SYT_STAAW
ID SYT_STAAW Reviewed; 645 AA.
AC Q8NW68;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Threonine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00184};
DE EC=6.1.1.3 {ECO:0000255|HAMAP-Rule:MF_00184};
DE AltName: Full=Threonyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00184};
DE Short=ThrRS {ECO:0000255|HAMAP-Rule:MF_00184};
GN Name=thrS {ECO:0000255|HAMAP-Rule:MF_00184}; OrderedLocusNames=MW1626;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
RN [2] {ECO:0007744|PDB:1NYQ, ECO:0007744|PDB:1NYR}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH ATP; THREONYL
RP ADENYLATE ANALOG AND ZINC, SUBUNIT, AND DOMAIN.
RX PubMed=12875846; DOI=10.1016/s0022-2836(03)00719-8;
RA Torres-Larios A., Sankaranarayanan R., Rees B., Dock-Bregeon A.C.,
RA Moras D.;
RT "Conformational movements and cooperativity upon amino acid, ATP and tRNA
RT binding in threonyl-tRNA synthetase.";
RL J. Mol. Biol. 331:201-211(2003).
CC -!- FUNCTION: Catalyzes the attachment of threonine to tRNA(Thr) in a two-
CC step reaction: L-threonine is first activated by ATP to form Thr-AMP
CC and then transferred to the acceptor end of tRNA(Thr). Also edits
CC incorrectly charged L-seryl-tRNA(Thr). {ECO:0000255|HAMAP-
CC Rule:MF_00184}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-
CC threonyl-tRNA(Thr); Xref=Rhea:RHEA:24624, Rhea:RHEA-COMP:9670,
CC Rhea:RHEA-COMP:9704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57926, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78534, ChEBI:CHEBI:456215; EC=6.1.1.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00184};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00184,
CC ECO:0000269|PubMed:12875846};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00184,
CC ECO:0000269|PubMed:12875846};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00184,
CC ECO:0000269|PubMed:12875846}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00184}.
CC -!- DOMAIN: The protein structure shows 2 N-terminal domains, the central
CC catalytic and C-terminal anticodon recognition domain. Comparison with
CC the E.coli structure shows the N-terminal domains (editing region) are
CC quite flexible with respect to the catalytic domain. The C-terminal
CC domain recognizes the anticodon region of the tRNA while the acceptor
CC arm is sandwiched between the N-terminal domains and the catalytic
CC domain (PubMed:12875846). {ECO:0000305|PubMed:12875846}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00184}.
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DR EMBL; BA000033; BAB95491.1; -; Genomic_DNA.
DR RefSeq; WP_000435132.1; NC_003923.1.
DR PDB; 1NYQ; X-ray; 3.20 A; A/B=1-645.
DR PDB; 1NYR; X-ray; 2.80 A; A/B=1-645.
DR PDBsum; 1NYQ; -.
DR PDBsum; 1NYR; -.
DR AlphaFoldDB; Q8NW68; -.
DR SMR; Q8NW68; -.
DR DrugBank; DB03355; 5'-O-(L-Threonylsulfamoyl)adenosine.
DR EnsemblBacteria; BAB95491; BAB95491; BAB95491.
DR KEGG; sam:MW1626; -.
DR HOGENOM; CLU_008554_0_1_9; -.
DR OMA; FYYDFAY; -.
DR BRENDA; 6.1.1.3; 3352.
DR EvolutionaryTrace; Q8NW68; -.
DR Proteomes; UP000000418; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004829; F:threonine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006435; P:threonyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00771; ThrRS_core; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 1.
DR HAMAP; MF_00184; Thr_tRNA_synth; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR012676; TGS-like.
DR InterPro; IPR002320; Thr-tRNA-ligase_IIa.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR033728; ThrRS_core.
DR InterPro; IPR012947; tRNA_SAD.
DR PANTHER; PTHR11451; PTHR11451; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF02824; TGS; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR Pfam; PF07973; tRNA_SAD; 1.
