ID   TSAC_ECOLI              Reviewed;         190 AA.
AC   P45748; Q2M6U7;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   24-JAN-2024, entry version 168.
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=Ribosome maturation factor TsaC;
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, yrdC;
GN   OrderedLocusNames=b3282, JW3243;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=B / BL21;
RX   PubMed=10493123;
RX   DOI=10.1002/(sici)1522-2683(19990801)20:11<2181::aid-elps2181>3.0.co;2-q;
RA   Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.;
RT   "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite
RT   chromatography.";
RL   Electrophoresis 20:2181-2195(1999).
RN   [4]
RP   FUNCTION IN MATURATION OF 16S RRNA.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=15716138; DOI=10.1016/j.bbaexp.2004.11.010;
RA   Kaczanowska M., Ryden-Aulin M.;
RT   "The YrdC protein -- a putative ribosome maturation factor.";
RL   Biochim. Biophys. Acta 1727:87-96(2005).
RN   [5]
RP   FUNCTION, ATP-BINDING, TRNA-BINDING, DISRUPTION PHENOTYPE, AND MUTAGENESIS
RP   OF LYS-50; ARG-52; LYS-56 AND ARG-110.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=19287007; DOI=10.1093/nar/gkp152;
RA   El Yacoubi B., Lyons B., Cruz Y., Reddy R., Nordin B., Agnelli F.,
RA   Williamson J.R., Schimmel P., Swairjo M.A., de Crecy-Lagard V.;
RT   "The universal YrdC/Sua5 family is required for the formation of
RT   threonylcarbamoyladenosine in tRNA.";
RL   Nucleic Acids Res. 37:2894-2909(2009).
RN   [6]
RP   FUNCTION.
RC   STRAIN=K12;
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   [7]
RP   PROPOSED FUNCTION AS A THREONYLCARBAMOYLTRANSFERASE, TRNA-BINDING,
RP   ATP-BINDING, AND THREONINE-BINDING.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=21775474; DOI=10.1261/rna.2592411;
RA   Harris K.A., Jones V., Bilbille Y., Swairjo M.A., Agris P.F.;
RT   "YrdC exhibits properties expected of a subunit for a tRNA
RT   threonylcarbamoyl transferase.";
RL   RNA 17:1678-1687(2011).
RN   [8]
RP   FUNCTION AS A TC-AMP SYNTHASE, CATALYTIC ACTIVITY, AND KINETIC PARAMETERS.
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).
RN   [9]
RP   FUNCTION IN T(6)A37 FORMATION, GENE NAME, AND INTERACTION WITH TSAB AND
RP   TSAD.
RC   STRAIN=K12;
RX   PubMed=22378793; DOI=10.1074/jbc.m112.344028;
RA   Deutsch C., El Yacoubi B., de Crecy-Lagard V., Iwata-Reuyl D.;
RT   "Biosynthesis of threonylcarbamoyl adenosine (t6A), a universal tRNA
RT   nucleoside.";
RL   J. Biol. Chem. 287:13666-13673(2012).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND RNA-BINDING.
RX   PubMed=11206077; DOI=10.1110/ps.9.12.2557;
RA   Teplova M., Tereshko V., Sanishvili R., Joachimiak A., Bushueva T.,
RA   Anderson W.F., Egli M.;
RT   "The structure of the yrdC gene product from Escherichia coli reveals a new
RT   fold and suggests a role in RNA binding.";
RL   Protein Sci. 9:2557-2566(2000).
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. Is also able to catalyze
CC       the reverse reaction in vitro, i.e. the formation of ATP from TC-AMP
CC       and PPi. Shows higher affinity for the full-length tRNA(Thr) lacking
CC       only the t(6)A37 modification than for its fully modified counterpart.
CC       Could also be required for the maturation of 16S rRNA. Binds to double-
CC       stranded RNA but does not interact tightly with either of the ribosomal
CC       subunits, or the 70S particles. {ECO:0000255|HAMAP-Rule:MF_01852,
CC       ECO:0000269|PubMed:15716138, ECO:0000269|PubMed:19287007,
CC       ECO:0000269|PubMed:21285948, ECO:0000269|PubMed:22378793,
CC       ECO:0000269|PubMed:23072323}.
