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P45748

- TSAC_ECOLI

UniProt

P45748 - TSAC_ECOLI

Protein

Threonylcarbamoyl-AMP synthase

Gene

tsaC

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 2 (15 Jul 1998)
      Previous versions | rss
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    Functioni

    Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t6A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, bicarbonate/CO2 and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of pyrophosphate. Is also able to catalyze the reverse reaction in vitro, i.e. the formation of ATP from TC-AMP and PPi. Shows higher affinity for the full-length tRNA(Thr) lacking only the t6A37 modification than for its fully modified counterpart. Could also be required for the maturation of 16S rRNA. Binds to double-stranded RNA but does not interact tightly with either of the ribosomal subunits, or the 70S particles.5 PublicationsUniRule annotation

    Catalytic activityi

    L-threonine + ATP + bicarbonate = L-threonylcarbamoyladenylate + diphosphate + H2O.1 PublicationUniRule annotation

    Kineticsi

    kcat is 0.10 sec(-1) for ATP-dependent TC-AMP formation and 20 sec(-1) for the reverse reaction.

    1. KM=93 µM for ATP1 Publication
    2. KM=0.68 µM for L-threonylcarbamoyl-AMP1 Publication

    GO - Molecular functioni

    1. ATP binding Source: EcoCyc
    2. double-stranded RNA binding Source: EcoCyc
    3. nucleotidyltransferase activity Source: UniProtKB
    4. tRNA binding Source: EcoCyc

    GO - Biological processi

    1. rRNA processing Source: UniProtKB-KW
    2. threonylcarbamoyladenosine biosynthetic process Source: EcoCyc

    Keywords - Molecular functioni

    Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    Ribosome biogenesis, rRNA processing, tRNA processing

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding, RNA-binding, tRNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:G7698-MONOMER.
    ECOL316407:JW3243-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Threonylcarbamoyl-AMP synthaseUniRule annotation (EC:2.7.7.87UniRule annotation)
    Short name:
    TC-AMP synthaseUniRule annotation
    Alternative name(s):
    L-threonylcarbamoyladenylate synthaseUniRule annotation
    Ribosome maturation factor TsaC
    t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaCUniRule annotation
    tRNA threonylcarbamoyladenosine biosynthesis protein TsaCUniRule annotation
    Gene namesi
    Name:tsaCUniRule annotation
    Synonyms:rimN, yrdC
    Ordered Locus Names:b3282, JW3243
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG12840. tsaC.

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: EcoCyc

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    The knockdown of this gene results in a loss of t6A37 modification in tRNAs.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi50 – 501K → A: Loss of activity. 1 Publication
    Mutagenesisi52 – 521R → A: Loss of activity. 1 Publication
    Mutagenesisi56 – 561K → A: No change in activity. 1 Publication
    Mutagenesisi110 – 1101R → A: No change in activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 190190Threonylcarbamoyl-AMP synthasePRO_0000202018Add
    BLAST

    Proteomic databases

    PaxDbiP45748.
    PRIDEiP45748.

    Expressioni

    Gene expression databases

    GenevestigatoriP45748.

    Interactioni

    Subunit structurei

    Interacts with TsaB and TsaD.1 Publication

    Protein-protein interaction databases

    DIPiDIP-12916N.
    IntActiP45748. 12 interactions.
    MINTiMINT-1230775.
    STRINGi511145.b3282.

    Structurei

    Secondary structure

    1
    190
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 1815
    Beta strandi23 – 264
    Beta strandi28 – 358
    Helixi40 – 5011
    Helixi54 – 563
    Beta strandi59 – 646
    Helixi65 – 684
    Helixi69 – 713
    Helixi79 – 868
    Beta strandi90 – 989
    Helixi105 – 1084
    Beta strandi111 – 1188
    Helixi122 – 13110
    Beta strandi135 – 1406
    Helixi151 – 1588
    Beta strandi177 – 1804
    Turni181 – 1833
    Beta strandi184 – 1863

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HRUX-ray2.00A/B1-188[»]
    ProteinModelPortaliP45748.
    SMRiP45748. Positions 3-188.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP45748.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini7 – 190184YrdC-likeUniRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the SUA5 family. TsaC subfamily.UniRule annotation
    Contains 1 YrdC-like domain.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0009.
    HOGENOMiHOG000076163.
    KOiK07566.
    OMAiQFGADFP.
    OrthoDBiEOG6C5RT4.
    PhylomeDBiP45748.

