ID   TUSD_PROMH              Reviewed;         130 AA.
AC   B4EYW2;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=PMI2798;
OS   Proteus mirabilis (strain HI4320).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=529507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI4320;
RX   PubMed=18375554; DOI=10.1128/jb.01981-07;
RA   Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA   Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA   Parkhill J., Mobley H.L.T.;
RT   "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT   both adherence and motility.";
RL   J. Bacteriol. 190:4027-4037(2008).
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; AM942759; CAR45516.1; -; Genomic_DNA.
DR   RefSeq; WP_004246892.1; NC_010554.1.
DR   AlphaFoldDB; B4EYW2; -.
DR   SMR; B4EYW2; -.
DR   STRING; 529507.PMI2798; -.
DR   EnsemblBacteria; CAR45516; CAR45516; PMI2798.
DR   GeneID; 6801510; -.
DR   KEGG; pmr:PMI2798; -.
DR   eggNOG; COG1553; Bacteria.
DR   HOGENOM; CLU_132095_0_0_6; -.
DR   OMA; PQDDRNI; -.
DR   Proteomes; UP000008319; 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; Reference proteome; Transferase; tRNA processing.
FT   CHAIN           1..130
FT                   /note="Sulfurtransferase TusD"
FT                   /id="PRO_1000205816"
FT   ACT_SITE        80
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00390"
SQ   SEQUENCE   130 AA;  14195 MW;  4B39023986B60DAA CRC64;
     MNLTYCLLVT GPHYGTEQAS SAYLFAKALL EKGHHIAQVF FYREGVSNAN QLVSPASDEF
     DLPKAWIALA SRYNIPLQVC VAAALRRGVV DEQQAKEQGL LSSNMATKFE LSGLGALAQA
     MLTCDRVVQF