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         ECO:0000269|PubMed:23072323};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=93 uM for ATP {ECO:0000269|PubMed:23072323};
CC         KM=0.68 uM for L-threonylcarbamoyl-AMP {ECO:0000269|PubMed:23072323};
CC         Note=kcat is 0.10 sec(-1) for ATP-dependent TC-AMP formation and 20
CC         sec(-1) for the reverse reaction.;
CC   -!- SUBUNIT: Interacts with TsaB and TsaD. {ECO:0000269|PubMed:22378793}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01852}.
CC   -!- DISRUPTION PHENOTYPE: The knockdown of this gene results in a loss of
CC       t(6)A37 modification in tRNAs. {ECO:0000269|PubMed:19287007}.
CC   -!- MISCELLANEOUS: TsaBCDE are necessary and sufficient for tRNA(NNU)
CC       t(6)A37 threonylcarbamoyladenosine modification in vitro in E.coli.
CC       {ECO:0000305|PubMed:22378793}.
CC   -!- MISCELLANEOUS: Unlike previously thought, the formation of TC-AMP does
CC       not proceed via an ATP-activated HCO(3)(-) intermediate such as
CC       carboxy-AMP. {ECO:0000305|PubMed:23072323}.
CC   -!- SIMILARITY: Belongs to the SUA5 family. TsaC subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01852}.
CC   -!- CAUTION: Was also proposed to catalyze the transfer of the
CC       threonylcarbamoyl moiety of TC-AMP to the N6 group of A37
CC       (PubMed:21285948, PubMed:21775474). However, it was shown that this
CC       reaction is catalyzed in B.subtilis by the TsaEBD proteins
CC       (PubMed:23072323). {ECO:0000305|PubMed:23072323}.
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 E.coli 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA58079.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U18997; AAA58079.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; U00096; AAC76307.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE78009.1; -; Genomic_DNA.
DR   PIR; E65120; E65120.
DR   RefSeq; NP_417741.1; NC_000913.3.
DR   RefSeq; WP_001301412.1; NZ_SSZK01000040.1.
DR   PDB; 1HRU; X-ray; 2.00 A; A/B=1-188.
DR   PDB; 2MX1; NMR; -; A=2-190.
DR   PDBsum; 1HRU; -.
DR   PDBsum; 2MX1; -.
DR   AlphaFoldDB; P45748; -.
DR   SMR; P45748; -.
DR   BioGRID; 4262454; 224.
DR   DIP; DIP-12916N; -.
DR   IntAct; P45748; 12.
DR   STRING; 511145.b3282; -.
DR   jPOST; P45748; -.
DR   PaxDb; 511145-b3282; -.
DR   EnsemblBacteria; AAC76307; AAC76307; b3282.
DR   GeneID; 947783; -.
DR   KEGG; ecj:JW3243; -.
DR   KEGG; eco:b3282; -.
DR   PATRIC; fig|1411691.4.peg.3449; -.
DR   EchoBASE; EB2689; -.
DR   eggNOG; COG0009; Bacteria.
DR   HOGENOM; CLU_031397_6_0_6; -.
DR   InParanoid; P45748; -.
DR   OMA; LVDAFWP; -.
DR   OrthoDB; 9814580at2; -.
DR   PhylomeDB; P45748; -.
DR   BioCyc; EcoCyc:G7698-MONOMER; -.
DR   BioCyc; MetaCyc:G7698-MONOMER; -.
DR   BRENDA; 2.7.7.87; 2026.
DR   EvolutionaryTrace; P45748; -.
DR   PRO; PR:P45748; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IDA:EcoCyc.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0005524; F:ATP binding; IDA:EcoCyc.
DR   GO; GO:0003725; F:double-stranded RNA binding; IDA:EcoCyc.
DR   GO; GO:0061710; F:L-threonylcarbamoyladenylate synthase; IDA:EcoCyc.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0000049; F:tRNA binding; IDA:EcoCyc.
DR   GO; GO:0006450; P:regulation of translational fidelity; IBA:GO_Central.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IDA:EcoCyc.
DR   Gene3D; 3.90.870.10; DHBP synthase; 1.
DR   HAMAP; MF_01852; TsaC; 1.
