ID   TUSD_YERE8              Reviewed;         131 AA.
AC   A1JS60;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Sulfurtransferase TusD {ECO:0000255|HAMAP-Rule:MF_00390};
DE            EC=2.8.1.- {ECO:0000255|HAMAP-Rule:MF_00390};
DE   AltName: Full=tRNA 2-thiouridine synthesizing protein D {ECO:0000255|HAMAP-Rule:MF_00390};
GN   Name=tusD {ECO:0000255|HAMAP-Rule:MF_00390}; OrderedLocusNames=YE3933;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(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:0000255|HAMAP-Rule:MF_00390}.
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:0000255|HAMAP-Rule:MF_00390}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00390}.
CC   -!- SIMILARITY: Belongs to the DsrE/TusD family. {ECO:0000255|HAMAP-
CC       Rule:MF_00390}.
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DR   EMBL; AM286415; CAL13952.1; -; Genomic_DNA.
DR   RefSeq; WP_011817322.1; NC_008800.1.
DR   RefSeq; YP_001008078.1; NC_008800.1.
DR   AlphaFoldDB; A1JS60; -.
DR   SMR; A1JS60; -.
DR   STRING; 393305.YE3933; -.
DR   EnsemblBacteria; CAL13952; CAL13952; YE3933.
DR   KEGG; yen:YE3933; -.
DR   PATRIC; fig|393305.7.peg.4183; -.
DR   eggNOG; COG1553; Bacteria.
DR   HOGENOM; CLU_132095_0_0_6; -.
DR   OMA; PQDDRNI; -.
DR   Proteomes; UP000000642; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016783; F:sulfurtransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Cytoplasm; Transferase; tRNA processing.
FT   CHAIN           1..131
FT                   /note="Sulfurtransferase TusD"
FT                   /id="PRO_1000013257"
FT   ACT_SITE        81
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00390"
SQ   SEQUENCE   131 AA;  14095 MW;  A2FCAC51BA21527A CRC64;
     MSGLKYGLMV TGPAYGTQQA SSAYQFAQAL INSGHHLVSV FFYREGVLNA NQLTTPANDE
     FDLVRAWQQL ANEHAVILNV CVAAALRRGI TDQHEAEQLN LAAANLQPGF TLSGLGALAE
     AALTCDRMVQ F