ID D3H112_ECO44 Unreviewed; 199 AA.
AC D3H112;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 08-NOV-2023, entry version 63.
DE RecName: Full=Chaperone protein TorD {ECO:0000256|HAMAP-Rule:MF_01150};
GN Name=torD {ECO:0000256|HAMAP-Rule:MF_01150,
GN ECO:0000313|EMBL:CBG33896.1};
GN OrderedLocusNames=EC042_1074 {ECO:0000313|EMBL:CBG33896.1};
OS Escherichia coli O44:H18 (strain 042 / EAEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=216592 {ECO:0000313|EMBL:CBG33896.1, ECO:0000313|Proteomes:UP000001407};
RN [1] {ECO:0000313|EMBL:CBG33896.1, ECO:0000313|Proteomes:UP000001407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=042 / EAEC {ECO:0000313|Proteomes:UP000001407};
RX PubMed=20098708; DOI=10.1371/journal.pone.0008801;
RA Chaudhuri R.R., Sebaihia M., Hobman J.L., Webber M.A., Leyton D.L.,
RA Goldberg M.D., Cunningham A.F., Scott-Tucker A., Ferguson P.R.,
RA Thomas C.M., Frankel G., Tang C.M., Dudley E.G., Roberts I.S., Rasko D.A.,
RA Pallen M.J., Parkhill J., Nataro J.P., Thomson N.R., Henderson I.R.;
RT "Complete genome sequence and comparative metabolic profiling of the
RT prototypical enteroaggregative Escherichia coli strain 042.";
RL PLoS ONE 5:E8801-E8801(2010).
CC -!- FUNCTION: Involved in the biogenesis of TorA. Acts on TorA before the
CC insertion of the molybdenum cofactor and, as a result, probably favors
CC a conformation of the apoenzyme that is competent for acquiring the
CC cofactor. {ECO:0000256|HAMAP-Rule:MF_01150}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01150}.
CC -!- SIMILARITY: Belongs to the TorD/DmsD family. TorD subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01150}.
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DR EMBL; FN554766; CBG33896.1; -; Genomic_DNA.
DR RefSeq; WP_000209852.1; NC_017626.1.
DR AlphaFoldDB; D3H112; -.
DR KEGG; elo:EC042_1074; -.
DR PATRIC; fig|216592.3.peg.1110; -.
DR HOGENOM; CLU_077650_4_0_6; -.
DR OMA; PYASMYI; -.
DR Proteomes; UP000001407; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.120.1820; -; 1.
DR Gene3D; 1.20.1280.20; HscB, C-terminal domain; 1.
DR HAMAP; MF_01150; TorD; 1.
DR InterPro; IPR023069; Chaperone_TorD.
DR InterPro; IPR020945; DMSO/NO3_reduct_chaperone.
DR InterPro; IPR036386; HscB_C_sf.
DR InterPro; IPR036411; TorD-like_sf.
DR PANTHER; PTHR34227:SF11; CHAPERONE PROTEIN TORD; 1.
DR PANTHER; PTHR34227; CHAPERONE PROTEIN YCDY; 1.
DR Pfam; PF02613; Nitrate_red_del; 1.
DR SUPFAM; SSF89155; TorD-like; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_01150};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01150}.
SQ SEQUENCE 199 AA; 22355 MW; 2614DF1A7425E301 CRC64;
MTTLTAPQIA CVYAWLAQLF SRELGDEQLT QIASTQMAEW FSLLKSEPPL TAAVNALENR
IAALTVRDDA RLELAADFCG LFLMTDKQAA LPYASAYKQD EQEIKRLLVE AGMETSGNFN
EPADHLAIYL ELLSHLHFSL GEGTVSARRI DSLRQKTLTA LRQWLPEFAA RCHQYDSFGF
YSALSQLLLV LVECDHQNR
//