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Protein

Threonine--tRNA ligase

Gene

thrS

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

Functioni

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

Catalytic activityi

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

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi334Zinc; catalytic1
Metal bindingi385Zinc; catalytic1
Metal bindingi511Zinc; catalytic1

GO - Molecular functioni

  • ATP binding Source: EcoliWiki
  • drug binding Source: EcoliWiki
  • ligase activity, forming aminoacyl-tRNA and related compounds Source: EcoliWiki
  • RNA binding Source: EcoliWiki
  • threonine-tRNA ligase activity Source: EcoCyc
  • translation repressor activity, nucleic acid binding Source: EcoCyc
  • zinc ion binding Source: EcoliWiki

GO - Biological processi

  • negative regulation of translational initiation Source: EcoCyc
  • threonyl-tRNA aminoacylation Source: EcoCyc
  • tRNA aminoacylation Source: EcoliWiki
  • tRNA aminoacylation for protein translation Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase, Repressor

Keywords - Biological processi

Protein biosynthesis, Translation regulation

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:THRS-MONOMER.
ECOL316407:JW1709-MONOMER.
MetaCyc:THRS-MONOMER.
BRENDAi6.1.1.3. 2026.

Protein family/group databases

MoonProtiP0A8M3.

Names & Taxonomyi

Protein namesi
Recommended name:
Threonine--tRNA ligase (EC:6.1.1.3)
Alternative name(s):
Threonyl-tRNA synthetase
Short name:
ThrRS
Gene namesi
Name:thrS
Ordered Locus Names:b1719, JW1709
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11001. thrS.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoliWiki
  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi334C → S: Activity very strongly affected. 1
Mutagenesisi385H → A or N: Activity very strongly affected. 1
Mutagenesisi511H → A or N: Activity very strongly affected. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001009731 – 642Threonine--tRNA ligaseAdd BLAST642

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei286N6-acetyllysine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP0A8M3.
PaxDbiP0A8M3.
PRIDEiP0A8M3.

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
rplAP0A7L02EBI-551254,EBI-543771

Protein-protein interaction databases

BioGridi4262193. 16 interactors.
850582. 1 interactor.
DIPiDIP-35823N.
IntActiP0A8M3. 49 interactors.
MINTiMINT-1229097.
STRINGi511145.b1719.

Structurei

Secondary structure

1642
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 5Combined sources3
Beta strandi11 – 13Combined sources3
Helixi20 – 27Combined sources8
Helixi29 – 34Combined sources6
Beta strandi37 – 40Combined sources4
Beta strandi43 – 46Combined sources4
Beta strandi55 – 60Combined sources6
Helixi65 – 86Combined sources22
Beta strandi101 – 107Combined sources7
Helixi114 – 128Combined sources15
Beta strandi135 – 138Combined sources4
Helixi141 – 150Combined sources10
Helixi154 – 163Combined sources10
Beta strandi171 – 175Combined sources5
Beta strandi178 – 183Combined sources6
Helixi190 – 192Combined sources3
Beta strandi196 – 205Combined sources10
Helixi206 – 208Combined sources3
Beta strandi214 – 222Combined sources9
Helixi226 – 240Combined sources15
Helixi244 – 250Combined sources7
Helixi268 – 287Combined sources20
Beta strandi297 – 300Combined sources4
Helixi301 – 306Combined sources6
Helixi309 – 312Combined sources4
Helixi314 – 316Combined sources3
Beta strandi319 – 322Combined sources4
Beta strandi325 – 329Combined sources5
Beta strandi331 – 333Combined sources3
Helixi334 – 341Combined sources8
Helixi348 – 350Combined sources3
Beta strandi352 – 362Combined sources11
Helixi367 – 369Combined sources3
Turni372 – 374Combined sources3
Beta strandi377 – 388Combined sources12
Helixi390 – 392Combined sources3
Helixi393 – 409Combined sources17
Turni410 – 412Combined sources3
Beta strandi417 – 421Combined sources5
Helixi431 – 447Combined sources17
Beta strandi453 – 455Combined sources3
Beta strandi461 – 463Combined sources3
Beta strandi465 – 471Combined sources7
Beta strandi477 – 488Combined sources12
Helixi489 – 492Combined sources4
Beta strandi502 – 505Combined sources4
Beta strandi508 – 517Combined sources10
Helixi518 – 529Combined sources12
Turni535 – 537Combined sources3
Beta strandi542 – 548Combined sources7
Helixi549 – 551Combined sources3
Helixi552 – 564Combined sources13
Beta strandi569 – 572Combined sources4
Beta strandi574 – 576Combined sources3
Helixi578 – 587Combined sources10
Beta strandi591 – 596Combined sources6
Helixi598 – 603Combined sources6
Beta strandi605 – 610Combined sources6
Beta strandi615 – 620Combined sources6
Helixi621 – 633Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4P3OX-ray2.50A/B242-642[»]
4P3PX-ray2.10A/B242-642[»]
ProteinModelPortaliP0A8M3.
SMRiP0A8M3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A8M3.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni243 – 534CatalyticAdd BLAST292

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C22. Bacteria.
COG0441. LUCA.
HOGENOMiHOG000003880.
InParanoidiP0A8M3.
KOiK01868.
OMAiFYYDFAY.
PhylomeDBiP0A8M3.

