ID   SYW_STAAW               Reviewed;         329 AA.
AC   P67594; Q99V94;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Tryptophan--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00140};
DE            EC=6.1.1.2 {ECO:0000255|HAMAP-Rule:MF_00140};
DE   AltName: Full=Tryptophanyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00140};
DE            Short=TrpRS {ECO:0000255|HAMAP-Rule:MF_00140};
GN   Name=trpS {ECO:0000255|HAMAP-Rule:MF_00140}; OrderedLocusNames=MW0878;
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).
CC   -!- FUNCTION: Catalyzes the attachment of tryptophan to tRNA(Trp).
CC       {ECO:0000255|HAMAP-Rule:MF_00140}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-
CC         tryptophanyl-tRNA(Trp); Xref=Rhea:RHEA:24080, Rhea:RHEA-COMP:9671,
CC         Rhea:RHEA-COMP:9705, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57912, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78535, ChEBI:CHEBI:456215; EC=6.1.1.2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00140};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00140}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00140}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00140}.
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DR   EMBL; BA000033; BAB94743.1; -; Genomic_DNA.
DR   RefSeq; WP_000448934.1; NC_003923.1.
DR   AlphaFoldDB; P67594; -.
DR   SMR; P67594; -.
DR   EnsemblBacteria; BAB94743; BAB94743; BAB94743.
DR   KEGG; sam:MW0878; -.
DR   HOGENOM; CLU_029244_1_1_9; -.
DR   OMA; GWGQFKP; -.
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:0004830; F:tryptophan-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00806; TrpRS_core; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00140_B; Trp_tRNA_synth_B; 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; IPR002306; Trp-tRNA-ligase.
DR   InterPro; IPR024109; Trp-tRNA-ligase_bac-type.
DR   Pfam; PF00579; tRNA-synt_1b; 1.
DR   PRINTS; PR01039; TRNASYNTHTRP.
DR   TIGRFAMs; TIGR00233; trpS; 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.
FT   CHAIN           1..329
FT                   /note="Tryptophan--tRNA ligase"
FT                   /id="PRO_0000136680"
FT   MOTIF           10..18
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT   MOTIF           193..197
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT   BINDING         9..11
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT   BINDING         17..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT   BINDING         133
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT   BINDING         145..147
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT   BINDING         184
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT   BINDING         193..197
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
SQ   SEQUENCE   329 AA;  36909 MW;  5F55F1B897FA0291 CRC64;
     METLFSGIQP SGIPTIGNYI GALKQFVDVQ NDYDCYFCIV DQHAITMPQD RLKLRKQTRQ
     LAAIYLASGI DPDKATLFIQ SEVPAHVQAG WMLTTIASVG ELERMTQYKD KAQKAVEGIP
     AGLLTYPPLM AADIVLYNTN IVPVGDDQKQ HIELTRNLVD RFNSRYNDVL VKPEIRMPKV
     GGRVMSLQDP TRKMSKSDDN AKNFISLLDE PNVAAKKIKS AVTDSDGIIK FDRDNKPGIT
     NLISIYAGLT DMPIKDIEAK YEGEGYGKFK GDLAEIVKAF LVEFQEKYES FYNSDKLDDI
     LDQGRDKAHK VSFKTVKKME KAMGLGRKR