Skip Header

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

P0A8M3

- SYT_ECOLI

UniProt

P0A8M3 - SYT_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

Threonine--tRNA ligase

Gene

thrS

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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

Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi334 – 3341Zinc; catalytic
Metal bindingi385 – 3851Zinc; catalytic
Metal bindingi511 – 5111Zinc; catalytic

GO - Molecular functioni

  1. ATP binding Source: EcoliWiki
  2. drug binding Source: EcoliWiki
  3. ligase activity, forming aminoacyl-tRNA and related compounds Source: EcoliWiki
  4. RNA binding Source: EcoliWiki
  5. threonine-tRNA ligase activity Source: EcoCyc
  6. translation repressor activity, nucleic acid binding Source: EcoCyc
  7. zinc ion binding Source: EcoliWiki

GO - Biological processi

  1. negative regulation of translational initiation Source: EcoCyc
  2. threonyl-tRNA aminoacylation Source: EcoCyc
  3. tRNA aminoacylation Source: EcoliWiki
  4. 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.
SABIO-RKP0A8M3.

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11001. thrS.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi334 – 3341C → S: Activity very strongly affected.
Mutagenesisi385 – 3851H → A or N: Activity very strongly affected.
Mutagenesisi511 – 5111H → A or N: Activity very strongly affected.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 642642Threonine--tRNA ligasePRO_0000100973Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei286 – 2861N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP0A8M3.
PRIDEiP0A8M3.

Expressioni

Gene expression databases

GenevestigatoriP0A8M3.

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

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

Protein-protein interaction databases

BioGridi850582. 1 interaction.
DIPiDIP-35823N.
IntActiP0A8M3. 49 interactions.
MINTiMINT-1229097.
STRINGi511145.b1719.

Structurei

Secondary structure

1
642
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53
Beta strandi11 – 133
Helixi20 – 278
Helixi29 – 346
Beta strandi37 – 404
Beta strandi43 – 464
Beta strandi55 – 606
Helixi65 – 8622
Beta strandi101 – 1077
Helixi114 – 12815
Beta strandi135 – 1384
Helixi141 – 15010
Helixi154 – 16310
Beta strandi171 – 1755
Beta strandi178 – 1836
Helixi190 – 1923
Beta strandi196 – 20510
Helixi206 – 2083
Beta strandi214 – 2229
Helixi226 – 24015
Helixi244 – 2507
Helixi268 – 28720
Beta strandi297 – 3004
Helixi301 – 3066
Helixi309 – 3124
Helixi314 – 3163
Beta strandi319 – 3224
Beta strandi325 – 3295
Beta strandi331 – 3333
Helixi334 – 3418
Helixi348 – 3503
Beta strandi352 – 36211
Helixi367 – 3693
Turni372 – 3743
Beta strandi377 – 38812
Helixi390 – 3923
Helixi393 – 40917
Turni410 – 4123
Beta strandi417 – 4215
Helixi431 – 44717
Beta strandi453 – 4553
Beta strandi461 – 4633
Beta strandi465 – 4717
Beta strandi477 – 48812
Helixi489 – 4924
Beta strandi502 – 5054
Beta strandi508 – 51710
Helixi518 – 52912
Turni535 – 5373
Beta strandi542 – 5487
Helixi549 – 5513
Helixi552 – 56413
Beta strandi569 – 5724
Helixi578 – 58710
Beta strandi591 – 5966
Helixi598 – 6036
Beta strandi605 – 6106
Beta strandi615 – 6206
Helixi621 – 63313

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP0A8M3.
SMRiP0A8M3. Positions 2-642.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A8M3.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni243 – 534292CatalyticAdd
BLAST

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

eggNOGiCOG0441.
HOGENOMiHOG000003880.
InParanoidiP0A8M3.
KOiK01868.
OMAiHFKLQKI.
OrthoDBiEOG61KBFJ.
PhylomeDBiP0A8M3.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
3.40.50.800. 1 hit.
HAMAPiMF_00184. Thr_tRNA_synth.
InterProiIPR002314. 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]
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti195 – 1951H → R in CAA23560. (PubMed:6353409)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
YP_489981.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74789; AAC74789; b1719.
BAA15498; BAA15498; BAA15498.
GeneIDi12933199.
946222.
KEGGiecj:Y75_p1694.
eco:b1719.
PATRICi32118742. VBIEscCol129921_1789.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi G64930. SYECTT.
RefSeqi NP_416234.1. NC_000913.3.
YP_489981.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EVK X-ray 2.00 A/B 242-642 [» ]
1EVL X-ray 1.55 A/B/C/D 242-642 [» ]
1FYF X-ray 1.65 A/B 242-642 [» ]
1KOG X-ray 3.50 A/B/C/D/E/F/G/H 242-642 [» ]
1QF6 X-ray 2.90 A 1-642 [» ]
1TJE X-ray 1.50 A 1-224 [» ]
1TKE X-ray 1.46 A 1-224 [» ]
1TKG X-ray 1.50 A 1-224 [» ]
1TKY X-ray 1.48 A 1-224 [» ]
4HWO X-ray 1.91 A/B 242-642 [» ]
4HWP X-ray 1.81 A/B 242-642 [» ]
4HWR X-ray 1.90 A/B 242-642 [» ]
4HWS X-ray 1.70 A/B 242-642 [» ]
ProteinModelPortali P0A8M3.
SMRi P0A8M3. Positions 2-642.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 850582. 1 interaction.
DIPi DIP-35823N.
IntActi P0A8M3. 49 interactions.
MINTi MINT-1229097.
STRINGi 511145.b1719.

Proteomic databases

PaxDbi P0A8M3.
PRIDEi P0A8M3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74789 ; AAC74789 ; b1719 .
BAA15498 ; BAA15498 ; BAA15498 .
GeneIDi 12933199.
946222.
KEGGi ecj:Y75_p1694.
eco:b1719.
PATRICi 32118742. VBIEscCol129921_1789.

Organism-specific databases

EchoBASEi EB0994.
EcoGenei EG11001. thrS.

Phylogenomic databases

eggNOGi COG0441.
HOGENOMi HOG000003880.
InParanoidi P0A8M3.
KOi K01868.
OMAi HFKLQKI.
OrthoDBi EOG61KBFJ.
PhylomeDBi P0A8M3.

Enzyme and pathway databases

BioCyci EcoCyc:THRS-MONOMER.
ECOL316407:JW1709-MONOMER.
MetaCyc:THRS-MONOMER.
SABIO-RK P0A8M3.

Miscellaneous databases

EvolutionaryTracei P0A8M3.
PROi P0A8M3.

Gene expression databases

Genevestigatori P0A8M3.

Family and domain databases

Gene3Di 3.10.20.30. 1 hit.
3.40.50.800. 1 hit.
HAMAPi MF_00184. Thr_tRNA_synth.
InterProi IPR002314. 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 ]
Pfami PF03129. HGTP_anticodon. 1 hit.
PF02824. TGS. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view ]
PRINTSi PR01047. TRNASYNTHTHR.
SMARTi SM00863. tRNA_SAD. 1 hit.
[Graphical view ]
SUPFAMi SSF52954. SSF52954. 1 hit.
SSF55186. SSF55186. 1 hit.
SSF81271. SSF81271. 1 hit.
TIGRFAMsi TIGR00418. thrS. 1 hit.
PROSITEi PS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. 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. Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 242-642.

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: October 29, 2014
This is version 96 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

External Data

Dasty 3