SYW_YERPE
ID SYW_YERPE Reviewed; 342 AA.
AC Q8ZJF2; Q0WKE5;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 121.
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=YPO0157, y3940, YP_0159;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAM87484.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAS60437.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAL18843.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; AL590842; CAL18843.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE009952; AAM87484.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE017042; AAS60437.1; ALT_INIT; Genomic_DNA.
DR PIR; AB0020; AB0020.
DR RefSeq; YP_002345243.1; NC_003143.1.
DR PDB; 3N9I; X-ray; 1.95 A; A/B=1-342.
DR PDBsum; 3N9I; -.
DR AlphaFoldDB; Q8ZJF2; -.
DR SMR; Q8ZJF2; -.
DR STRING; 214092.YPO0157; -.
DR PaxDb; Q8ZJF2; -.
DR DNASU; 1148887; -.
DR EnsemblBacteria; AAM87484; AAM87484; y3940.
DR EnsemblBacteria; AAS60437; AAS60437; YP_0159.
DR KEGG; ype:YPO0157; -.
DR KEGG; ypk:y3940; -.
DR KEGG; ypm:YP_0159; -.
DR PATRIC; fig|214092.21.peg.385; -.
DR eggNOG; COG0180; Bacteria.
DR HOGENOM; CLU_029244_1_1_6; -.
DR EvolutionaryTrace; Q8ZJF2; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004830; F:tryptophan-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IBA:GO_Central.
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..342
FT /note="Tryptophan--tRNA ligase"
FT /id="PRO_0000136716"
FT MOTIF 20..28
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT MOTIF 203..207
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 27..28
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 194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT BINDING 203..207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:3N9I"
FT HELIX 26..31
FT /evidence="ECO:0007829|PDB:3N9I"
FT HELIX 33..37
FT /evidence="ECO:0007829|PDB:3N9I"
FT TURN 38..42
FT /evidence="ECO:0007829|PDB:3N9I"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:3N9I"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:3N9I"
FT HELIX 61..78
FT /evidence="ECO:0007829|PDB:3N9I"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:3N9I"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:3N9I"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:3N9I"
FT HELIX 95..104
FT /evidence="ECO:0007829|PDB:3N9I"
FT HELIX 109..113
FT /evidence="ECO:0007829|PDB:3N9I"
FT HELIX 116..124
FT /evidence="ECO:0007829|PDB:3N9I"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:3N9I"
FT HELIX 131..145
FT /evidence="ECO:0007829|PDB:3N9I"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:3N9I"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:3N9I"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:3N9I"
FT HELIX 159..176
FT /evidence="ECO:0007829|PDB:3N9I"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:3N9I"
FT HELIX 221..229
FT /evidence="ECO:0007829|PDB:3N9I"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:3N9I"
FT HELIX 249..262
FT /evidence="ECO:0007829|PDB:3N9I"
FT HELIX 266..272
FT /evidence="ECO:0007829|PDB:3N9I"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:3N9I"
FT HELIX 278..304
FT /evidence="ECO:0007829|PDB:3N9I"
FT HELIX 307..336
FT /evidence="ECO:0007829|PDB:3N9I"
SQ SEQUENCE 342 AA; 38225 MW; 79B4EDAEC31E0745 CRC64;
MVLSKPTVSS KPIVFSGAQP SGELTIGNYM GALRQWVQMQ DDYDCIYCIV DLHAITARQD
PALLRKRTLD TLALYLACGI DPKKSTIFVQ SHVPEHSQLS WALNCYTYFG ELSRMTQFKD
KSARYAENIN AGLFDYPVLM AADILLYQTN QVPVGEDQKQ HLELSRDIAS RFNNLYGDIF
KIPEPFIPKA GARVMSLQDP TKKMSKSDDN RNNVIELLED PKSVVKKIKR AMTDSDEPAL
IRYDVEKKAG VSNLLDILSG VTGQSIPELE AQFTGQMYGH LKGAVADAVS GMLSELQERY
RTYREDEALL QDVMREGAAK ARARAQVTLA KVYEAIGFVA QP
