ID   SYY2_STRT2              Reviewed;         302 AA.
AC   Q5M4D1;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Tyrosine--tRNA ligase 2;
DE            EC=6.1.1.1;
DE   AltName: Full=Tyrosyl-tRNA synthetase 2;
DE            Short=TyrRS 2;
GN   Name=tyrS2; Synonyms=tyrSE; OrderedLocusNames=stu1043;
OS   Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=264199;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-250 / LMG 18311;
RX   PubMed=15543133; DOI=10.1038/nbt1034;
RA   Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA   Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA   Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA   Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT   "Complete sequence and comparative genome analysis of the dairy bacterium
RT   Streptococcus thermophilus.";
RL   Nat. Biotechnol. 22:1554-1558(2004).
CC   -!- FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-
CC       step reaction: tyrosine is first activated by ATP to form Tyr-AMP and
CC       then transferred to the acceptor end of tRNA(Tyr). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-
CC         tyrosyl-tRNA(Tyr); Xref=Rhea:RHEA:10220, Rhea:RHEA-COMP:9706,
CC         Rhea:RHEA-COMP:9707, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58315, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78536, ChEBI:CHEBI:456215; EC=6.1.1.1;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       TyrS type 1 subfamily. {ECO:0000305}.
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DR   EMBL; CP000023; AAV60695.1; -; Genomic_DNA.
DR   RefSeq; WP_002948690.1; NC_006448.1.
DR   AlphaFoldDB; Q5M4D1; -.
DR   SMR; Q5M4D1; -.
DR   STRING; 264199.stu1043; -.
DR   EnsemblBacteria; AAV60695; AAV60695; stu1043.
DR   GeneID; 66898879; -.
DR   KEGG; stl:stu1043; -.
DR   eggNOG; COG0162; Bacteria.
DR   HOGENOM; CLU_024003_0_0_9; -.
DR   OMA; WEGVENE; -.
DR   Proteomes; UP000001170; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004831; F:tyrosine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00805; TyrRS_core; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002305; aa-tRNA-synth_Ic.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR002307; Tyr-tRNA-ligase.
DR   InterPro; IPR024088; Tyr-tRNA-ligase_bac-type.
DR   PANTHER; PTHR11766; PTHR11766; 1.
DR   Pfam; PF00579; tRNA-synt_1b; 1.
DR   PRINTS; PR01040; TRNASYNTHTYR.
DR   TIGRFAMs; TIGR00234; tyrS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding.
FT   CHAIN           1..302
FT                   /note="Tyrosine--tRNA ligase 2"
FT                   /id="PRO_0000234796"
FT   MOTIF           38..47
FT                   /note="'HIGH' region"
FT   MOTIF           220..224
FT                   /note="'KMSKS' region"
FT   BINDING         33
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000250"
FT   BINDING         160
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000250"
FT   BINDING         164
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   302 AA;  34298 MW;  DED6C3109420909F CRC64;
     MKLFEDLQWR GLVKQYSSDS LIEKLNNGKL TFYIGTDPTA DSLHLGHYSS FLIAKRLAKY
     GHQPIILIGG ATALVGDPRG TSERDLAEQE KIFDNFEKLK NQIQKIFPYE IVNNYDWTKN
     IMAIDFLREF GKHITAGYMS NKELVKRQFA TGISFTEFSY MLLQGMDFYH LFTTKGVTLQ
     IAGSDQWGNM TTGIDLVRKK TGEEVFAMTM PLITDEEGKK FGKSEGNAIW ISENKNTPEE
     LHNFLLNVSD DIVISLLKKL TFLSRKDIEE IESRHKNGTG YAQGILADTV TFDIHGVSIN
     KK