DR   InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR   InterPro; IPR006070; Sua5-like_dom.
DR   InterPro; IPR023535; TC-AMP_synthase.
DR   PANTHER; PTHR17490; SUA5; 1.
DR   PANTHER; PTHR17490:SF18; THREONYLCARBAMOYL-AMP SYNTHASE; 1.
DR   Pfam; PF01300; Sua5_yciO_yrdC; 1.
DR   SUPFAM; SSF55821; YrdC/RibB; 1.
DR   PROSITE; PS51163; YRDC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cytoplasm; Nucleotide-binding;
KW   Nucleotidyltransferase; Reference proteome; Ribosome biogenesis;
KW   RNA-binding; rRNA processing; Transferase; tRNA processing; tRNA-binding.
FT   CHAIN           1..190
FT                   /note="Threonylcarbamoyl-AMP synthase"
FT                   /id="PRO_0000202018"
FT   DOMAIN          7..190
FT                   /note="YrdC-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01852"
FT   MUTAGEN         50
FT                   /note="K->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:19287007"
FT   MUTAGEN         52
FT                   /note="R->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:19287007"
FT   MUTAGEN         56
FT                   /note="K->A: No change in activity."
FT                   /evidence="ECO:0000269|PubMed:19287007"
FT   MUTAGEN         110
FT                   /note="R->A: No change in activity."
FT                   /evidence="ECO:0000269|PubMed:19287007"
FT   HELIX           4..18
FT                   /evidence="ECO:0007829|PDB:1HRU"
FT   STRAND          23..26
FT                   /evidence="ECO:0007829|PDB:1HRU"
FT   STRAND          28..35
FT                   /evidence="ECO:0007829|PDB:1HRU"
FT   HELIX           40..50
FT                   /evidence="ECO:0007829|PDB:1HRU"
FT   HELIX           54..56
FT                   /evidence="ECO:0007829|PDB:1HRU"
FT   STRAND          59..64
FT                   /evidence="ECO:0007829|PDB:1HRU"
FT   HELIX           65..68
FT                   /evidence="ECO:0007829|PDB:1HRU"
FT   HELIX           69..71
FT                   /evidence="ECO:0007829|PDB:1HRU"
FT   TURN            74..76
FT                   /evidence="ECO:0007829|PDB:2MX1"
FT   HELIX           79..86
FT                   /evidence="ECO:0007829|PDB:1HRU"
FT   STRAND          90..98
FT                   /evidence="ECO:0007829|PDB:1HRU"
FT   STRAND          101..103
FT                   /evidence="ECO:0007829|PDB:2MX1"
FT   HELIX           105..108
FT                   /evidence="ECO:0007829|PDB:1HRU"
FT   STRAND          111..118
FT                   /evidence="ECO:0007829|PDB:1HRU"
FT   HELIX           122..131
FT                   /evidence="ECO:0007829|PDB:1HRU"
FT   STRAND          135..140
FT                   /evidence="ECO:0007829|PDB:1HRU"
FT   STRAND          143..145
FT                   /evidence="ECO:0007829|PDB:2MX1"
FT   HELIX           151..158
FT                   /evidence="ECO:0007829|PDB:1HRU"
FT   STRAND          161..164
FT                   /evidence="ECO:0007829|PDB:2MX1"
FT   STRAND          177..180
FT                   /evidence="ECO:0007829|PDB:1HRU"
FT   TURN            181..183
FT                   /evidence="ECO:0007829|PDB:1HRU"
FT   STRAND          184..186
FT                   /evidence="ECO:0007829|PDB:1HRU"
SQ   SEQUENCE   190 AA;  20768 MW;  4DCAAA8873FAB56F CRC64;
     MNNNLQRDAI AAAIDVLNEE RVIAYPTEAV FGVGCDPDSE TAVMRLLELK QRPVDKGLIL
     IAANYEQLKP YIDDTMLTDV QRETIFSRWP GPVTFVFPAP ATTPRWLTGR FDSLAVRVTD
     HPLVVALCQA YGKPLVSTSA NLSGLPPCRT VDEVRAQFGA AFPVVPGETG GRLNPSEIRD
     ALTGELFRQG
//