ID   TSAE_RICPR              Reviewed;         144 AA.
AC   Q9ZED0;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaE;
DE   AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaE;
GN   Name=tsaE; OrderedLocusNames=RP013;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
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; AJ235270; CAA14485.1; -; Genomic_DNA.
DR   PIR; F71708; F71708.
DR   RefSeq; NP_220408.1; NC_000963.1.
DR   RefSeq; WP_004596691.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZED0; -.
DR   SMR; Q9ZED0; -.
DR   STRING; 272947.RP013; -.
DR   EnsemblBacteria; CAA14485; CAA14485; CAA14485.
DR   GeneID; 57569141; -.
DR   KEGG; rpr:RP013; -.
DR   PATRIC; fig|272947.5.peg.13; -.
DR   eggNOG; COG0802; Bacteria.
DR   HOGENOM; CLU_087829_5_0_5; -.
DR   OMA; FTDDAIC; -.
DR   Proteomes; UP000002480; 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   Reference proteome; tRNA processing.
FT   CHAIN           1..144
FT                   /note="tRNA threonylcarbamoyladenosine biosynthesis protein
FT                   TsaE"
FT                   /id="PRO_0000096217"
FT   BINDING         34..39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         38
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   144 AA;  16862 MW;  4EDEF0133AB83698 CRC64;
     MHTLNSKKET KNFAKLFAQN LKPNDIVLLN GDLGAGKTFF CREIIKHFCG KNTNIISPTF
     NLLQIYKTPK FNIYHYDMYR IKSPEEIYEL GFEEALNGNL ILIEWSEIIK HLLTPPLIEV
     NLKVLDNNKR LCSIHKENFL FDFL