TSAE_SYNY3
ID TSAE_SYNY3 Reviewed; 157 AA.
AC P74415;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaE;
DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaE;
GN Name=tsaE; OrderedLocusNames=sll0257;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
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; BA000022; BAA18515.1; -; Genomic_DNA.
DR PIR; S76256; S76256.
DR AlphaFoldDB; P74415; -.
DR SMR; P74415; -.
DR STRING; 1148.1653602; -.
DR PaxDb; P74415; -.
DR EnsemblBacteria; BAA18515; BAA18515; BAA18515.
DR KEGG; syn:sll0257; -.
DR eggNOG; COG0802; Bacteria.
DR InParanoid; P74415; -.
DR OMA; FTDDAIC; -.
DR PhylomeDB; P74415; -.
DR Proteomes; UP000001425; 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; IBA:GO_Central.
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..157
FT /note="tRNA threonylcarbamoyladenosine biosynthesis protein
FT TsaE"
FT /id="PRO_0000096219"
FT BINDING 40..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 44
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 157 AA; 17735 MW; 4D53F1879D1C8F1F CRC64;
MNENSMEFFL PDLNATDQWG QQLAQQLPLG TIILLQGDLG AGKTSLVQGL GRGLGITGEI
VSPTFTIVNE YREGKMPLYH LDLYRLNTLE VEYLYPEQYW QGEDFPLGIT AVEWPERLPQ
LPSQYLQIQL CHQGEGRSIA LTAQDWAMDL KELLPPS
