SYW_GEOSE
ID SYW_GEOSE Reviewed; 328 AA.
AC P00953;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Tryptophan--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00140};
DE EC=6.1.1.2 {ECO:0000255|HAMAP-Rule:MF_00140, ECO:0000269|PubMed:26555258};
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};
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3026925; DOI=10.1016/0378-1119(86)90164-2;
RA Barstow D.A., Sharman A.F., Atkinson T., Minton N.P.;
RT "Cloning and complete nucleotide sequence of the Bacillus
RT stearothermophilus tryptophanyl tRNA synthetase gene.";
RL Gene 46:37-45(1986).
RN [2]
RP PROTEIN SEQUENCE OF 1-327.
RX PubMed=891985; DOI=10.1016/0014-5793(77)80471-7;
RA Winter G.P., Hartley B.S.;
RT "The amino acid sequence of tryptophanyl tRNA synthetase from Bacillus
RT stearothermophilus.";
RL FEBS Lett. 80:340-342(1977).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RX PubMed=7743129; DOI=10.1016/s0969-2126(01)00132-0;
RA Doublie S., Bricogne G., Gilmore C., Carter C.W. Jr.;
RT "Tryptophanyl-tRNA synthetase crystal structure reveals an unexpected
RT homology to tyrosyl-tRNA synthetase.";
RL Structure 3:17-31(1995).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RX PubMed=10716174; DOI=10.1110/ps.9.2.218;
RA Ilyin V.A., Temple B., Hu M., Li G.-P., Yin Y., Vachette P.,
RA Carter C.W. Jr.;
RT "2.9-A crystal structure of ligand-free tryptophanyl-tRNA synthetase:
RT domain movements fragment the adenine nucleotide binding site.";
RL Protein Sci. 9:218-231(2000).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ATP AND INHIBITOR
RP INDOLMYCIN, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=26555258; DOI=10.1074/jbc.m115.690321;
RA Williams T.L., Yin Y.W., Carter C.W. Jr.;
RT "Selective inhibition of bacterial tryptophanyl-tRNA synthetases by
RT Indolmycin is mechanism-based.";
RL J. Biol. Chem. 291:255-265(2016).
CC -!- FUNCTION: Catalyzes the attachment of tryptophan to tRNA(Trp).
CC {ECO:0000255|HAMAP-Rule:MF_00140, ECO:0000269|PubMed:26555258}.
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 ECO:0000269|PubMed:26555258};
CC -!- ACTIVITY REGULATION: Inhibited by indolmycin, a competitive inhibitor
CC for tryptophan. {ECO:0000269|PubMed:26555258}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3 uM for tryptophan {ECO:0000269|PubMed:26555258};
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; M14742; AAA22873.1; -; Genomic_DNA.
DR PIR; A26055; YWBSF.
DR PDB; 1D2R; X-ray; 2.90 A; A/B/C/D/E/F=1-326.
DR PDB; 1I6K; X-ray; 1.72 A; A=1-328.
DR PDB; 1I6L; X-ray; 1.72 A; A=1-328.
DR PDB; 1I6M; X-ray; 1.72 A; A=1-328.
DR PDB; 1M83; X-ray; 2.20 A; A=1-328.
DR PDB; 1MAU; X-ray; 2.15 A; A=1-328.
DR PDB; 1MAW; X-ray; 3.00 A; A/B/C/D/E/F=1-328.
DR PDB; 1MB2; X-ray; 2.70 A; A/B/C/D/E/F=1-328.
DR PDB; 2OV4; X-ray; 2.50 A; A=1-328.
DR PDB; 3FHJ; X-ray; 2.65 A; A/B/C/D/E/F=1-326.
DR PDB; 3FI0; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=1-326.
DR PDB; 5DK4; X-ray; 1.90 A; A=2-328.
DR PDB; 7CKI; X-ray; 2.30 A; A=1-328.
DR PDB; 7CMS; X-ray; 2.20 A; A/B=1-328.
DR PDBsum; 1D2R; -.
DR PDBsum; 1I6K; -.
DR PDBsum; 1I6L; -.
DR PDBsum; 1I6M; -.
DR PDBsum; 1M83; -.
DR PDBsum; 1MAU; -.
DR PDBsum; 1MAW; -.