DR PRINTS; PR01047; TRNASYNTHTHR.
DR SMART; SM00863; tRNA_SAD; 1.
DR SUPFAM; SSF55186; SSF55186; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR SUPFAM; SSF81271; SSF81271; 1.
DR TIGRFAMs; TIGR00418; thrS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS51880; TGS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Metal-binding; Nucleotide-binding; Protein biosynthesis; RNA-binding;
KW tRNA-binding; Zinc.
FT CHAIN 1..645
FT /note="Threonine--tRNA ligase"
FT /id="PRO_0000101052"
FT DOMAIN 1..63
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT REGION 1..62
FT /note="N1 domain"
FT /evidence="ECO:0000305|PubMed:12875846"
FT REGION 63..223
FT /note="N2 domain"
FT /evidence="ECO:0000305|PubMed:12875846"
FT REGION 242..540
FT /note="Catalytic"
FT /evidence="ECO:0000305|PubMed:12875846"
FT REGION 541..645
FT /note="Anticodon recognition"
FT /evidence="ECO:0000305|PubMed:12875846"
FT BINDING 336
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184,
FT ECO:0000269|PubMed:12875846"
FT BINDING 365
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:12875846"
FT BINDING 365
FT /ligand="L-threonine"
FT /ligand_id="ChEBI:CHEBI:57926"
FT /evidence="ECO:0000269|PubMed:12875846"
FT BINDING 377..378
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:12875846"
FT BINDING 387
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184,
FT ECO:0000269|PubMed:12875846"
FT BINDING 468
FT /ligand="L-threonine"
FT /ligand_id="ChEBI:CHEBI:57926"
FT /evidence="ECO:0000269|PubMed:12875846"
FT BINDING 471
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:12875846"
FT BINDING 485..486
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:12875846"
FT BINDING 517
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184,
FT ECO:0000269|PubMed:12875846"
FT BINDING 522
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:12875846"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:1NYQ"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:1NYQ"
FT HELIX 22..27
FT /evidence="ECO:0007829|PDB:1NYR"
FT HELIX 31..36
FT /evidence="ECO:0007829|PDB:1NYR"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:1NYR"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:1NYR"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:1NYQ"
FT HELIX 67..88
FT /evidence="ECO:0007829|PDB:1NYR"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:1NYR"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:1NYR"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:1NYQ"
FT HELIX 119..131
FT /evidence="ECO:0007829|PDB:1NYR"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:1NYR"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:1NYR"
FT HELIX 145..149
FT /evidence="ECO:0007829|PDB:1NYR"
FT HELIX 154..160
FT /evidence="ECO:0007829|PDB:1NYR"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:1NYR"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:1NYR"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:1NYR"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:1NYR"
FT STRAND 194..204
FT /evidence="ECO:0007829|PDB:1NYR"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:1NYR"
FT STRAND 213..224
FT /evidence="ECO:0007829|PDB:1NYR"
