TTUA_THEMA
ID TTUA_THEMA Reviewed; 304 AA.
AC Q9WY40; G4FHB1;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=tRNA-5-methyluridine(54) 2-sulfurtransferase {ECO:0000305|PubMed:28655838};
DE EC=2.8.1.- {ECO:0000269|PubMed:28655838};
DE AltName: Full=tRNA thiouridine synthetase TtuA;
GN Name=ttuA {ECO:0000303|PubMed:28655838};
GN OrderedLocusNames=TM_0197 {ECO:0000312|EMBL:AAD35289.1};
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ZINC-BINDING, AND PATHWAY.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=28655838; DOI=10.1073/pnas.1700902114;
RA Arragain S., Bimai O., Legrand P., Caillat S., Ravanat J.L., Touati N.,
RA Binet L., Atta M., Fontecave M., Golinelli-Pimpaneau B.;
RT "Nonredox thiolation in tRNA occurring via sulfur activation by a [4Fe-4S]
RT cluster.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:7355-7360(2017).
CC -!- FUNCTION: Catalyzes the ATP-dependent 2-thiolation of 5-methyluridine
CC residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2-
CC thiouridine (m(5)s(2)U or s(2)T) (PubMed:28655838). This modification
CC allows thermal stabilization of tRNAs in thermophilic microorganisms,
CC and is required for cell growth at high temperatures (By similarity).
CC Can use free sulfide as sulfur source in vitro (PubMed:28655838).
CC {ECO:0000250|UniProtKB:Q72LF3, ECO:0000269|PubMed:28655838}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-methyluridine(54) in tRNA + ATP + hydrogen sulfide = 5-
CC methyl-2-thiouridine(54) in tRNA + AMP + diphosphate;
CC Xref=Rhea:RHEA:55188, Rhea:RHEA-COMP:10167, Rhea:RHEA-COMP:13344,
CC ChEBI:CHEBI:29919, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:74447, ChEBI:CHEBI:136799, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:28655838};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:28655838};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is chelated by
CC three Cys residues, the fourth Fe with a free coordination site may
CC bind a small ligand, such as exogenous sulfide, thus acting as a sulfur
CC carrier. {ECO:0000269|PubMed:28655838};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:28655838};
CC -!- PATHWAY: tRNA modification. {ECO:0000269|PubMed:28655838}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:28655838}.
CC -!- MISCELLANEOUS: In TtuA from T.thermophilus, the sulfur inserted into
CC the nucleoside comes from the C-terminal thiocarboxylate of TtuB, but
CC there is no TtuB ortholog in T.maritima. {ECO:0000305}.
CC -!- MISCELLANEOUS: The thiolation reaction likely consists of two steps: a
CC first activation step by ATP to form an adenylated intermediate of the
CC target base of tRNA, and a second nucleophilic substitution step of the
CC sulfur (S) atom supplied by the hydrosulfide attached to the Fe-S
CC cluster. {ECO:0000305|PubMed:28655838}.
CC -!- SIMILARITY: Belongs to the TtcA family. TtuA subfamily. {ECO:0000305}.
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DR EMBL; AE000512; AAD35289.1; -; Genomic_DNA.
DR PIR; E72407; E72407.
DR RefSeq; NP_228012.1; NC_000853.1.
DR RefSeq; WP_004082849.1; NZ_CP011107.1.
DR AlphaFoldDB; Q9WY40; -.
DR SMR; Q9WY40; -.
DR STRING; 243274.THEMA_03745; -.
DR EnsemblBacteria; AAD35289; AAD35289; TM_0197.
DR KEGG; tma:TM0197; -.
DR PATRIC; fig|243274.17.peg.194; -.
DR eggNOG; COG0037; Bacteria.
DR InParanoid; Q9WY40; -.
DR OMA; MNLDQKQ; -.
DR OrthoDB; 1051352at2; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0002144; C:cytosolic tRNA wobble base thiouridylase complex; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0002143; P:tRNA wobble position uridine thiolation; IBA:GO_Central.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR011063; TilS/TtcA_N.
DR InterPro; IPR035107; tRNA_thiolation_TtcA_Ctu1.
DR InterPro; IPR020554; UPF0021_CS.
DR Pfam; PF01171; ATP_bind_3; 1.
DR PIRSF; PIRSF004976; ATPase_YdaO; 1.
DR PROSITE; PS01263; UPF0021; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; ATP-binding; Iron; Iron-sulfur; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; RNA-binding; Transferase;
KW tRNA processing; tRNA-binding; Zinc.
FT CHAIN 1..304
FT /note="tRNA-5-methyluridine(54) 2-sulfurtransferase"
FT /id="PRO_0000442362"
FT BINDING 3
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O58038"
FT BINDING 6
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O58038"
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O58038"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O58038"
FT BINDING 53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O58038"
FT BINDING 79
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O58038"
FT BINDING 131
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:O58038"
FT BINDING 134
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:O58038"
FT BINDING 138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O58038"
FT BINDING 157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O58038"
FT BINDING 224
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:O58038"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O58038"
FT BINDING 277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O58038"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O58038"
FT BINDING 289
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O58038"
SQ SEQUENCE 304 AA; 34934 MW; FBDC135106A00DD5 CRC64;
MKCTKCGKPA SVKLRHYNIK LCKEHFNEFI EQRVEKAIKK FKMFGRNSKI LIAVSGGKDS
VSLWHMLKKL GYEVDALFIR AGKSGMVQKA QEIVEKNAEL LNTKLHIVDA TEYFGGLSTQ
EISIMLRRPV CSICGVVRRY LMNKFAYENG YDVVVTGHNL NDEASVLLGN ILHWQEGYLE
RQWPLLPKTH EKLVPKAKPL VLNYEEDIKL YATLNEIPHL EMACPFSVGA TSLVYKKILR
ELEEEQPGIT LNFYLGFLKR KKEPKFEVEG LRECKECGYP TTAEVCSFCR LRKQVEKRKN
KTPA
