SYW_ECOLI
ID SYW_ECOLI Reviewed; 334 AA.
AC P00954; Q2M749;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2003, sequence version 3.
DT 03-AUG-2022, entry version 172.
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:10918062};
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=b3384, JW3347;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7042706; DOI=10.1016/s0021-9258(20)65116-x;
RA Hall C.V., van Cleemput M., Muench K.H., Yanofsky C.;
RT "The nucleotide sequence of the structural gene for Escherichia coli
RT tryptophanyl-tRNA synthetase.";
RL J. Biol. Chem. 257:6132-6136(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7603433; DOI=10.1007/bf00290345;
RA Lyngstadaas A., Lobner-Olesen A., Boye E.;
RT "Characterization of three genes in the dam-containing operon of
RT Escherichia coli.";
RL Mol. Gen. Genet. 247:546-554(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTANTS.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8555191; DOI=10.1021/bi952103d;
RA Sever S., Rogers K., Rogers M.J., Carter C. Jr., Soell D.;
RT "Escherichia coli tryptophanyl-tRNA synthetase mutants selected for
RT tryptophan auxotrophy implicate the dimer interface in optimizing amino
RT acid binding.";
RL Biochemistry 35:32-40(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP CONFIRMS PROTEIN SEQUENCE BY AMINO ACID ANALYSIS.
RX PubMed=334569; DOI=10.1016/0014-5793(77)80618-2;
RA Winter G.P., Hartley B.S., McLachlan A.D., Lee M., Muench K.H.;
RT "Sequence homologies between the tryptophanyl tRNA synthetases of Bacillus
RT stearothermophilus and Escherichia coli.";
RL FEBS Lett. 82:348-350(1977).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11 AND 152-171.
RX PubMed=6171561; DOI=10.1128/jb.148.3.941-949.1981;
RA Hall C.V., Yanofsky C.;
RT "Cloning and characterization of the gene for Escherichia coli
RT tryptophanyl-transfer ribonucleic acid synthetase.";
RL J. Bacteriol. 148:941-949(1981).
RN [8]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RC STRAIN=K12 / K37;
RX PubMed=10918062; DOI=10.1074/jbc.m005166200;
RA Soutourina J., Plateau P., Blanquet S.;
RT "Metabolism of D-aminoacyl-tRNAs in Escherichia coli and Saccharomyces
RT cerevisiae cells.";
RL J. Biol. Chem. 275:32535-32542(2000).
CC -!- FUNCTION: Catalyzes the attachment of tryptophan to tRNA(Trp). Amino
CC acylates tRNA(Trp) with both L- and D-tryptophan, although D-tryptophan
CC is a poor substrate (PubMed:10918062). {ECO:0000255|HAMAP-
CC Rule:MF_00140, ECO:0000269|PubMed:10918062}.
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:10918062};
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; V00371; CAA23670.1; -; Genomic_DNA.
DR EMBL; Z19601; CAA79669.1; -; Genomic_DNA.
DR EMBL; U38647; AAA92300.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58181.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76409.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77907.1; -; Genomic_DNA.
DR PIR; C65133; YWEC.
DR RefSeq; NP_417843.1; NC_000913.3.
DR RefSeq; WP_000165552.1; NZ_SSZK01000008.1.
DR PDB; 5V0I; X-ray; 1.90 A; A/B=1-334.
DR PDBsum; 5V0I; -.
DR AlphaFoldDB; P00954; -.
DR SMR; P00954; -.
DR BioGRID; 4259293; 179.
DR DIP; DIP-11042N; -.
DR IntAct; P00954; 12.
DR STRING; 511145.b3384; -.
DR jPOST; P00954; -.
DR PaxDb; P00954; -.
DR PRIDE; P00954; -.
DR EnsemblBacteria; AAC76409; AAC76409; b3384.
DR EnsemblBacteria; BAE77907; BAE77907; BAE77907.
DR GeneID; 947894; -.
DR KEGG; ecj:JW3347; -.
DR KEGG; eco:b3384; -.
DR PATRIC; fig|1411691.4.peg.3346; -.
DR EchoBASE; EB1023; -.
DR eggNOG; COG0180; Bacteria.
DR HOGENOM; CLU_029244_1_1_6; -.
DR InParanoid; P00954; -.
DR OMA; GWGQFKP; -.
DR PhylomeDB; P00954; -.
DR BioCyc; EcoCyc:TRPS-MON; -.
DR BioCyc; MetaCyc:TRPS-MON; -.
DR SABIO-RK; P00954; -.
DR PRO; PR:P00954; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004830; F:tryptophan-tRNA ligase activity; IDA:EcoCyc.
DR GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IMP:EcoCyc.
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..334
FT /note="Tryptophan--tRNA ligase"
FT /id="PRO_0000136628"
FT MOTIF 12..20
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT MOTIF 195..199
FT /note="'KMSKS' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT BINDING 11..13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT BINDING 19..20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT BINDING 135
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT BINDING 147..149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT BINDING 186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT BINDING 195..199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT VARIANT 60
FT /note="T -> R (in TRPS567C; reduced activity,
FT thermolabile)"
FT VARIANT 91
FT /note="L -> F (in TRPS10330; reduced activity)"
FT VARIANT 112
FT /note="D -> E (in TRPS9969; no effect in activity)"
FT VARIANT 129
FT /note="P -> S (in TRPS9969; reduced activity)"
FT VARIANT 133
FT /note="A -> E (in TRPS42C; reduced activity)"
FT VARIANT 196
FT /note="M -> I (in TRPS271C; activity largely reduced)"
FT VARIANT 329
FT /note="G -> S (in TRPS4040; reduced activity)"
FT CONFLICT 30
FT /note="N -> K (in Ref. 1; CAA23670 and 2; CAA79669)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="E -> Q (in Ref. 1; CAA23670 and 2; CAA79669)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="P -> R (in Ref. 1; CAA23670, 2; CAA79669 and 3;
FT AAA92300)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 334 AA; 37438 MW; CBAC73ABB8406026 CRC64;
MTKPIVFSGA QPSGELTIGN YMGALRQWVN MQDDYHCIYC IVDQHAITVR QDAQKLRKAT
LDTLALYLAC GIDPEKSTIF VQSHVPEHAQ LGWALNCYTY FGELSRMTQF KDKSARYAEN
INAGLFDYPV LMAADILLYQ TNLVPVGEDQ KQHLELSRDI AQRFNALYGE IFKVPEPFIP
KSGARVMSLL EPTKKMSKSD DNRNNVIGLL EDPKSVVKKI KRAVTDSDEP PVVRYDVQNK
AGVSNLLDIL SAVTGQSIPE LEKQFEGKMY GHLKGEVADA VSGMLTELQE RYHRFRNDEA
FLQQVMKDGA EKASAHASRT LKAVYEAIGF VAKP
