ID SYW_STRP8 Reviewed; 340 AA. AC P67598; Q8NYZ2; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 27-MAR-2024, entry version 96. 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}; GN OrderedLocusNames=spyM18_2245; OS Streptococcus pyogenes serotype M18 (strain MGAS8232). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=186103; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGAS8232; RX PubMed=11917108; DOI=10.1073/pnas.062526099; RA Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S., RA Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F., Parkins L.D., RA Beres S.B., Campbell D.S., Smith T.M., Zhang Q., Kapur V., Daly J.A., RA Veasy L.G., Musser J.M.; RT "Genome sequence and comparative microarray analysis of serotype M18 group RT A Streptococcus strains associated with acute rheumatic fever outbreaks."; RL Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE009949; AAL98674.1; -; Genomic_DNA. DR RefSeq; WP_002991455.1; NC_003485.1. DR AlphaFoldDB; P67598; -. DR SMR; P67598; -. DR GeneID; 69901625; -. DR KEGG; spm:spyM18_2245; -. DR HOGENOM; CLU_029244_0_1_9; -. 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; HUPs; 1. DR Gene3D; 1.10.240.10; Tyrosyl-Transfer RNA Synthetase; 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 NCBIfam; TIGR00233; trpS; 1. DR PANTHER; PTHR43766; TRYPTOPHAN--TRNA LIGASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR43766:SF1; TRYPTOPHAN--TRNA LIGASE, MITOCHONDRIAL; 1. DR Pfam; PF00579; tRNA-synt_1b; 1. DR PRINTS; PR01039; TRNASYNTHTRP. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 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..340 FT /note="Tryptophan--tRNA ligase" FT /id="PRO_0000136695" FT MOTIF 12..20 FT /note="'HIGH' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140" FT MOTIF 202..206 FT /note="'KMSKS' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140" FT BINDING 11..13 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140" FT BINDING 19..20 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140" FT BINDING 140 FT /ligand="L-tryptophan" FT /ligand_id="ChEBI:CHEBI:57912" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140" FT BINDING 152..154 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140" FT BINDING 194 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140" FT BINDING 202..206 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140" SQ SEQUENCE 340 AA; 38373 MW; 5518E2E1E0757157 CRC64; MTKPIILTGD RPTGKLHLGH YVGSLKNRVF LQNENKYKMF VFLADQQALT DHAKESELIQ ESIGNVALDY LSVGLDPKQS TIFIQSQIPE LAELSMYYMN LVSLARLERN PTVKTEIAQK GFGESIPSGF LVYPVSQAAD ITAFKANLVP VGNDQKPMIE QTREIVRSFN HTYHTDCLVE PEGIYPENEK AGRLPGLDGN AKMSKSLGNG IYLSDDADTV RKKVMSMYTD PNHIKIEDPG QIEGNMVFHY LDIFARKEDQ ADIEAMKEHY QRGGLGDVKT KRYLLDILER ELAPIRERRL EYAKDMGEVF RMLQEGSQKA RTVAAKTLSE VKSAMGINYF //