    Family and domain databases

    Gene3Di3.90.870.10. 1 hit.
    HAMAPiMF_01852. TsaC.
    InterProiIPR017945. DHBP_synth_RibB-like_a/b_dom.
    IPR023535. TC-AMP_synthase.
    IPR006070. YrdC-like_dom.
    [Graphical view]
    PfamiPF01300. Sua5_yciO_yrdC. 1 hit.
    [Graphical view]
    SUPFAMiSSF55821. SSF55821. 1 hit.
    PROSITEiPS51163. YRDC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P45748-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNNNLQRDAI AAAIDVLNEE RVIAYPTEAV FGVGCDPDSE TAVMRLLELK    50
    QRPVDKGLIL IAANYEQLKP YIDDTMLTDV QRETIFSRWP GPVTFVFPAP 100
    ATTPRWLTGR FDSLAVRVTD HPLVVALCQA YGKPLVSTSA NLSGLPPCRT 150
    VDEVRAQFGA AFPVVPGETG GRLNPSEIRD ALTGELFRQG 190
    Length:190
    Mass (Da):20,768
    Last modified:July 15, 1998 - v2
    Checksum:i4DCAAA8873FAB56F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U18997 Genomic DNA. Translation: AAA58079.1. Frameshift.
    U00096 Genomic DNA. Translation: AAC76307.1.
    AP009048 Genomic DNA. Translation: BAE78009.1.
    PIRiE65120.
    RefSeqiNP_417741.1. NC_000913.3.
    YP_492150.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76307; AAC76307; b3282.
    BAE78009; BAE78009; BAE78009.
    GeneIDi12933460.
    947783.
    KEGGiecj:Y75_p3894.
    eco:b3282.
    PATRICi32121998. VBIEscCol129921_3376.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U18997 Genomic DNA. Translation: AAA58079.1 . Frameshift.
    U00096 Genomic DNA. Translation: AAC76307.1 .
    AP009048 Genomic DNA. Translation: BAE78009.1 .
    PIRi E65120.
    RefSeqi NP_417741.1. NC_000913.3.
    YP_492150.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HRU X-ray 2.00 A/B 1-188 [» ]
    ProteinModelPortali P45748.
    SMRi P45748. Positions 3-188.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-12916N.
    IntActi P45748. 12 interactions.
    MINTi MINT-1230775.
    STRINGi 511145.b3282.

    Proteomic databases

    PaxDbi P45748.
    PRIDEi P45748.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76307 ; AAC76307 ; b3282 .
    BAE78009 ; BAE78009 ; BAE78009 .
    GeneIDi 12933460.
    947783.
    KEGGi ecj:Y75_p3894.
    eco:b3282.
    PATRICi 32121998. VBIEscCol129921_3376.

    Organism-specific databases

    EchoBASEi EB2689.
    EcoGenei EG12840. tsaC.

    Phylogenomic databases

    eggNOGi COG0009.
    HOGENOMi HOG000076163.
    KOi K07566.
    OMAi QFGADFP.
    OrthoDBi EOG6C5RT4.
    PhylomeDBi P45748.

    Enzyme and pathway databases

    BioCyci EcoCyc:G7698-MONOMER.
    ECOL316407:JW3243-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P45748.
    PROi P45748.

    Gene expression databases

    Genevestigatori P45748.

