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P0A8M3 (SYT_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Threonine--tRNA ligase

EC=6.1.1.3
Alternative name(s):
Threonyl-tRNA synthetase
Short name=ThrRS
Gene names
Name:thrS
Ordered Locus Names:b1719, JW1709
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length642 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

ThrS is also a translational repressor protein, it controls the translation of its own gene by binding to its mRNA. HAMAP-Rule MF_00184

Catalytic activity

ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr). HAMAP-Rule MF_00184

Cofactor

Binds 1 zinc ion per subunit.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00184.

Domain

The C-terminal domain recognizes the anticodon bases but the N-terminal contributes also to the precise recognition of tRNA(Thr) by ThrRS. HAMAP-Rule MF_00184

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

rplAP0A7L02EBI-551254,EBI-543771

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 642642Threonine--tRNA ligase HAMAP-Rule MF_00184
PRO_0000100973

Regions

Region243 – 534292Catalytic HAMAP-Rule MF_00184

Sites

Metal binding3341Zinc; catalytic
Metal binding3851Zinc; catalytic
Metal binding5111Zinc; catalytic

Amino acid modifications

Modified residue2861N6-acetyllysine Ref.7

Experimental info

Mutagenesis3341C → S: Activity very strongly affected.
Mutagenesis3851H → A or N: Activity very strongly affected.
Mutagenesis5111H → A or N: Activity very strongly affected.
Sequence conflict1951H → R in CAA23560. Ref.1

Secondary structure

............................................................................................................. 642
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A8M3 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: 38D8913B19CDAB7B

FASTA64274,014
        10         20         30         40         50         60 
MPVITLPDGS QRHYDHAVSP MDVALDIGPG LAKACIAGRV NGELVDACDL IENDAQLSII 

        70         80         90        100        110        120 
TAKDEEGLEI IRHSCAHLLG HAIKQLWPHT KMAIGPVIDN GFYYDVDLDR TLTQEDVEAL 

       130        140        150        160        170        180 
EKRMHELAEK NYDVIKKKVS WHEARETFAN RGESYKVSIL DENIAHDDKP GLYFHEEYVD 

       190        200        210        220        230        240 
MCRGPHVPNM RFCHHFKLMK TAGAYWRGDS NNKMLQRIYG TAWADKKALN AYLQRLEEAA 

       250        260        270        280        290        300 
KRDHRKIGKQ LDLYHMQEEA PGMVFWHNDG WTIFRELEVF VRSKLKEYQY QEVKGPFMMD 

       310        320        330        340        350        360 
RVLWEKTGHW DNYKDAMFTT SSENREYCIK PMNCPGHVQI FNQGLKSYRD LPLRMAEFGS 

       370        380        390        400        410        420 
CHRNEPSGSL HGLMRVRGFT QDDAHIFCTE EQIRDEVNGC IRLVYDMYST FGFEKIVVKL 

       430        440        450        460        470        480 
STRPEKRIGS DEMWDRAEAD LAVALEENNI PFEYQLGEGA FYGPKIEFTL YDCLDRAWQC 

       490        500        510        520        530        540 
GTVQLDFSLP SRLSASYVGE DNERKVPVMI HRAILGSMER FIGILTEEFA GFFPTWLAPV 

       550        560        570        580        590        600 
QVVIMNITDS QSEYVNELTQ KLSNAGIRVK ADLRNEKIGF KIREHTLRRV PYMLVCGDKE 

