ID   TSAE_MYCTO              Reviewed;         168 AA.
AC   P9WFS6; L0TCQ3; P67171; Q50706;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaE;
DE   AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaE;
GN   Name=tsaE; OrderedLocusNames=MT3531;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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 TsaD and TsaB. TsaE seems to play an indirect role in the
CC       t(6)A biosynthesis pathway, possibly in regulating the core enzymatic
CC       function of TsaD (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TsaE family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK47869.1; -; Genomic_DNA.
DR   PIR; C70738; C70738.
DR   RefSeq; WP_003418042.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WFS6; -.
DR   SMR; P9WFS6; -.
DR   EnsemblBacteria; AAK47869; AAK47869; MT3531.
DR   KEGG; mtc:MT3531; -.
DR   PATRIC; fig|83331.31.peg.3788; -.
DR   HOGENOM; CLU_087829_1_1_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003442; T6A_TsaE.
DR   Pfam; PF02367; TsaE; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00150; T6A_YjeE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Magnesium; Metal-binding; Nucleotide-binding;
KW   tRNA processing.
FT   CHAIN           1..168
FT                   /note="tRNA threonylcarbamoyladenosine biosynthesis protein
FT                   TsaE"
FT                   /id="PRO_0000428485"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         54..59
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         58
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         132
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   168 AA;  18214 MW;  625F08C7BE52CCA0 CRC64;
     MSREGIRRRP KARAGLTGGG TATLPRVEDT LTLGSRLGEQ LCAGDVVVLS GPLGAGKTVL
     AKGIAMAMDV EGPITSPTFV LARMHRPRRP GTPAMVHVDV YRLLDHNSAD LLSELDSLDL
     DTDLEDAVVV VEWGEGLAER LSQRHLDVRL ERVSHSDTRI ATWSWGRS