ID   TORD_SALTY              Reviewed;         210 AA.
AC   Q8ZKZ8;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Chaperone protein TorD {ECO:0000255|HAMAP-Rule:MF_01150};
GN   Name=torD {ECO:0000255|HAMAP-Rule:MF_01150}; OrderedLocusNames=STM3821;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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; AE006468; AAL22680.1; -; Genomic_DNA.
DR   RefSeq; NP_462721.1; NC_003197.2.
DR   RefSeq; WP_000595421.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZKZ8; -.
DR   SMR; Q8ZKZ8; -.
DR   STRING; 99287.STM3821; -.
DR   PaxDb; Q8ZKZ8; -.
DR   EnsemblBacteria; AAL22680; AAL22680; STM3821.
DR   GeneID; 1255348; -.
DR   KEGG; stm:STM3821; -.
DR   PATRIC; fig|99287.12.peg.4045; -.
DR   HOGENOM; CLU_077650_4_0_6; -.
DR   OMA; PYASMYI; -.
DR   PhylomeDB; Q8ZKZ8; -.
DR   BioCyc; SENT99287:STM3821-MON; -.
DR   Proteomes; UP000001014; 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; Reference proteome.
FT   CHAIN           1..210
FT                   /note="Chaperone protein TorD"
FT                   /id="PRO_0000211641"
SQ   SEQUENCE   210 AA;  23800 MW;  C8EE75D91484B388 CRC64;
     MIKQPALAQE QYACVYAWLA LLFFREVDDE GLIQLQSAEI ADWLALLKRQ PALAASVALL
     EQKIAALSLR QDAQLELAAD FCGLFLMTDK KSALPYASQY PQQEPGMIKH LLLEAGMEVN
     DDFKEPTDHL AIYLELLSHL HFSLGESFQQ RRMNKLRQKT LSSLLEWLPE FTNNCLKHDP
     YGFYAALSQL LLAIVRFDDG KEDLSIVAAE