ID   TORD_SALBC              Reviewed;         209 AA.
AC   F8VF07;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Chaperone protein TorD {ECO:0000255|HAMAP-Rule:MF_01150};
GN   Name=torD {ECO:0000255|HAMAP-Rule:MF_01150}; OrderedLocusNames=SBG_2023;
OS   Salmonella bongori (strain ATCC 43975 / DSM 13772 / NCTC 12419).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=218493;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43975 / DSM 13772 / NCTC 12419;
RX   PubMed=21876672; DOI=10.1371/journal.ppat.1002191;
RA   Fookes M., Schroeder G.N., Langridge G.C., Blondel C.J., Mammina C.,
RA   Connor T.R., Seth-Smith H., Vernikos G.S., Robinson K.S., Sanders M.,
RA   Petty N.K., Kingsley R.A., Baumler A.J., Nuccio S.P., Contreras I.,
RA   Santiviago C.A., Maskell D., Barrow P., Humphrey T., Nastasi A.,
RA   Roberts M., Frankel G., Parkhill J., Dougan G., Thomson N.R.;
RT   "Salmonella bongori provides insights into the evolution of the
RT   Salmonellae.";
RL   PLoS Pathog. 7:E1002191-E1002191(2011).
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; FR877557; CCC31084.1; -; Genomic_DNA.
DR   RefSeq; WP_001164840.1; NC_015761.1.
DR   AlphaFoldDB; F8VF07; -.
DR   SMR; F8VF07; -.
DR   EnsemblBacteria; CCC31084; CCC31084; SBG_2023.
DR   KEGG; sbg:SBG_2023; -.
DR   eggNOG; COG3381; Bacteria.
DR   OMA; PYASMYI; -.
DR   OrthoDB; 1995553at2; -.
DR   Proteomes; UP000000289; 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..209
FT                   /note="Chaperone protein TorD"
FT                   /id="PRO_0000414898"
SQ   SEQUENCE   209 AA;  23730 MW;  3C20C159CD66ADC4 CRC64;
     MQHSSVTSPR AAIYQWFSQL LFQELTEAQL VTLGGRESRA WIASLSTIPG LASDVKRFER
     SLTRVLHREA REQELAADFA SLFLLAPPVG VSPYAGHYPH TTPAQERRQM NALLVEQALA
     PRENEASDHI AIQLALMAEQ ISREASVATQ YYFLQHHILC WAPLFMASCQ QREAEGFYVL
     AVAMIVHFMH EDAQYLESLL MDNVYCRNH