_TaxID=1453496 {ECO:0000313|EMBL:AIU72378.1, ECO:0000313|Proteomes:UP000029986};
RN [1] {ECO:0000313|EMBL:AIU72378.1, ECO:0000313|Proteomes:UP000029986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FB1 {ECO:0000313|EMBL:AIU72378.1,
RC ECO:0000313|Proteomes:UP000029986};
RX PubMed=25075225; DOI=10.1186/1757-4749-6-29;
RA Tan J.Y., Yin W.F., Chan K.G.;
RT "Gene clusters of Hafnia alvei strain FB1 important in survival and
RT pathogenesis: a draft genome perspective.";
RL Gut Pathog. 6:29-29(2014).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP009706; AIU72378.1; -; Genomic_DNA.
DR RefSeq; WP_025800955.1; NZ_CP009706.1.
DR AlphaFoldDB; A0A097R0W6; -.
DR KEGG; hav:AT03_08230; -.
DR PATRIC; fig|1453496.5.peg.1641; -.
DR eggNOG; COG3381; Bacteria.
DR HOGENOM; CLU_077650_7_1_6; -.
DR OrthoDB; 3174863at2; -.
DR Proteomes; UP000029986; 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:UP000029986}.
SQ SEQUENCE 204 AA; 23027 MW; 22B427BD5C176A5B CRC64;
MLQPQQLQDI AISARALGAL FYYSPESEAC TPLVEIFTSS EWCSEWPYGS EPQLAQCMTQ
LAAATNESLE DAYQRLFIGP HALPAPPWGS VYLDKESVLF GDSTLALRQW MRQHHIEGQS
GQKEPEDQFG LMLMMAAWLA ETQPQALGEF LSVHLLPWSS RYLTLMIQDA QHPFYQGLAE
LAMLTLASWQ QQLAIMPVAC ELYR
//