    Family and domain databases

    Gene3Di 3.90.870.10. 1 hit.
    HAMAPi MF_01852. TsaC.
    InterProi IPR017945. DHBP_synth_RibB-like_a/b_dom.
    IPR023535. TC-AMP_synthase.
    IPR006070. YrdC-like_dom.
    [Graphical view ]
    Pfami PF01300. Sua5_yciO_yrdC. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55821. SSF55821. 1 hit.
    PROSITEi PS51163. YRDC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    2. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite chromatography."
      Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.
      Electrophoresis 20:2181-2195(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: B / BL21.
    4. "The YrdC protein -- a putative ribosome maturation factor."
      Kaczanowska M., Ryden-Aulin M.
      Biochim. Biophys. Acta 1727:87-96(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MATURATION OF 16S RRNA.
      Strain: K12 / MG1655 / ATCC 47076.
    5. "The universal YrdC/Sua5 family is required for the formation of threonylcarbamoyladenosine in tRNA."
      El Yacoubi B., Lyons B., Cruz Y., Reddy R., Nordin B., Agnelli F., Williamson J.R., Schimmel P., Swairjo M.A., de Crecy-Lagard V.
      Nucleic Acids Res. 37:2894-2909(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ATP-BINDING, TRNA-BINDING, DISRUPTION PHENOTYPE, MUTAGENESIS OF LYS-50; ARG-52; LYS-56 AND ARG-110.
      Strain: K12 / MG1655 / ATCC 47076.
    6. "A role for the universal Kae1/Qri7/YgjD (COG0533) family in tRNA modification."
      El Yacoubi B., Hatin I., Deutsch C., Kahveci T., Rousset J.P., Iwata-Reuyl D., Murzin A.G., de Crecy-Lagard V.
      EMBO J. 30:882-893(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: K12.
    7. "YrdC exhibits properties expected of a subunit for a tRNA threonylcarbamoyl transferase."
      Harris K.A., Jones V., Bilbille Y., Swairjo M.A., Agris P.F.
      RNA 17:1678-1687(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROPOSED FUNCTION AS A THREONYLCARBAMOYLTRANSFERASE, TRNA-BINDING, ATP-BINDING, THREONINE-BINDING.
      Strain: K12 / MG1655 / ATCC 47076.
    8. "Mechanism of N6-threonylcarbamoyladenosine (t(6)A) biosynthesis: isolation and characterization of the intermediate threonylcarbamoyl-AMP."
      Lauhon C.T.
      Biochemistry 51:8950-8963(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A TC-AMP SYNTHASE, CATALYTIC ACTIVITY, KINETIC PARAMETERS.
    9. "Biosynthesis of threonylcarbamoyl adenosine (t6A), a universal tRNA nucleoside."
      Deutsch C., El Yacoubi B., de Crecy-Lagard V., Iwata-Reuyl D.
      J. Biol. Chem. 287:13666-13673(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN T(6)A37 FORMATION, GENE NAME, INTERACTION WITH TSAB AND TSAD.
      Strain: K12.
    10. "The structure of the yrdC gene product from Escherichia coli reveals a new fold and suggests a role in RNA binding."
      Teplova M., Tereshko V., Sanishvili R., Joachimiak A., Bushueva T., Anderson W.F., Egli M.
      Protein Sci. 9:2557-2566(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), RNA-BINDING.

    Entry informationi

    Entry nameiTSAC_ECOLI
    AccessioniPrimary (citable) accession number: P45748
    Secondary accession number(s): Q2M6U7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: July 15, 1998
    Last modified: October 1, 2014
    This is version 115 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    TsaBCDE are necessary and sufficient for tRNA(NNU) t6A37 threonylcarbamoyladenosine modification in vitro in E.coli.1 Publication
    Unlike previously thought, the formation of TC-AMP does not proceed via an ATP-activated bicarbonate intermediate such as carboxy-AMP.1 Publication

    Caution

    Was also proposed to catalyze the transfer of the threonylcarbamoyl moiety of TC-AMP to the N6 group of A37 (PubMed:21285948 and PubMed:21775474). However, it was shown that this reaction is catalyzed in B.subtilis by the TsaEBD proteins (PubMed:23072323).1 Publication
    The well-known t6A modification appears to be a hydrolyzed artifact of natural cyclic t6A (ct6A) that occurs during the preparation and handling of tRNA in E.coli and many other species (PubMed:23242255). In these species, the t6A modification is processed further by dehydration into ct6A, a reaction catalyzed by TcdA.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3