ID SYW_STAES Reviewed; 329 AA. AC Q8CT69; DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 111. 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=SE_0685; OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=176280; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12228 / FDA PCI 1200; RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x; RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q., RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H., RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.; RT "Genome-based analysis of virulence genes in a non-biofilm-forming RT Staphylococcus epidermidis strain (ATCC 12228)."; RL Mol. Microbiol. 49:1577-1593(2003). 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; AE015929; AAO04282.1; -; Genomic_DNA. DR RefSeq; NP_764240.1; NC_004461.1. DR RefSeq; WP_001829285.1; NZ_WBME01000066.1. DR AlphaFoldDB; Q8CT69; -. DR SMR; Q8CT69; -. DR GeneID; 50019174; -. DR KEGG; sep:SE_0685; -. DR PATRIC; fig|176280.10.peg.659; -. DR eggNOG; COG0180; Bacteria. DR HOGENOM; CLU_029244_1_1_9; -. DR OrthoDB; 9801042at2; -. DR BRENDA; 6.1.1.2; 5875. DR Proteomes; UP000001411; 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; 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..329 FT /note="Tryptophan--tRNA ligase" FT /id="PRO_0000136681" 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; 36970 MW; 274C1EB9EBC89356 CRC64; METLFSGIQP SGIPTIGNYI GALKQFVDVQ DDYECFFCIV DQHAITVPQD RLKLRKQIRQ LAAIYLATGI DPDKSTLFIQ SEVPAHVQAG WMLTTIASIG ELERMTQFKD KAQKRADGVP AGLLTYPPLM AADIVIYNTN IVPVGDDQKQ HMELTRNLVD RFNSRYNDVL VKPEVRMPKV GGRVMSLQDP TKKMSKSDDN QKNFISLLDE PHVAAKKIKS AVTDSDGIIK FDRENKPGIS NLLSIYSGLT NESIKNIESK YEGEGYGKFK GDLSEIVKDF LINFQEKYAS FYNSDDLDDI LDKGKEKAQK ASFKTLKKME KAMGLGRKR //