Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P45748

- TSAC_ECOLI

UniProt

P45748 - TSAC_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Threonylcarbamoyl-AMP synthase

Gene

tsaC

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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 – 1815Combined sources
Beta strandi23 – 264Combined sources
Beta strandi28 – 358Combined sources
Helixi40 – 5011Combined sources
Helixi54 – 563Combined sources
Beta strandi59 – 646Combined sources
Helixi65 – 684Combined sources
Helixi69 – 713Combined sources
Helixi79 – 868Combined sources
Beta strandi90 – 989Combined sources
Helixi105 – 1084Combined sources
Beta strandi111 – 1188Combined sources
Helixi122 – 13110Combined sources
Beta strandi135 – 1406Combined sources
Helixi151 – 1588Combined sources
Beta strandi177 – 1804Combined sources
Turni181 – 1833Combined sources
Beta strandi184 – 1863Combined sources

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.
InParanoidiP45748.
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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNNNLQRDAI AAAIDVLNEE RVIAYPTEAV FGVGCDPDSE TAVMRLLELK
60 70 80 90 100
QRPVDKGLIL IAANYEQLKP YIDDTMLTDV QRETIFSRWP GPVTFVFPAP
110 120 130 140 150
ATTPRWLTGR FDSLAVRVTD HPLVVALCQA YGKPLVSTSA NLSGLPPCRT
160 170 180 190
VDEVRAQFGA AFPVVPGETG GRLNPSEIRD ALTGELFRQG
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.
InParanoidi P45748.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 116 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