FT HELIX 225..240
FT /evidence="ECO:0007829|PDB:1NYR"
FT HELIX 243..249
FT /evidence="ECO:0007829|PDB:1NYR"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:1NYR"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:1NYR"
FT STRAND 260..266
FT /evidence="ECO:0007829|PDB:1NYR"
FT HELIX 268..287
FT /evidence="ECO:0007829|PDB:1NYR"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:1NYR"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:1NYR"
FT HELIX 302..307
FT /evidence="ECO:0007829|PDB:1NYR"
FT HELIX 309..312
FT /evidence="ECO:0007829|PDB:1NYR"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:1NYR"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:1NYR"
FT STRAND 327..331
FT /evidence="ECO:0007829|PDB:1NYR"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:1NYR"
FT HELIX 336..344
FT /evidence="ECO:0007829|PDB:1NYR"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:1NYR"
FT STRAND 355..364
FT /evidence="ECO:0007829|PDB:1NYR"
FT TURN 369..371
FT /evidence="ECO:0007829|PDB:1NYR"
FT TURN 374..376
FT /evidence="ECO:0007829|PDB:1NYR"
FT STRAND 379..390
FT /evidence="ECO:0007829|PDB:1NYR"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:1NYR"
FT HELIX 395..412
FT /evidence="ECO:0007829|PDB:1NYR"
FT STRAND 418..424
FT /evidence="ECO:0007829|PDB:1NYR"
FT STRAND 430..434
FT /evidence="ECO:0007829|PDB:1NYR"
FT HELIX 437..454
FT /evidence="ECO:0007829|PDB:1NYR"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:1NYR"
FT STRAND 471..476
FT /evidence="ECO:0007829|PDB:1NYR"
FT STRAND 484..494
FT /evidence="ECO:0007829|PDB:1NYR"
FT HELIX 495..498
FT /evidence="ECO:0007829|PDB:1NYR"
FT STRAND 506..508
FT /evidence="ECO:0007829|PDB:1NYQ"
FT STRAND 514..523
FT /evidence="ECO:0007829|PDB:1NYR"
FT HELIX 524..535
FT /evidence="ECO:0007829|PDB:1NYR"
FT TURN 541..543
FT /evidence="ECO:0007829|PDB:1NYR"
FT STRAND 548..554
FT /evidence="ECO:0007829|PDB:1NYR"
FT HELIX 555..570
FT /evidence="ECO:0007829|PDB:1NYR"
FT TURN 571..573
FT /evidence="ECO:0007829|PDB:1NYR"
FT STRAND 576..578
FT /evidence="ECO:0007829|PDB:1NYR"
FT HELIX 585..595
FT /evidence="ECO:0007829|PDB:1NYR"
FT STRAND 598..603
FT /evidence="ECO:0007829|PDB:1NYR"
FT HELIX 605..609
FT /evidence="ECO:0007829|PDB:1NYR"
FT STRAND 612..617
FT /evidence="ECO:0007829|PDB:1NYR"
FT STRAND 625..627
FT /evidence="ECO:0007829|PDB:1NYR"
FT HELIX 628..640
FT /evidence="ECO:0007829|PDB:1NYR"
SQ SEQUENCE 645 AA; 74460 MW; 18FF7CFC22892FBA CRC64;
MEQINIQFPD GNKKAFDKGT TTEDIAQSIS PGLRKKAVAG KFNGQLVDLT KPLETDGSIE
IVTPGSEEAL EVLRHSTAHL MAHAIKRLYG NVKFGVGPVI EGGFYYDFDI DQNISSDDFE
QIEKTMKQIV NENMKIERKV VSRDEAKELF SNDEYKLELI DAIPEDENVT LYSQGDFTDL
CRGVHVPSTA KIKEFKLLST AGAYWRGDSN NKMLQRIYGT AFFDKKELKA HLQMLEERKE
RDHRKIGKEL ELFTNSQLVG AGLPLWLPNG ATIRREIERY IVDKEVSMGY DHVYTPVLAN
VDLYKTSGHW DHYQEDMFPP MQLDETESMV LRPMNCPHHM MIYANKPHSY RELPIRIAEL
GTMHRYEASG AVSGLQRVRG MTLNDSHIFV RPDQIKEEFK RVVNMIIDVY KDFGFEDYSF
RLSYRDPEDK EKYFDDDDMW NKAENMLKEA ADELGLSYEE AIGEAAFYGP KLDVQVKTAM
GKEETLSTAQ LDFLLPERFD LTYIGQDGEH HRPVVIHRGV VSTMERFVAF LTEETKGAFP
TWLAPKQVQI IPVNVDLHYD YARQLQDELK SQGVRVSIDD RNEKMGYKIR EAQMQKIPYQ
IVVGDKEVEN NQVNVRQYGS QDQETVEKDE FIWNLVDEIR LKKHR
