TUSD_ECOLI
ID TUSD_ECOLI Reviewed; 128 AA.
AC P45532; Q2M710;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Sulfurtransferase TusD;
DE EC=2.8.1.-;
DE AltName: Full=tRNA 2-thiouridine synthesizing protein D;
GN Name=tusD; Synonyms=yheN; OrderedLocusNames=b3345, JW3307;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3]
RP FUNCTION, MUTAGENESIS OF CYS-78, AND SUBUNIT.
RX PubMed=16387657; DOI=10.1016/j.molcel.2005.11.001;
RA Ikeuchi Y., Shigi N., Kato J., Nishimura A., Suzuki T.;
RT "Mechanistic insights into sulfur relay by multiple sulfur mediators
RT involved in thiouridine biosynthesis at tRNA wobble positions.";
RL Mol. Cell 21:97-108(2006).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS), MUTAGENESIS OF CYS-78 AND CYS-122,
RP AND SUBUNIT.
RX PubMed=16472754; DOI=10.1016/j.str.2005.11.009;
RA Numata T., Fukai S., Ikeuchi Y., Suzuki T., Nureki O.;
RT "Structural basis for sulfur relay to RNA mediated by heterohexameric
RT TusBCD complex.";
RL Structure 14:357-366(2006).
CC -!- FUNCTION: Part of a sulfur-relay system required for 2-thiolation of 5-
CC methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions.
CC Accepts sulfur from TusA and transfers it in turn to TusE.
CC {ECO:0000269|PubMed:16387657}.
CC -!- SUBUNIT: Heterohexamer, formed by a dimer of trimers. The hexameric
CC TusBCD complex contains 2 copies each of TusB, TusC and TusD. The
CC TusBCD complex interacts with TusE. {ECO:0000269|PubMed:16387657,
CC ECO:0000269|PubMed:16472754}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DsrE/TusD family. {ECO:0000305}.
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DR EMBL; U18997; AAA58142.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76370.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77946.1; -; Genomic_DNA.
DR PIR; D65128; D65128.
DR RefSeq; NP_417804.1; NC_000913.3.
DR RefSeq; WP_001209680.1; NZ_SSZK01000008.1.
DR PDB; 2D1P; X-ray; 2.15 A; A/D/G=1-128.
DR PDBsum; 2D1P; -.
DR AlphaFoldDB; P45532; -.
DR SMR; P45532; -.
DR BioGRID; 4262469; 33.
DR ComplexPortal; CPX-2144; TusBCDE complex.
DR DIP; DIP-12310N; -.
DR IntAct; P45532; 1.
DR STRING; 511145.b3345; -.
DR jPOST; P45532; -.
DR PaxDb; P45532; -.
DR PRIDE; P45532; -.
DR EnsemblBacteria; AAC76370; AAC76370; b3345.
DR EnsemblBacteria; BAE77946; BAE77946; BAE77946.
DR GeneID; 947852; -.
DR KEGG; ecj:JW3307; -.
DR KEGG; eco:b3345; -.
DR PATRIC; fig|1411691.4.peg.3386; -.
DR EchoBASE; EB2735; -.
DR eggNOG; COG1553; Bacteria.
DR HOGENOM; CLU_132095_0_0_6; -.
DR InParanoid; P45532; -.
DR OMA; PQDDRNI; -.
DR PhylomeDB; P45532; -.
DR BioCyc; EcoCyc:G7714-MON; -.
DR BioCyc; MetaCyc:G7714-MON; -.
DR EvolutionaryTrace; P45532; -.
DR PRO; PR:P45532; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:1990228; C:sulfurtransferase complex; IDA:EcoCyc.
DR GO; GO:0097163; F:sulfur carrier activity; IDA:EcoCyc.
DR GO; GO:0016783; F:sulfurtransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0002143; P:tRNA wobble position uridine thiolation; IDA:ComplexPortal.
DR Gene3D; 3.40.1260.10; -; 1.
DR HAMAP; MF_00390; Thiourid_synth_D; 1.
DR InterPro; IPR027396; DsrEFH-like.
DR InterPro; IPR003787; Sulphur_relay_DsrE/F-like.
DR InterPro; IPR017463; Sulphur_relay_TusD/DsrE.
DR Pfam; PF02635; DrsE; 1.
DR SUPFAM; SSF75169; SSF75169; 1.
DR TIGRFAMs; TIGR03012; sulf_tusD_dsrE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome; Transferase; tRNA processing.
FT CHAIN 1..128
FT /note="Sulfurtransferase TusD"
FT /id="PRO_0000214724"
FT ACT_SITE 78
FT /note="Cysteine persulfide intermediate"
FT MUTAGEN 78
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16387657,
FT ECO:0000269|PubMed:16472754"
FT MUTAGEN 122
FT /note="C->S: Reduced activity."
FT /evidence="ECO:0000269|PubMed:16472754"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:2D1P"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:2D1P"
FT HELIX 16..29
FT /evidence="ECO:0007829|PDB:2D1P"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:2D1P"
FT HELIX 41..47
FT /evidence="ECO:0007829|PDB:2D1P"
FT HELIX 60..71
FT /evidence="ECO:0007829|PDB:2D1P"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:2D1P"
FT HELIX 79..84
FT /evidence="ECO:0007829|PDB:2D1P"
FT HELIX 90..96
FT /evidence="ECO:0007829|PDB:2D1P"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:2D1P"
FT HELIX 113..121
FT /evidence="ECO:0007829|PDB:2D1P"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:2D1P"
SQ SEQUENCE 128 AA; 13641 MW; 87B2754849A0FEFF CRC64;
MRFAIVVTGP AYGTQQASSA FQFAQALIAD GHELSSVFFY REGVYNANQL TSPASDEFDL
VRAWQQLNAQ HGVALNICVA AALRRGVVDE TEAGRLGLAS SNLQQGFTLS GLGALAEASL
TCDRVVQF
