ID   TUSD_PECCP              Reviewed;         129 AA.
AC   C6DG85;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 59.
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=PC1_3833;
OS   Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=561230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001657; ACT14848.1; -; Genomic_DNA.
DR   RefSeq; WP_015841933.1; NC_012917.1.
DR   AlphaFoldDB; C6DG85; -.
DR   SMR; C6DG85; -.
DR   STRING; 561230.PC1_3833; -.
DR   EnsemblBacteria; ACT14848; ACT14848; PC1_3833.
DR   KEGG; pct:PC1_3833; -.
DR   eggNOG; COG1553; Bacteria.
DR   HOGENOM; CLU_132095_0_0_6; -.
DR   OMA; PQDDRNI; -.
DR   OrthoDB; 1997912at2; -.
DR   Proteomes; UP000002736; 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..129
FT                   /note="Sulfurtransferase TusD"
FT                   /id="PRO_1000205815"
FT   ACT_SITE        79
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00390"
SQ   SEQUENCE   129 AA;  13822 MW;  359DA2CE5B233961 CRC64;
     MLSYCLLVTG PAYGTQQASS ALQFAQALLA EGHRLKSVFF YREGVLNANQ LTSPANDEFD
     LVRAWQLLGE THQVALNVCV AAALRRGVTD AQQAAQLNLA GANLQPGFVL SGLGELAQSV
     LTCDRVIQF