TORD_ECOBW
ID TORD_ECOBW Reviewed; 199 AA.
AC C4ZQC6;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, 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=BWG_0852;
OS Escherichia coli (strain K12 / MC4100 / BW2952).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=595496;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MC4100 / BW2952;
RX PubMed=19376874; DOI=10.1128/jb.00118-09;
RA Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R.,
RA Wang L.;
RT "Genomic sequencing reveals regulatory mutations and recombinational events
RT in the widely used MC4100 lineage of Escherichia coli K-12.";
RL J. Bacteriol. 191:4025-4029(2009).
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; CP001396; ACR62138.1; -; Genomic_DNA.
DR RefSeq; WP_000209861.1; NC_012759.1.
DR AlphaFoldDB; C4ZQC6; -.
DR SMR; C4ZQC6; -.
DR KEGG; ebw:BWG_0852; -.
DR HOGENOM; CLU_077650_4_0_6; -.
DR OMA; PYASMYI; -.
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_1000213664"
SQ SEQUENCE 199 AA; 22601 MW; 5B81980534F2DE68 CRC64;
MTTLTAQQIA CVYAWLAQLF SRELDDEQLT QIASAQMAEW FSLLKNEPPL TAAVNELENR
IATLTVRDDA RLELAADFCG LFLMTDKQAA LPYASAYKQD EQEIKRLLVE AGMETSGNFN
EPADHLAIYL ELLSHLHFSL GEGTVPARRI DSLRQKTLTA LWQWLPEFVA RCRQYDSFGF
YAALSQLLLV LVECDHQNR