ID   SYW_CAMJE               Reviewed;         319 AA.
AC   Q9PIB4; Q0PBC2;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 117.
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=Cj0388;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 /
OS   NCTC 11168).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
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; AL111168; CAL34538.1; -; Genomic_DNA.
DR   PIR; B81382; B81382.
DR   RefSeq; WP_002858719.1; NZ_SZUC01000004.1.
DR   RefSeq; YP_002343825.1; NC_002163.1.
DR   PDB; 3M5W; X-ray; 2.32 A; A/B=1-319.
DR   PDB; 3TZL; X-ray; 2.15 A; A/B=1-319.
DR   PDBsum; 3M5W; -.
DR   PDBsum; 3TZL; -.
DR   AlphaFoldDB; Q9PIB4; -.
DR   SMR; Q9PIB4; -.
DR   IntAct; Q9PIB4; 3.
DR   STRING; 192222.Cj0388; -.
DR   PaxDb; 192222-Cj0388; -.
DR   EnsemblBacteria; CAL34538; CAL34538; Cj0388.
DR   GeneID; 904711; -.
DR   KEGG; cje:Cj0388; -.
DR   PATRIC; fig|192222.6.peg.379; -.
DR   eggNOG; COG0180; Bacteria.
DR   HOGENOM; CLU_029244_1_1_7; -.
DR   OrthoDB; 9801042at2; -.
DR   EvolutionaryTrace; Q9PIB4; -.
DR   Proteomes; UP000000799; 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   1: Evidence at protein level;
KW   3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..319
FT                   /note="Tryptophan--tRNA ligase"
FT                   /id="PRO_0000136613"
FT   MOTIF           9..17
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT   MOTIF           189..193
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT   BINDING         8..10
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT   BINDING         16..17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT   BINDING         131
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT   BINDING         143..145
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT   BINDING         182
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT   BINDING         189..193
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT   STRAND          3..7
FT                   /evidence="ECO:0007829|PDB:3TZL"
FT   HELIX           15..20
FT                   /evidence="ECO:0007829|PDB:3TZL"
FT   HELIX           22..27
FT                   /evidence="ECO:0007829|PDB:3TZL"
FT   TURN            28..31
FT                   /evidence="ECO:0007829|PDB:3TZL"
FT   STRAND          35..38
FT                   /evidence="ECO:0007829|PDB:3TZL"
FT   HELIX           40..43
FT                   /evidence="ECO:0007829|PDB:3TZL"
FT   TURN            44..46
FT                   /evidence="ECO:0007829|PDB:3TZL"
FT   HELIX           50..66
FT                   /evidence="ECO:0007829|PDB:3TZL"
FT   TURN            71..73
FT                   /evidence="ECO:0007829|PDB:3TZL"
FT   STRAND          74..78
FT                   /evidence="ECO:0007829|PDB:3TZL"
FT   HELIX           79..81
FT                   /evidence="ECO:0007829|PDB:3TZL"
FT   HELIX           84..92
FT                   /evidence="ECO:0007829|PDB:3TZL"
FT   HELIX           93..95
FT                   /evidence="ECO:0007829|PDB:3TZL"
FT   HELIX           98..102
FT                   /evidence="ECO:0007829|PDB:3TZL"
FT   HELIX           105..112
FT                   /evidence="ECO:0007829|PDB:3TZL"
FT   HELIX           119..134
FT                   /evidence="ECO:0007829|PDB:3TZL"
FT   STRAND          138..141
FT                   /evidence="ECO:0007829|PDB:3TZL"
FT   HELIX           144..146
FT                   /evidence="ECO:0007829|PDB:3TZL"
FT   HELIX           147..164
FT                   /evidence="ECO:0007829|PDB:3TZL"
FT   STRAND          172..174
FT                   /evidence="ECO:0007829|PDB:3TZL"
FT   STRAND          187..189
FT                   /evidence="ECO:0007829|PDB:3TZL"
FT   HELIX           192..194
FT                   /evidence="ECO:0007829|PDB:3TZL"
FT   STRAND          199..201
FT                   /evidence="ECO:0007829|PDB:3TZL"
FT   HELIX           204..212
FT                   /evidence="ECO:0007829|PDB:3TZL"
FT   HELIX           227..229
FT                   /evidence="ECO:0007829|PDB:3TZL"
FT   HELIX           231..236
FT                   /evidence="ECO:0007829|PDB:3TZL"
FT   HELIX           237..239
FT                   /evidence="ECO:0007829|PDB:3TZL"
FT   HELIX           242..254
FT                   /evidence="ECO:0007829|PDB:3TZL"
FT   HELIX           259..273
FT                   /evidence="ECO:0007829|PDB:3TZL"
FT   HELIX           275..286
FT                   /evidence="ECO:0007829|PDB:3TZL"
FT   HELIX           288..317
FT                   /evidence="ECO:0007829|PDB:3TZL"
SQ   SEQUENCE   319 AA;  36084 MW;  CB620B2B67AA6666 CRC64;
     MRVLTGLQPS GDLHIGNYFG AIKQMVDAQE KSQMFMFIAN YHAMTSSQDG EKLKQNSLKA
     AAAFLSLGID PQKSVFWLQS DVKEVMELYW ILSQFTPMGL LERAHSYKDK VAKGLSASHG
     LFSYPVLMAA DILLFDTRIV PVGKDQIQHV EIARDIALKV NNEWGEIFTL PEARVNEEVA
     VVVGTDGAKM SKSYQNTIDI FSSEKTLKKQ ISSIVTDSTA LEDPKDHENC NIFKIAKLFL
     DESGQKELQI RYEKGGEGYG HFKIYLNELV NAYFKEAREK YNELLEKPSH LKEILDFGAT
     KARKIAQEKM QKIYEKIGL
//