ID   SYY2_BACSU              Reviewed;         413 AA.
AC   P25151;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   02-SEP-2026, entry version 161.
DE   RecName: Full=Tyrosine--tRNA ligase 2 {ECO:0000255|HAMAP-Rule:MF_02007};
DE            EC=6.1.1.1 {ECO:0000255|HAMAP-Rule:MF_02007};
DE   AltName: Full=Tyrosyl-tRNA synthetase 2 {ECO:0000255|HAMAP-Rule:MF_02007};
DE            Short=TyrRS 2 {ECO:0000255|HAMAP-Rule:MF_02007};
GN   Name=tyrS2 {ECO:0000255|HAMAP-Rule:MF_02007};
GN   Synonyms=tyrR, tyrS1, tyrT, tyrZ; OrderedLocusNames=BSU38460;
GN   ORFNames=ipa-9r;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=1806041; DOI=10.3109/10425179109020780;
RA   Glaser P., Kunst F., Debarbouille M., Vertes A., Danchin A., Dedonder R.;
RT   "A gene encoding a tyrosine tRNA synthetase is located near sacS in
RT   Bacillus subtilis.";
RL   DNA Seq. 1:251-261(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA   Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA   Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA   Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT   "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT   region from 325 degrees to 333 degrees.";
RL   Mol. Microbiol. 10:371-384(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
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:0000255|HAMAP-
CC       Rule:MF_02007}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tRNA(Tyr) + L-tyrosine + ATP = L-tyrosyl-tRNA(Tyr) + AMP +
CC         diphosphate + H(+); 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         Evidence={ECO:0000255|HAMAP-Rule:MF_02007};
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       TyrS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02007}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA36724.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X52480; CAA36724.1; ALT_INIT; Genomic_DNA.
DR   EMBL; X73124; CAA51565.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15872.1; -; Genomic_DNA.
DR   PIR; S16426; S16426.
DR   RefSeq; NP_391725.1; NC_000964.3.
DR   RefSeq; WP_010886638.1; NC_000964.3.
DR   AlphaFoldDB; P25151; -.
DR   SMR; P25151; -.
DR   FunCoup; P25151; 115.
DR   STRING; 224308.BSU38460; -.
DR   PaxDb; 224308-BSU38460; -.
DR   EnsemblBacteria; CAB15872; CAB15872; BSU_38460.
DR   GeneID; 937345; -.
DR   KEGG; bsu:BSU38460; -.
DR   PATRIC; fig|224308.43.peg.4031; -.
DR   eggNOG; COG0162; Bacteria.
DR   InParanoid; P25151; -.
DR   OrthoDB; 9804243at2; -.
DR   PhylomeDB; P25151; -.
DR   BioCyc; BSUB:BSU38460-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   AbasyAtlas; P25151; -.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0004831; F:tyrosine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd00165; S4; 1.
DR   CDD; cd00805; TyrRS_core; 1.
DR   FunFam; 1.10.240.10:FF:000006; Tyrosine--tRNA ligase; 1.
DR   FunFam; 3.10.290.10:FF:000022; Tyrosine--tRNA ligase; 1.
DR   FunFam; 3.40.50.620:FF:000061; Tyrosine--tRNA ligase; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.10.290.10; RNA-binding S4 domain; 1.
DR   Gene3D; 1.10.240.10; Tyrosyl-Transfer RNA Synthetase; 1.
DR   HAMAP; MF_02007; Tyr_tRNA_synth_type2; 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; IPR002942; S4_RNA-bd.
DR   InterPro; IPR036986; S4_RNA-bd_sf.
DR   InterPro; IPR054608; SYY-like_C.
DR   InterPro; IPR002307; Tyr-tRNA-ligase.
DR   InterPro; IPR024088; Tyr-tRNA-ligase_bac-type.
DR   InterPro; IPR024108; Tyr-tRNA-ligase_bac_2.
DR   NCBIfam; TIGR00234; tyrS; 1.
DR   PANTHER; PTHR11766:SF1; TYROSINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR11766; TYROSYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF22421; SYY_C-terminal; 1.
DR   Pfam; PF00579; tRNA-synt_1b; 1.
DR   PRINTS; PR01040; TRNASYNTHTYR.
DR   SMART; SM00363; S4; 1.
DR   SUPFAM; SSF55174; Alpha-L RNA-binding motif; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR   PROSITE; PS50889; S4; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; Repeat;
KW   RNA-binding.
FT   CHAIN           1..413
FT                   /note="Tyrosine--tRNA ligase 2"
FT                   /id="PRO_0000055644"
FT   REPEAT          89..94
FT                   /note="1"
FT   REPEAT          96..101
FT                   /note="2"
FT   DOMAIN          353..413
FT                   /note="S4 RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02007"
FT   REGION          89..101
FT                   /note="2 X 6 AA tandem repeats"
FT   MOTIF           58..67
FT                   /note="'HIGH' region"
FT   MOTIF           242..246
FT                   /note="'KMSKS' region"
FT   BINDING         245
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02007"
SQ   SEQUENCE   413 AA;  47100 MW;  2C6FD6DADEBC33F7 CRC64;
     MMRTFEQLTA SQQKEVERQL QLYMTGAHEV IPPEELKAKL VKSISTGTPL KIKLGLDPSA
     PDVHLGHTVV LNKLRQFQEN GHIVQLLIGD FTGKIGDPTG KSAARKQLTD EEVQHNAKTY
     FEQFGKVLDP EKVELHYNSK WLKTLNLEDV IELAGKITVA RLMERDDFEE RIAMQKPISL
     HEFFYPLMQG YDSVVLESDI ELGGTDQHFN VLMGRHFQER YNKEKQVVIL MPLLEGLDGV
     EKMSKSKHNY IGINEHPNDM YGKTMSLPDS LMKKYIHLAT DLELEEKKQL VKDLETGAVH
     PRDAKMLLAR TIVRMYHGEK AAEAAEHSFK TVFQENSLPE DIPAVNWKGE KTIAMIDLLV
     KLKLLSSKSE ARRMIQNGGV RIDGEKVTDV HAKAEIRENM IIQVGKRKFL KLQ
//