ID   TUSD_KLEP3              Reviewed;         128 AA.
AC   B5XN82;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 55.
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=KPK_0387;
OS   Klebsiella pneumoniae (strain 342).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=507522;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=342;
RX   PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA   Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA   Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA   Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA   Methe B.A.;
RT   "Complete genome sequence of the N2-fixing broad host range endophyte
RT   Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL   PLoS Genet. 4:E1000141-E1000141(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; CP000964; ACI07727.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5XN82; -.
DR   SMR; B5XN82; -.
DR   EnsemblBacteria; ACI07727; ACI07727; KPK_0387.
DR   KEGG; kpe:KPK_0387; -.
DR   HOGENOM; CLU_132095_0_0_6; -.
DR   OMA; PQDDRNI; -.
DR   OrthoDB; 1997912at2; -.
DR   Proteomes; UP000001734; 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_1000122866"
FT   ACT_SITE        78
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00390"
SQ   SEQUENCE   128 AA;  13864 MW;  F8D31F4A03BCAC2C CRC64;
     MRFALTVTGP AYGTQQASSA WQFAQAVLQE GHELACVFFY REGVLNANQL TAPASDEFDL
     VRAWQSLHDE QGVALHICVA AALRRGVTDE REAQQLALAS HNLQPGFTLS GLGALAEAAL
     TCDRMVQF