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P0A8M3

- SYT_ECOLI

UniProt

P0A8M3 - SYT_ECOLI

Protein

Threonine--tRNA ligase

Gene

thrS

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (07 Jun 2005)
      Previous versions | rss
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    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. protein binding Source: IntAct
    5. RNA binding Source: EcoliWiki
    6. threonine-tRNA ligase activity Source: EcoCyc
    7. translation repressor activity, nucleic acid binding Source: EcoCyc
    8. 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

    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

    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.
    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

    MPVITLPDGS QRHYDHAVSP MDVALDIGPG LAKACIAGRV NGELVDACDL    50
    IENDAQLSII TAKDEEGLEI IRHSCAHLLG HAIKQLWPHT KMAIGPVIDN 100
    GFYYDVDLDR TLTQEDVEAL EKRMHELAEK NYDVIKKKVS WHEARETFAN 150
    RGESYKVSIL DENIAHDDKP GLYFHEEYVD MCRGPHVPNM RFCHHFKLMK 200
    TAGAYWRGDS NNKMLQRIYG TAWADKKALN AYLQRLEEAA KRDHRKIGKQ 250
    LDLYHMQEEA PGMVFWHNDG WTIFRELEVF VRSKLKEYQY QEVKGPFMMD 300
    RVLWEKTGHW DNYKDAMFTT SSENREYCIK PMNCPGHVQI FNQGLKSYRD 350
    LPLRMAEFGS CHRNEPSGSL HGLMRVRGFT QDDAHIFCTE EQIRDEVNGC 400
    IRLVYDMYST FGFEKIVVKL STRPEKRIGS DEMWDRAEAD LAVALEENNI 450
    PFEYQLGEGA FYGPKIEFTL YDCLDRAWQC GTVQLDFSLP SRLSASYVGE 500
    DNERKVPVMI HRAILGSMER FIGILTEEFA GFFPTWLAPV QVVIMNITDS 550
    QSEYVNELTQ KLSNAGIRVK ADLRNEKIGF KIREHTLRRV PYMLVCGDKE 600
    VESGKVAVRT RRGKDLGSMD VNEVIEKLQQ EIRSRSLKQL EE 642
    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.
    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

    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 1, 2014
    This is version 95 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