TUSD_ECO81
ID TUSD_ECO81 Reviewed; 128 AA.
AC B7N1C6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 61.
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=ECED1_4005;
OS Escherichia coli O81 (strain ED1a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585397;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ED1a;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928162; CAR10144.2; -; Genomic_DNA.
DR RefSeq; WP_001209693.1; NC_011745.1.
DR AlphaFoldDB; B7N1C6; -.
DR SMR; B7N1C6; -.
DR EnsemblBacteria; CAR10144; CAR10144; ECED1_4005.
DR KEGG; ecq:ECED1_4005; -.
DR HOGENOM; CLU_132095_0_0_6; -.
DR OMA; PQDDRNI; -.
DR Proteomes; UP000000748; 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_1000134416"
FT ACT_SITE 78
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00390"
SQ SEQUENCE 128 AA; 13610 MW; C7B3D142FDAE444F CRC64;
MRFAIVVTGP AYGTQQASSA FQFAQALIAE GHELSSVFFY REGVYNANQL TSPASDEFDL
VRGWQQLNAQ HGVALNICVA AALRRGVVDE TEAGRLGLAS SNLQPGFTLS GLGALAEASL
TCDRVVQF