ID   SYW_TROWT               Reviewed;         335 AA.
AC   Q83FN1;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=TWT_686;
OS   Tropheryma whipplei (strain Twist) (Whipple's bacillus).
OC   Bacteria; Actinobacteria; Micrococcales; Tropherymataceae; Tropheryma.
OX   NCBI_TaxID=203267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Twist;
RX   PubMed=12902375; DOI=10.1101/gr.1474603;
RA   Raoult D., Ogata H., Audic S., Robert C., Suhre K., Drancourt M.,
RA   Claverie J.-M.;
RT   "Tropheryma whipplei twist: a human pathogenic Actinobacteria with a
RT   reduced genome.";
RL   Genome Res. 13:1800-1809(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}.
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DR   EMBL; AE014184; AAO44783.1; -; Genomic_DNA.
DR   RefSeq; WP_011102729.1; NC_004572.3.
DR   AlphaFoldDB; Q83FN1; -.
DR   SMR; Q83FN1; -.
DR   STRING; 203267.TWT_686; -.
DR   EnsemblBacteria; AAO44783; AAO44783; TWT_686.
DR   KEGG; twh:TWT_686; -.
DR   eggNOG; COG0180; Bacteria.
DR   HOGENOM; CLU_029244_1_1_11; -.
DR   OMA; GWGQFKP; -.
DR   OrthoDB; 951354at2; -.
DR   Proteomes; UP000002200; 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; Reference proteome.
FT   CHAIN           1..335
FT                   /note="Tryptophan--tRNA ligase"
FT                   /id="PRO_0000136703"
FT   MOTIF           20..29
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT   MOTIF           201..205
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT   BINDING         19..21
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT   BINDING         28..29
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT   BINDING         143
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT   BINDING         155..157
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT   BINDING         192
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT   BINDING         201..205
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
SQ   SEQUENCE   335 AA;  37351 MW;  F16CFE9163BBE958 CRC64;
     MTSSAIRINK KPVVLSGIQP SSGMLHLGNY LGALKSFGRM QDDYTTYFML ANLHSMTFPQ
     NPEVLRENTI RIAAQCIAAG IDPAKSIVFL QSDVYQHNQL AWVLGNVCIF GEAARMTQFK
     DKSGKQGNIS TGLFTYPILM ASDILLYDSA FVPVGADQKQ HLELTRTLAR RFNAQYGQTF
     LVPQPFECSI RIYDLQDPAV KMSKSSATES GTIFLLDSPD KIVKKIMRSV TDSEDVIGYD
     RETKPGVSNL VVMYSCLTDC TIEQTVNIYS GKKYSVLKKD LSDILVEVCT TIATRTNELL
     DDKNYIRKIL VTASEQARGV AQKTIDRVYE KLGVY