ID   TORD_ECOSE              Reviewed;         199 AA.
AC   B6I974;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Chaperone protein TorD {ECO:0000255|HAMAP-Rule:MF_01150};
GN   Name=torD {ECO:0000255|HAMAP-Rule:MF_01150}; OrderedLocusNames=ECSE_1060;
OS   Escherichia coli (strain SE11).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=409438;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SE11;
RX   PubMed=18931093; DOI=10.1093/dnares/dsn026;
RA   Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T.,
RA   Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.;
RT   "Complete genome sequence and comparative analysis of the wild-type
RT   commensal Escherichia coli strain SE11 isolated from a healthy adult.";
RL   DNA Res. 15:375-386(2008).
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:0000255|HAMAP-Rule:MF_01150}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01150}.
CC   -!- SIMILARITY: Belongs to the TorD/DmsD family. TorD subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01150}.
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DR   EMBL; AP009240; BAG76584.1; -; Genomic_DNA.
DR   RefSeq; WP_000209869.1; NC_011415.1.
DR   AlphaFoldDB; B6I974; -.
DR   SMR; B6I974; -.
DR   EnsemblBacteria; BAG76584; BAG76584; ECSE_1060.
DR   GeneID; 66670724; -.
DR   KEGG; ecy:ECSE_1060; -.
DR   HOGENOM; CLU_077650_4_0_6; -.
DR   OMA; PYASMYI; -.
DR   Proteomes; UP000008199; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR   GO; GO:0051259; P:protein complex oligomerization; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.1280.20; -; 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   Pfam; PF02613; Nitrate_red_del; 1.
DR   SUPFAM; SSF89155; SSF89155; 1.
PE   3: Inferred from homology;
KW   Chaperone; Cytoplasm.
FT   CHAIN           1..199
FT                   /note="Chaperone protein TorD"
FT                   /id="PRO_1000137509"
SQ   SEQUENCE   199 AA;  22503 MW;  009F2FF226075412 CRC64;
     MTTLTAQQIA CVYAWLAQLF SRELDDEQLT QIASAQMAEW FSLLKSEPPL AAAVNELENC
     IATLTVRDDA RLELAADFCG LFLMTDKQAA LPYASAYKQD EQEIKRLLVE AGMETSGNFN
     EPADHLAIYL ELLSHLHFSL GEGTVPARRI DSLRQKTLTA LWQWLPEFVV RCRQYDSFGF
     YAALSQLLLV LVESDHQNR