TSAD_BACSU
ID TSAD_BACSU Reviewed; 346 AA.
AC O05518;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase {ECO:0000255|HAMAP-Rule:MF_01445};
DE EC=2.3.1.234 {ECO:0000255|HAMAP-Rule:MF_01445};
DE AltName: Full=N6-L-threonylcarbamoyladenine synthase {ECO:0000255|HAMAP-Rule:MF_01445};
DE Short=t(6)A synthase {ECO:0000255|HAMAP-Rule:MF_01445};
DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaD {ECO:0000255|HAMAP-Rule:MF_01445};
DE AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaD {ECO:0000255|HAMAP-Rule:MF_01445};
GN Name=tsaD {ECO:0000255|HAMAP-Rule:MF_01445}; Synonyms=gcp, ydiE;
GN OrderedLocusNames=BSU05940;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=9202461; DOI=10.1099/00221287-143-6-1861;
RA Sadaie Y., Yata K., Fujita M., Sagai H., Itaya M., Kasahara Y.,
RA Ogasawara N.;
RT "Nucleotide sequence and analysis of the phoB-rrnE-groESL region of the
RT Bacillus subtilis chromosome.";
RL Microbiology 143:1861-1866(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION, SUBUNIT, AND TSAB REQUIREMENT.
RC STRAIN=168;
RX PubMed=21285948; DOI=10.1038/emboj.2010.363;
RA El Yacoubi B., Hatin I., Deutsch C., Kahveci T., Rousset J.P.,
RA Iwata-Reuyl D., Murzin A.G., de Crecy-Lagard V.;
RT "A role for the universal Kae1/Qri7/YgjD (COG0533) family in tRNA
RT modification.";
RL EMBO J. 30:882-893(2011).
RN [4]
RP FUNCTION.
RC STRAIN=168;
RX PubMed=23072323; DOI=10.1021/bi301233d;
RA Lauhon C.T.;
RT "Mechanism of N6-threonylcarbamoyladenosine (t(6)A) biosynthesis: isolation
RT and characterization of the intermediate threonylcarbamoyl-AMP.";
RL Biochemistry 51:8950-8963(2012).
CC -!- FUNCTION: Required for the formation of a threonylcarbamoyl group on
CC adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning
CC with adenine. Is involved in the transfer of the threonylcarbamoyl
CC moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37,
CC together with TsaE and TsaB; this reaction does not require ATP in
CC vitro. TsaD likely plays a direct catalytic role in this reaction.
CC {ECO:0000269|PubMed:21285948, ECO:0000269|PubMed:23072323}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP +
CC H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA;
CC Xref=Rhea:RHEA:37059, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10163,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:73682, ChEBI:CHEBI:74411,
CC ChEBI:CHEBI:74418, ChEBI:CHEBI:456215; EC=2.3.1.234;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01445};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01445};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01445};
CC -!- SUBUNIT: May form a heterodimer with TsaB.
CC {ECO:0000269|PubMed:21285948}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01445}.
CC -!- MISCELLANEOUS: The four proteins YwlC, TsaD, TsaB and TsaE are
CC necessary and sufficient for tRNA(NNU) t(6)A37
CC threonylcarbamoyladenosine biosynthesis in vitro in B.subtilis.
CC {ECO:0000305|PubMed:23072323}.
CC -!- SIMILARITY: Belongs to the KAE1 / TsaD family. {ECO:0000255|HAMAP-
CC Rule:MF_01445}.
CC -!- CAUTION: The well-known t(6)A modification appears to be a hydrolyzed
CC artifact of natural cyclic t(6)A (ct(6)A) that occurs during the
CC preparation and handling of tRNA in B.subtilis and many other species
CC (PubMed:23242255). In these species, the t(6)A modification is
CC processed further by dehydration into ct(6)A, a reaction catalyzed by
CC TcdA. {ECO:0000305}.
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DR EMBL; D88802; BAA19718.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12413.1; -; Genomic_DNA.
DR PIR; F69786; F69786.
DR RefSeq; NP_388475.1; NC_000964.3.
DR RefSeq; WP_003244138.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; O05518; -.
DR SMR; O05518; -.
DR STRING; 224308.BSU05940; -.
DR jPOST; O05518; -.
DR PaxDb; O05518; -.
DR PRIDE; O05518; -.
DR EnsemblBacteria; CAB12413; CAB12413; BSU_05940.
DR GeneID; 938020; -.
DR KEGG; bsu:BSU05940; -.
DR PATRIC; fig|224308.179.peg.639; -.
DR eggNOG; COG0533; Bacteria.
DR InParanoid; O05518; -.
DR OMA; HLEGHIY; -.
DR PhylomeDB; O05518; -.
DR BioCyc; BSUB:BSU05940-MON; -.
DR BRENDA; 2.3.1.234; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0061711; F:N(6)-L-threonylcarbamoyladenine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IDA:UniProtKB.
DR HAMAP; MF_01445; TsaD; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000905; Gcp-like_dom.
DR InterPro; IPR017861; KAE1/TsaD.
DR InterPro; IPR017860; Peptidase_M22_CS.
DR InterPro; IPR022450; TsaD.
DR PANTHER; PTHR11735; PTHR11735; 1.
DR PANTHER; PTHR11735:SF6; PTHR11735:SF6; 1.
DR Pfam; PF00814; TsaD; 1.
DR PRINTS; PR00789; OSIALOPTASE.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR00329; gcp_kae1; 1.
DR TIGRFAMs; TIGR03723; T6A_TsaD_YgjD; 1.
DR PROSITE; PS01016; GLYCOPROTEASE; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Iron; Metal-binding; Reference proteome;
KW Transferase; tRNA processing.
FT CHAIN 1..346
FT /note="tRNA N6-adenosine threonylcarbamoyltransferase"
FT /id="PRO_0000096957"
FT BINDING 117
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT BINDING 121
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT BINDING 139..143
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT BINDING 278
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT BINDING 307
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
SQ SEQUENCE 346 AA; 36842 MW; 0C7F1618780DBA1A CRC64;
MSEQKDMYVL GIETSCDETA AAIVKNGKEI ISNVVASQIE SHKRFGGVVP EIASRHHVEQ
ITLVIEEAFR KAGMTYSDID AIAVTEGPGL VGALLIGVNA AKALSFAYNI PLVGVHHIAG
HIYANRLVED IVFPALALVV SGGHTELVYM KEHGSFEVIG ETLDDAAGEA YDKVARTMGL
PYPGGPQIDK LAEKGNDNIP LPRAWLEEGS YNFSFSGLKS AVINTLHNAS QKGQEIAPED
LSASFQNSVI DVLVTKTARA AKEYDVKQVL LAGGVAANRG LRAALEKEFA QHEGITLVIP
PLALCTDNAA MIAAAGTIAF EKGIRGAYDM NGQPGLELTS YQSLTR
