TUSD_ECO8A
ID TUSD_ECO8A Reviewed; 128 AA.
AC B7M1P6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 64.
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=ECIAI1_3481;
OS Escherichia coli O8 (strain IAI1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585034;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAI1;
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}.
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; CU928160; CAR00283.1; -; Genomic_DNA.
DR RefSeq; WP_001209710.1; NC_011741.1.
DR AlphaFoldDB; B7M1P6; -.
DR SMR; B7M1P6; -.
DR GeneID; 58460169; -.
DR KEGG; ecr:ECIAI1_3481; -.
DR HOGENOM; CLU_132095_0_0_6; -.
DR OMA; PQDDRNI; -.
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_1000122859"
FT ACT_SITE 78
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00390"
SQ SEQUENCE 128 AA; 13652 MW; CF1BC2FE90A0A4A1 CRC64;
MRFAIVVTGP AYGTQQASSA FQFAQALIVE GHELSSVFFY REGVYNANQL TSPASDEFDL
VRGWQQLNAQ HGVALNICVA AALRRGIVDE TEAGRLGLAS SNLQPGFTLS GLGALAEASL
TCDRVVQF