TUSD_ECO7I
ID TUSD_ECO7I Reviewed; 128 AA.
AC B7NLQ0;
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};
GN OrderedLocusNames=ECIAI39_3825;
OS Escherichia coli O7:K1 (strain IAI39 / ExPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAI39 / ExPEC;
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; CU928164; CAR19939.1; -; Genomic_DNA.
DR RefSeq; WP_001209685.1; NC_011750.1.
DR RefSeq; YP_002409722.1; NC_011750.1.
DR AlphaFoldDB; B7NLQ0; -.
DR SMR; B7NLQ0; -.
DR STRING; 585057.ECIAI39_3825; -.
DR EnsemblBacteria; CAR19939; CAR19939; ECIAI39_3825.
DR KEGG; ect:ECIAI39_3825; -.
DR PATRIC; fig|585057.6.peg.3962; -.
DR HOGENOM; CLU_132095_0_0_6; -.
DR OMA; PQDDRNI; -.
DR Proteomes; UP000000749; 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_1000122858"
FT ACT_SITE 78
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00390"
SQ SEQUENCE 128 AA; 13630 MW; 8C8352E07FBE554C CRC64;
MRFAIVVTGP AYGTQQASSA FQFAQALIAE GHELSCVFFY REGVYNANQL TSPASDEFDL
VRGWQQLNAQ HGVALNICVA AALRRGIVDE TEAGRLGLAS SNLQSGFTLS GLGALAEASL
TCDRVVQF