SYW_CAMJE
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 03-AUG-2022, entry version 110.
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 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; 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; NC_002163.1.
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; Q9PIB4; -.
DR PRIDE; Q9PIB4; -.
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 OMA; GWGQFKP; -.
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; -; 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 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
