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P45748 (TSAC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Threonylcarbamoyl-AMP synthase

Short name=TC-AMP synthase
EC=2.7.7.87
Alternative name(s):
L-threonylcarbamoyladenylate synthase
Ribosome maturation factor TsaC
t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaC
tRNA threonylcarbamoyladenosine biosynthesis protein TsaC
Gene names
Name:tsaC
Synonyms:rimN, yrdC
Ordered Locus Names:b3282, JW3243
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length190 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9

Catalytic activity

L-threonine + ATP + bicarbonate = L-threonylcarbamoyladenylate + diphosphate + H2O. Ref.8

Subunit structure

Interacts with TsaB and TsaD. Ref.9

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_01852.

Disruption phenotype

The knockdown of this gene results in a loss of t6A37 modification in tRNAs. Ref.5

Miscellaneous

TsaBCDE are necessary and sufficient for tRNA(NNU) t6A37 threonylcarbamoyladenosine modification in vitro in E.coli (Ref.9).

Unlike previously thought, the formation of TC-AMP does not proceed via an ATP-activated bicarbonate intermediate such as carboxy-AMP (Ref.8).

Sequence similarities

Belongs to the SUA5 family. TsaC subfamily.

Contains 1 YrdC-like domain.

Caution

Was also proposed to catalyze the transfer of the threonylcarbamoyl moiety of TC-AMP to the N6 group of A37 (Ref.6 and Ref.7). However, it was shown that this reaction is catalyzed in B.subtilis by the TsaEBD proteins (Ref.8).

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.

Biophysicochemical properties

Kinetic parameters:

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

KM=93 µM for ATP Ref.8

KM=0.68 µM for L-threonylcarbamoyl-AMP

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 190190Threonylcarbamoyl-AMP synthase HAMAP-Rule MF_01852
PRO_0000202018

Regions

Domain7 – 190184YrdC-like

Experimental info

Mutagenesis501K → A: Loss of activity. Ref.5
Mutagenesis521R → A: Loss of activity. Ref.5
Mutagenesis561K → A: No change in activity. Ref.5
Mutagenesis1101R → A: No change in activity. Ref.5

Secondary structure

................................. 190
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P45748 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: 4DCAAA8873FAB56F

FASTA19020,768
        10         20         30         40         50         60 
MNNNLQRDAI AAAIDVLNEE RVIAYPTEAV FGVGCDPDSE TAVMRLLELK QRPVDKGLIL 

        70         80         90        100        110        120 
IAANYEQLKP YIDDTMLTDV QRETIFSRWP GPVTFVFPAP ATTPRWLTGR FDSLAVRVTD 

       130        140        150        160        170        180 
HPLVVALCQA YGKPLVSTSA NLSGLPPCRT VDEVRAQFGA AFPVVPGETG GRLNPSEIRD 

       190 
ALTGELFRQG 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U18997 Genomic DNA. Translation: AAA58079.1. Frameshift.
U00096 Genomic DNA. Translation: AAC76307.1.
AP009048 Genomic DNA. Translation: BAE78009.1.
PIRE65120.
RefSeqNP_417741.1. NC_000913.3.
YP_492150.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HRUX-ray2.00A/B1-188[»]
ProteinModelPortalP45748.
SMRP45748. Positions 3-188.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-12916N.
IntActP45748. 12 interactions.
MINTMINT-1230775.
STRING511145.b3282.

Proteomic databases

PaxDbP45748.
PRIDEP45748.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76307; AAC76307; b3282.
BAE78009; BAE78009; BAE78009.
GeneID12933460.
947783.
KEGGecj:Y75_p3894.
eco:b3282.
PATRIC32121998. VBIEscCol129921_3376.

Organism-specific databases

EchoBASEEB2689.
EcoGeneEG12840. tsaC.

Phylogenomic databases

eggNOGCOG0009.
HOGENOMHOG000076163.
KOK07566.
OMAQFGADFP.
OrthoDBEOG6C5RT4.
PhylomeDBP45748.

Enzyme and pathway databases

BioCycEcoCyc:G7698-MONOMER.
ECOL316407:JW3243-MONOMER.

Gene expression databases

GenevestigatorP45748.

Family and domain databases

Gene3D3.90.870.10. 1 hit.
HAMAPMF_01852. TsaC.
InterProIPR017945. DHBP_synth_RibB-like_a/b_dom.
IPR023535. TC-AMP_synthase.
IPR006070. YrdC-like_dom.
[Graphical view]
PfamPF01300. Sua5_yciO_yrdC. 1 hit.
[Graphical view]
SUPFAMSSF55821. SSF55821. 1 hit.
PROSITEPS51163. YRDC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP45748.
PROP45748.

Entry information

Entry nameTSAC_ECOLI
AccessionPrimary (citable) accession number: P45748
Secondary accession number(s): Q2M6U7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: July 15, 1998
Last modified: June 11, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene