ID   TSAC_YERPN              Reviewed;         190 AA.
AC   Q1CCY0; D1Q2I4;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Threonylcarbamoyl-AMP synthase {ECO:0000255|HAMAP-Rule:MF_01852};
DE            Short=TC-AMP synthase {ECO:0000255|HAMAP-Rule:MF_01852};
DE            EC=2.7.7.87 {ECO:0000255|HAMAP-Rule:MF_01852};
DE   AltName: Full=L-threonylcarbamoyladenylate synthase {ECO:0000255|HAMAP-Rule:MF_01852};
DE   AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaC {ECO:0000255|HAMAP-Rule:MF_01852};
DE   AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaC {ECO:0000255|HAMAP-Rule:MF_01852};
GN   Name=tsaC {ECO:0000255|HAMAP-Rule:MF_01852}; Synonyms=rimN;
GN   OrderedLocusNames=YPN_3823; ORFNames=YP516_4345;
OS   Yersinia pestis bv. Antiqua (strain Nepal516).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=377628;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nepal516;
RX   PubMed=16740952; DOI=10.1128/jb.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA   Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT   evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nepal516;
RA   Plunkett G. III, Anderson B.D., Baumler D.J., Burland V., Cabot E.L.,
RA   Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Munk A.C., Tapia R.,
RA   Green L.D., Rogers Y.C., Detter J.C., Bruce D.C., Brettin T.S.;
RT   "Yersinia pestis Nepal516A whole genome shotgun sequencing project.";
RL   Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
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. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2)
CC       and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate
CC       intermediate, with the release of diphosphate. {ECO:0000255|HAMAP-
CC       Rule:MF_01852}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + L-threonine = diphosphate + H2O + L-
CC         threonylcarbamoyladenylate; Xref=Rhea:RHEA:36407, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57926, ChEBI:CHEBI:73682; EC=2.7.7.87;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01852};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01852}.
CC   -!- SIMILARITY: Belongs to the SUA5 family. TsaC subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01852}.
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DR   EMBL; CP000305; ABG20150.1; -; Genomic_DNA.
DR   EMBL; ACNQ01000019; EEO74737.1; -; Genomic_DNA.
DR   RefSeq; WP_002209025.1; NZ_ACNQ01000019.1.
DR   AlphaFoldDB; Q1CCY0; -.
DR   SMR; Q1CCY0; -.
DR   EnsemblBacteria; ABG20150; ABG20150; YPN_3823.
DR   GeneID; 66843915; -.
DR   KEGG; ypn:YPN_3823; -.
DR   HOGENOM; CLU_031397_6_0_6; -.
DR   OMA; LVDAFWP; -.
DR   Proteomes; UP000008936; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR   GO; GO:0061710; F:L-threonylcarbamoyladenylate synthase; IEA:UniProtKB-EC.
DR   GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01852; TsaC; 1.
DR   InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR   InterPro; IPR023535; TC-AMP_synthase.
DR   InterPro; IPR006070; YrdC-like_dom.
DR   PANTHER; PTHR17490:SF8; PTHR17490:SF8; 1.
DR   Pfam; PF01300; Sua5_yciO_yrdC; 1.
DR   SUPFAM; SSF55821; SSF55821; 1.
DR   PROSITE; PS51163; YRDC; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Nucleotide-binding; Nucleotidyltransferase;
KW   Transferase; tRNA processing.
FT   CHAIN           1..190
FT                   /note="Threonylcarbamoyl-AMP synthase"
FT                   /id="PRO_0000353026"
FT   DOMAIN          7..190
FT                   /note="YrdC-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01852"
SQ   SEQUENCE   190 AA;  21153 MW;  0F2025485617D199 CRC64;
     MNQQENNFVL ADIVRALRQE EVIAYPTEAV FGLGCDPDSE KAVNTLLALK QRPWQKGLIL
     VAANYAQLEP YINDSMLNEI QRETLFSTWP GPITWVIPAR VETPQWLTGC FDSLAVRVSN
     HPLVQQLCAE YGKPLVSTSA NLSGHEPCRT EEEVRIQFGP SLPVLSGHVG GRLNPSEIRD
     ALTGKRFRQG