ID TORD_ECOLI Reviewed; 199 AA.
AC P36662;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 24-JAN-2024, entry version 153.
DE RecName: Full=Chaperone protein TorD;
GN Name=torD; OrderedLocusNames=b0998, JW0983;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8022286; DOI=10.1111/j.1365-2958.1994.tb00393.x;
RA Mejean V., Iobbi-Nivol C., Lepelletier M., Giordano G., Chippaux M.,
RA Pascal M.-C.;
RT "TMAO anaerobic respiration in Escherichia coli: involvement of the tor
RT operon.";
RL Mol. Microbiol. 11:1169-1179(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8302830; DOI=10.1073/pnas.91.3.1054;
RA Ueguchi C., Kakeda M., Yamada H., Mizuno T.;
RT "An analogue of the DnaJ molecular chaperone in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:1054-1058(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PROTEIN SEQUENCE OF 1-10, FUNCTION, SUBCELLULAR LOCATION, AND
RP CHARACTERIZATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=9632735; DOI=10.1074/jbc.273.26.16615;
RA Pommier J., Mejean V., Giordano G., Iobbi-Nivol C.;
RT "TorD, a cytoplasmic chaperone that interacts with the unfolded
RT trimethylamine N-oxide reductase enzyme (TorA) in Escherichia coli.";
RL J. Biol. Chem. 273:16615-16620(1998).
RN [7]
RP FUNCTION.
RX PubMed=12766163; DOI=10.1074/jbc.m302730200;
RA Ilbert M., Mejean V., Giudici-Orticoni M.-T., Samama J.-P., Iobbi-Nivol C.;
RT "Involvement of a mate chaperone (TorD) in the maturation pathway of
RT molybdoenzyme TorA.";
RL J. Biol. Chem. 278:28787-28792(2003).
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:0000269|PubMed:12766163, ECO:0000269|PubMed:9632735}.
CC -!- INTERACTION:
CC P36662; P33225: torA; NbExp=24; IntAct=EBI-6406226, EBI-557008;
CC P36662; P36662: torD; NbExp=4; IntAct=EBI-6406226, EBI-6406226;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9632735}.
CC -!- SIMILARITY: Belongs to the TorD/DmsD family. TorD subfamily.
CC {ECO:0000305}.
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DR EMBL; X73888; CAA52096.1; -; Genomic_DNA.
DR EMBL; D16500; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U00096; AAC74083.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA36140.1; -; Genomic_DNA.
DR PIR; D64841; D64841.
DR RefSeq; NP_415518.1; NC_000913.3.
DR RefSeq; WP_000209894.1; NZ_SSZK01000002.1.
DR AlphaFoldDB; P36662; -.
DR SMR; P36662; -.
DR BioGRID; 4260700; 117.
DR BioGRID; 849997; 2.
DR DIP; DIP-11015N; -.
DR IntAct; P36662; 4.
DR MINT; P36662; -.
DR STRING; 511145.b0998; -.
DR TCDB; 5.A.3.4.1; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR PaxDb; 511145-b0998; -.
DR EnsemblBacteria; AAC74083; AAC74083; b0998.
DR GeneID; 945625; -.
DR KEGG; ecj:JW0983; -.
DR KEGG; eco:b0998; -.
DR PATRIC; fig|511145.12.peg.1034; -.
DR EchoBASE; EB2112; -.
DR eggNOG; COG3381; Bacteria.
DR HOGENOM; CLU_077650_4_0_6; -.
DR InParanoid; P36662; -.
DR OMA; PYASMYI; -.
DR OrthoDB; 7849731at2; -.
DR PhylomeDB; P36662; -.
DR BioCyc; EcoCyc:EG12195-MONOMER; -.
DR SABIO-RK; P36662; -.
DR PRO; PR:P36662; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IMP:EcoliWiki.
DR GO; GO:0042277; F:peptide binding; IMP:EcoliWiki.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR GO; GO:0051604; P:protein maturation; IEP:EcoliWiki.
DR Gene3D; 1.20.120.1820; -; 1.
DR Gene3D; 1.20.1280.20; HscB, C-terminal domain; 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 PANTHER; PTHR34227:SF11; CHAPERONE PROTEIN TORD; 1.
DR PANTHER; PTHR34227; CHAPERONE PROTEIN YCDY; 1.
DR Pfam; PF02613; Nitrate_red_del; 1.
DR SUPFAM; SSF89155; TorD-like; 1.
PE 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Direct protein sequencing; Reference proteome.
FT CHAIN 1..199
FT /note="Chaperone protein TorD"
FT /id="PRO_0000211634"
FT CONFLICT 46
FT /note="S -> N (in Ref. 1; CAA52096)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 199 AA; 22574 MW; F58357DA153FDE74 CRC64;
MTTLTAQQIA CVYAWLAQLF SRELDDEQLT QIASAQMAEW FSLLKSEPPL TAAVNELENR
IATLTVRDDA RLELAADFCG LFLMTDKQAA LPYASAYKQD EQEIKRLLVE AGMETSGNFN
EPADHLAIYL ELLSHLHFSL GEGTVPARRI DSLRQKTLTA LWQWLPEFVA RCRQYDSFGF
YAALSQLLLV LVECDHQNR
//
