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Database: UniProt
Entry: D3H112_ECO44
LinkDB: D3H112_ECO44
Original site: D3H112_ECO44 
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
//
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