       610        620        630        640 
VESGKVAVRT RRGKDLGSMD VNEVIEKLQQ EIRSRSLKQL EE 

« Hide

References

« Hide 'large scale' references
[1]"Structural and transcriptional evidence for related thrS and infC expression."
Mayaux J.-F., Fayat G., Fromant M., Springer M., Grunberg-Manago M., Blanquet S.
Proc. Natl. Acad. Sci. U.S.A. 80:6152-6156(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map."
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. expand/collapse author list , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"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.
[4]"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.
[5]"Genetic definition of the translational operator of the threonine-tRNA ligase gene in Escherichia coli."
Springer M., Graffe M., Butler J.S., Grunberg-Manago M.
Proc. Natl. Acad. Sci. U.S.A. 83:4384-4388(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-47, MECHANISM OF TRANSLATION REGULATION.
[6]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[7]"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-286, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[8]"The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site."
Sankaranarayanan R., Dock-Bregeon A.-C., Romby P., Caillet J., Springer M., Rees B., Ehresmann C., Ehresmann B., Moras D.
Cell 97:371-381(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
[9]"Zinc ion mediated amino acid discrimination by threonyl-tRNA synthetase."
Sankaranarayanan R., Dock-Bregeon A.-C., Rees B., Bovee M., Caillet J., Romby P., Francklyn C.S., Moras D.
Nat. Struct. Biol. 7:461-465(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 242-642.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V00291 Genomic DNA. Translation: CAA23560.1.
U00096 Genomic DNA. Translation: AAC74789.1.
AP009048 Genomic DNA. Translation: BAA15498.1.
M13549 Genomic DNA. Translation: AAA24674.1.
PIRSYECTT. G64930.
RefSeqNP_416234.1. NC_000913.3.
YP_489981.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EVKX-ray2.00A/B242-642[»]
1EVLX-ray1.55A/B/C/D242-642[»]
1FYFX-ray1.65A/B242-642[»]
1KOGX-ray3.50A/B/C/D/E/F/G/H242-642[»]
1QF6X-ray2.90A1-642[»]
1TJEX-ray1.50A1-224[»]
1TKEX-ray1.46A1-224[»]
1TKGX-ray1.50A1-224[»]
1TKYX-ray1.48A1-224[»]
4HWOX-ray1.91A/B242-642[»]
4HWPX-ray1.81A/B242-642[»]
4HWRX-ray1.90A/B242-642[»]
4HWSX-ray1.70A/B242-642[»]
ProteinModelPortalP0A8M3.
SMRP0A8M3. Positions 2-642.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid850582. 1 interaction.
DIPDIP-35823N.
IntActP0A8M3. 49 interactions.
MINTMINT-1229097.
STRING511145.b1719.

Proteomic databases

PaxDbP0A8M3.
PRIDEP0A8M3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74789; AAC74789; b1719.
BAA15498; BAA15498; BAA15498.
GeneID12933199.
946222.
KEGGecj:Y75_p1694.
eco:b1719.
PATRIC32118742. VBIEscCol129921_1789.

Organism-specific databases

EchoBASEEB0994.
EcoGeneEG11001. thrS.

Phylogenomic databases

eggNOGCOG0441.
HOGENOMHOG000003880.
KOK01868.
OMACVGHIKV.
OrthoDBEOG61KBFJ.
PhylomeDBP0A8M3.
ProtClustDBPRK00413.

Enzyme and pathway databases

BioCycEcoCyc:THRS-MONOMER.
ECOL316407:JW1709-MONOMER.
MetaCyc:THRS-MONOMER.
SABIO-RKP0A8M3.

Gene expression databases

GenevestigatorP0A8M3.

Family and domain databases

Gene3D3.10.20.30. 1 hit.
3.40.50.800. 1 hit.
HAMAPMF_00184. Thr_tRNA_synth.
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR012675. Beta-grasp_dom.
IPR004095. TGS.
IPR012676. TGS-like.
IPR002320. Thr-tRNA-ligase_IIa.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view]
PfamPF03129. HGTP_anticodon. 1 hit.
PF02824. TGS. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSPR01047. TRNASYNTHTHR.
SMARTSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMSSF52954. SSF52954. 1 hit.
SSF55186. SSF55186. 1 hit.
SSF81271. SSF81271. 1 hit.
TIGRFAMsTIGR00418. thrS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A8M3.
PROP0A8M3.

Entry information

Entry nameSYT_ECOLI
AccessionPrimary (citable) accession number: P0A8M3
Secondary accession number(s): P00955, P78166, P78241
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 7, 2005
Last modified: April 16, 2014
This is version 92 of the entry and version 1 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

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries