ID   TUSD_SALA4              Reviewed;         128 AA.
AC   B5F8G3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   25-MAY-2022, entry version 58.
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=SeAg_B3648;
OS   Salmonella agona (strain SL483).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=454166;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL483;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001138; ACH49271.1; -; Genomic_DNA.
DR   RefSeq; WP_001268010.1; NC_011149.1.
DR   AlphaFoldDB; B5F8G3; -.
DR   SMR; B5F8G3; -.
DR   EnsemblBacteria; ACH49271; ACH49271; SeAg_B3648.
DR   KEGG; sea:SeAg_B3648; -.
DR   HOGENOM; CLU_132095_0_0_6; -.
DR   OMA; PQDDRNI; -.
DR   Proteomes; UP000008819; 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..128
FT                   /note="Sulfurtransferase TusD"
FT                   /id="PRO_1000122867"
FT   ACT_SITE        78
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00390"
SQ   SEQUENCE   128 AA;  13758 MW;  62A184F98AC5F1F0 CRC64;
     MRYAIMVTGP AYGTQQASSA LQFAHALLNE GHELASVFFY REGVYNANLL TSPASDEYDL
     VRAWQKLNTQ HGVALNICVA AALRRGIIDE TEAGRLALPS ANLQPGFTLS GLGALAEASL
     TCDRVVQF