DR PDBsum; 1MB2; -.
DR PDBsum; 2OV4; -.
DR PDBsum; 3FHJ; -.
DR PDBsum; 3FI0; -.
DR PDBsum; 5DK4; -.
DR PDBsum; 7CKI; -.
DR PDBsum; 7CMS; -.
DR AlphaFoldDB; P00953; -.
DR SMR; P00953; -.
DR DIP; DIP-48697N; -.
DR DrugBank; DB00150; Tryptophan.
DR DrugBank; DB04537; Tryptophanamide.
DR DrugBank; DB01831; Tryptophanyl-5'amp.
DR PRIDE; P00953; -.
DR BRENDA; 6.1.1.2; 623.
DR EvolutionaryTrace; P00953; -.
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;
KW Direct protein sequencing; Ligase; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..328
FT /note="Tryptophan--tRNA ligase"
FT /id="PRO_0000136601"
FT MOTIF 10..18
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140, ECO:0000305"
FT MOTIF 192..196
FT /note="'KMSKS' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140, ECO:0000305"
FT BINDING 9..11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140,
FT ECO:0000269|PubMed:26555258, ECO:0007744|PDB:5DK4"
FT BINDING 17..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140,
FT ECO:0000269|PubMed:26555258, ECO:0007744|PDB:5DK4"
FT BINDING 132
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140,
FT ECO:0000269|PubMed:26555258, ECO:0007744|PDB:5DK4"
FT BINDING 144..146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140,
FT ECO:0000269|PubMed:26555258, ECO:0007744|PDB:5DK4"
FT BINDING 183
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140,
FT ECO:0000269|PubMed:26555258, ECO:0007744|PDB:5DK4"
FT BINDING 192..196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140,
FT ECO:0000269|PubMed:26555258, ECO:0007744|PDB:5DK4"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:1I6K"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:5DK4"
FT HELIX 16..21
FT /evidence="ECO:0007829|PDB:1I6K"
FT HELIX 23..29
FT /evidence="ECO:0007829|PDB:1I6K"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:1I6K"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:1I6K"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:1I6K"
FT HELIX 51..67
FT /evidence="ECO:0007829|PDB:1I6K"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:1I6K"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:1I6K"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:1I6K"
FT HELIX 85..96
FT /evidence="ECO:0007829|PDB:1I6K"
FT HELIX 99..103
FT /evidence="ECO:0007829|PDB:1I6K"
FT HELIX 106..112
FT /evidence="ECO:0007829|PDB:1I6K"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:7CMS"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:1I6K"
FT HELIX 125..134
FT /evidence="ECO:0007829|PDB:1I6K"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:1I6K"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:1I6K"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:1I6K"
FT HELIX 148..165
FT /evidence="ECO:0007829|PDB:1I6K"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:1I6K"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:1I6K"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:1I6K"
FT HELIX 210..219
FT /evidence="ECO:0007829|PDB:1I6K"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:1I6K"
FT HELIX 236..249
FT /evidence="ECO:0007829|PDB:1I6K"
FT HELIX 253..259
FT /evidence="ECO:0007829|PDB:1I6K"
FT TURN 260..262
FT /evidence="ECO:0007829|PDB:1I6K"
FT HELIX 265..291
FT /evidence="ECO:0007829|PDB:1I6K"
FT HELIX 295..322
FT /evidence="ECO:0007829|PDB:1I6K"
SQ SEQUENCE 328 AA; 37193 MW; B8C4C6028F0913B0 CRC64;
MKTIFSGIQP SGVITIGNYI GALRQFVELQ HEYNCYFCIV DQHAITVWQD PHELRQNIRR
LAAKYLAVGI DPTQATLFIQ SEVPAHAQAA WMLQCIVYIG ELERMTQFKE KSAGKEAVSA
GLLTYPPLMA ADILLYNTDI VPVGEDQKQH IELTRDLAER FNKRYGELFT IPEARIPKVG
ARIMSLVDPT KKMSKSDPNP KAYITLLDDA KTIEKKIKSA VTDSEGTIRY DKEAKPGISN
LLNIYSTLSG QSIEELERQY EGKGYGVFKA DLAQVVIETL RPIQERYHHW MESEELDRVL
DEGAEKANRV ASEMVRKMEQ AMGLGRRR
