TSAC_ECOLI
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 03-AUG-2022, entry version 161.
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; Proteobacteria; 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 and 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; P45748; -.
DR PRIDE; P45748; -.
DR EnsemblBacteria; AAC76307; AAC76307; b3282.
DR EnsemblBacteria; BAE78009; BAE78009; BAE78009.
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 PhylomeDB; P45748; -.
DR BioCyc; EcoCyc:G7698-MON; -.
DR BioCyc; MetaCyc:G7698-MON; -.
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 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 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