Family and domain databases

CDDicd00771. ThrRS_core. 1 hit.
Gene3Di3.10.20.30. 1 hit.
3.40.50.800. 1 hit.
HAMAPiMF_00184. Thr_tRNA_synth. 1 hit.
InterProiIPR002314. aa-tRNA-synt_IIb.
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.
IPR033728. ThrRS_core.
IPR012947. tRNA_SAD.
[Graphical view]
PfamiPF03129. HGTP_anticodon. 1 hit.
PF02824. TGS. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSiPR01047. TRNASYNTHTHR.
SMARTiSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMiSSF52954. SSF52954. 1 hit.
SSF55186. SSF55186. 1 hit.
SSF81271. SSF81271. 1 hit.
TIGRFAMsiTIGR00418. thrS. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A8M3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPVITLPDGS QRHYDHAVSP MDVALDIGPG LAKACIAGRV NGELVDACDL
60 70 80 90 100
IENDAQLSII TAKDEEGLEI IRHSCAHLLG HAIKQLWPHT KMAIGPVIDN
110 120 130 140 150
GFYYDVDLDR TLTQEDVEAL EKRMHELAEK NYDVIKKKVS WHEARETFAN
160 170 180 190 200
RGESYKVSIL DENIAHDDKP GLYFHEEYVD MCRGPHVPNM RFCHHFKLMK
210 220 230 240 250
TAGAYWRGDS NNKMLQRIYG TAWADKKALN AYLQRLEEAA KRDHRKIGKQ
260 270 280 290 300
LDLYHMQEEA PGMVFWHNDG WTIFRELEVF VRSKLKEYQY QEVKGPFMMD
310 320 330 340 350
RVLWEKTGHW DNYKDAMFTT SSENREYCIK PMNCPGHVQI FNQGLKSYRD
360 370 380 390 400
LPLRMAEFGS CHRNEPSGSL HGLMRVRGFT QDDAHIFCTE EQIRDEVNGC
410 420 430 440 450
IRLVYDMYST FGFEKIVVKL STRPEKRIGS DEMWDRAEAD LAVALEENNI
460 470 480 490 500
PFEYQLGEGA FYGPKIEFTL YDCLDRAWQC GTVQLDFSLP SRLSASYVGE
510 520 530 540 550
DNERKVPVMI HRAILGSMER FIGILTEEFA GFFPTWLAPV QVVIMNITDS
560 570 580 590 600
QSEYVNELTQ KLSNAGIRVK ADLRNEKIGF KIREHTLRRV PYMLVCGDKE
610 620 630 640
VESGKVAVRT RRGKDLGSMD VNEVIEKLQQ EIRSRSLKQL EE
Length:642
Mass (Da):74,014
Last modified:June 7, 2005 - v1
Checksum:i38D8913B19CDAB7B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti195H → R in CAA23560 (PubMed:6353409).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00291 Genomic DNA. Translation: CAA23560.1.
U00096 Genomic DNA. Translation: AAC74789.1.
AP009048 Genomic DNA. Translation: BAA15498.1.
M13549 Genomic DNA. Translation: AAA24674.1.
PIRiG64930. SYECTT.
RefSeqiNP_416234.1. NC_000913.3.
WP_001144202.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74789; AAC74789; b1719.
BAA15498; BAA15498; BAA15498.
GeneIDi946222.
KEGGiecj:JW1709.
eco:b1719.
PATRICi32118742. VBIEscCol129921_1789.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00291 Genomic DNA. Translation: CAA23560.1.
U00096 Genomic DNA. Translation: AAC74789.1.
AP009048 Genomic DNA. Translation: BAA15498.1.
M13549 Genomic DNA. Translation: AAA24674.1.
PIRiG64930. SYECTT.
RefSeqiNP_416234.1. NC_000913.3.
WP_001144202.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4P3OX-ray2.50A/B242-642[»]
4P3PX-ray2.10A/B242-642[»]
ProteinModelPortaliP0A8M3.
SMRiP0A8M3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262193. 16 interactors.
850582. 1 interactor.
DIPiDIP-35823N.
IntActiP0A8M3. 49 interactors.
MINTiMINT-1229097.
STRINGi511145.b1719.

Protein family/group databases

MoonProtiP0A8M3.

Proteomic databases

EPDiP0A8M3.
PaxDbiP0A8M3.
PRIDEiP0A8M3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74789; AAC74789; b1719.
BAA15498; BAA15498; BAA15498.
GeneIDi946222.
KEGGiecj:JW1709.
eco:b1719.
PATRICi32118742. VBIEscCol129921_1789.

Organism-specific databases

EchoBASEiEB0994.
EcoGeneiEG11001. thrS.

Phylogenomic databases

eggNOGiENOG4105C22. Bacteria.
COG0441. LUCA.
HOGENOMiHOG000003880.
InParanoidiP0A8M3.
KOiK01868.
OMAiFYYDFAY.
PhylomeDBiP0A8M3.

Enzyme and pathway databases

BioCyciEcoCyc:THRS-MONOMER.
ECOL316407:JW1709-MONOMER.
MetaCyc:THRS-MONOMER.
BRENDAi6.1.1.3. 2026.

Miscellaneous databases

EvolutionaryTraceiP0A8M3.
PROiP0A8M3.

Family and domain databases

CDDicd00771. ThrRS_core. 1 hit.
Gene3Di3.10.20.30. 1 hit.
3.40.50.800. 1 hit.
HAMAPiMF_00184. Thr_tRNA_synth. 1 hit.
InterProiIPR002314. aa-tRNA-synt_IIb.
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.
IPR033728. ThrRS_core.
IPR012947. tRNA_SAD.
[Graphical view]
PfamiPF03129. HGTP_anticodon. 1 hit.
PF02824. TGS. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSiPR01047. TRNASYNTHTHR.
SMARTiSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMiSSF52954. SSF52954. 1 hit.
SSF55186. SSF55186. 1 hit.
SSF81271. SSF81271. 1 hit.
TIGRFAMsiTIGR00418. thrS. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSYT_ECOLI
AccessioniPrimary (citable) accession number: P0A8M3
Secondary accession number(s): P00955, P78166, P78241
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 7, 2005
Last modified: November 2, 2016
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.