TORD_ECOL6
ID TORD_ECOL6 Reviewed; 199 AA.
AC Q8FJ52;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Chaperone protein TorD {ECO:0000255|HAMAP-Rule:MF_01150};
GN Name=torD {ECO:0000255|HAMAP-Rule:MF_01150}; OrderedLocusNames=c1134;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN79602.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014075; AAN79602.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000209907.1; NC_004431.1.
DR AlphaFoldDB; Q8FJ52; -.
DR SMR; Q8FJ52; -.
DR STRING; 199310.c1134; -.
DR EnsemblBacteria; AAN79602; AAN79602; c1134.
DR KEGG; ecc:c1134; -.
DR eggNOG; COG3381; Bacteria.
DR HOGENOM; CLU_077650_4_0_6; -.
DR OMA; PYASMYI; -.
DR Proteomes; UP000001410; 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_0000211635"
SQ SEQUENCE 199 AA; 22439 MW; E0F850902747ACDF CRC64;
MTTLTAQQIA CVYAWLAQLF SRELDDEQLT QIASAQMAEW FSLLKSEPPL TAAVNGLENS
IATLTVRDDA RLELAADFCG LFLMTDKQAA LPYASAYKQD EQEIKRLLVE AGMETSGNFN
EPADHLAIYP ELLSHLHFSL GEGTVPARRI DGLRQKTLTA LREWLPEFAA RCRQYDRFGF
YAALSQLLLV LVECDYQKR