SYV_ECOLI
ID SYV_ECOLI Reviewed; 951 AA.
AC P07118; P78142; Q2M651; Q7X4V7;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Valine--tRNA ligase;
DE EC=6.1.1.9;
DE AltName: Full=Valyl-tRNA synthetase;
DE Short=ValRS;
GN Name=valS; OrderedLocusNames=b4258, JW4215;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3317277; DOI=10.1093/nar/15.21.9081;
RA Haertlein M., Frank R., Madern D.;
RT "Nucleotide sequence of Escherichia coli valyl-tRNA synthetase gene valS.";
RL Nucleic Acids Res. 15:9081-9082(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3275660; DOI=10.1016/s0021-9258(19)35434-1;
RA Heck J.D., Hatfield G.W.;
RT "Valyl-tRNA synthetase gene of Escherichia coli K12. Primary structure and
RT homology within a family of aminoacyl-tRNA synthetases.";
RL J. Biol. Chem. 263:868-877(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-801.
RC STRAIN=B / MD6014;
RA Ramchandani J.H., Bhattacharjee S.K., Mahajan S.K.;
RT "Nucleotide sequence of the valS-holC region of Escherichia coli B.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PROTEIN SEQUENCE OF 1-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
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 MUTAGENESIS OF THR-222.
RX PubMed=11313495; DOI=10.1126/science.1057718;
RA Doering V., Mootz H.D., Nangle L.A., Hendrickson T.L., de Crecy-Lagard V.,
RA Schimmel P., Marliere P.;
RT "Enlarging the amino acid set of Escherichia coli by infiltration of the
RT valine coding pathway.";
RL Science 292:501-504(2001).
RN [10]
RP KINETIC PARAMETERS, AND MUTAGENESIS OF LYS-277.
RX PubMed=12475234; DOI=10.1021/bi0205101;
RA Hountondji C., Lazennec C., Beauvallet C., Dessen P., Pernollet J.-C.,
RA Plateau P., Blanquet S.;
RT "Crucial role of conserved lysine 277 in the fidelity of tRNA
RT aminoacylation by Escherichia coli valyl-tRNA synthetase.";
RL Biochemistry 41:14856-14865(2002).
CC -!- FUNCTION: Catalyzes the attachment of valine to tRNA(Val). As ValRS can
CC inadvertently accommodate and process structurally similar amino acids
CC such as threonine, to avoid such errors, it has a 'posttransfer'
CC editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-
CC dependent manner.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-
CC tRNA(Val); Xref=Rhea:RHEA:10704, Rhea:RHEA-COMP:9672, Rhea:RHEA-
CC COMP:9708, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57762,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78537, ChEBI:CHEBI:456215; EC=6.1.1.9;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.1 uM for tRNA {ECO:0000269|PubMed:12475234};
CC KM=47 uM for valine {ECO:0000269|PubMed:12475234};
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DOMAIN: ValRS has two distinct active sites: one for aminoacylation and
CC one for editing. The misactivated threonine is translocated from the
CC active site to the editing site.
CC -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC activity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 1 subfamily. {ECO:0000305}.
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DR EMBL; X05891; CAA29322.1; -; Genomic_DNA.
DR EMBL; J03497; AAA24657.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97155.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77215.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78255.1; -; Genomic_DNA.
DR EMBL; AY283771; AAP43521.1; -; Genomic_DNA.
DR PIR; E65238; SYECVT.
DR RefSeq; NP_418679.1; NC_000913.3.
DR RefSeq; WP_000416392.1; NZ_STEB01000013.1.
DR AlphaFoldDB; P07118; -.
DR SMR; P07118; -.
DR BioGRID; 4262724; 7.
DR BioGRID; 853071; 1.
DR DIP; DIP-11112N; -.
DR IntAct; P07118; 6.
DR STRING; 511145.b4258; -.
DR jPOST; P07118; -.
DR PaxDb; P07118; -.
DR PRIDE; P07118; -.
DR EnsemblBacteria; AAC77215; AAC77215; b4258.
DR EnsemblBacteria; BAE78255; BAE78255; BAE78255.
DR GeneID; 948785; -.
DR KEGG; ecj:JW4215; -.
DR KEGG; eco:b4258; -.
DR PATRIC; fig|1411691.4.peg.2446; -.
DR EchoBASE; EB1060; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_6; -.
DR InParanoid; P07118; -.
DR OMA; FATKLWN; -.
DR PhylomeDB; P07118; -.
DR BioCyc; EcoCyc:VALS-MON; -.
DR BioCyc; MetaCyc:VALS-MON; -.
DR BRENDA; 6.1.1.9; 2026.
DR SABIO-RK; P07118; -.
DR PRO; PR:P07118; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0004832; F:valine-tRNA ligase activity; IDA:EcoCyc.
DR GO; GO:0061475; P:cytosolic valyl-tRNA aminoacylation; IMP:EcoCyc.
DR GO; GO:0045903; P:positive regulation of translational fidelity; IMP:EcoCyc.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IMP:EcoCyc.
DR CDD; cd07962; Anticodon_Ia_Val; 1.
DR Gene3D; 1.10.287.380; -; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR Gene3D; 3.90.740.10; -; 2.
DR HAMAP; MF_02004; Val_tRNA_synth_type1; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033705; Anticodon_Ia_Val.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR010978; tRNA-bd_arm.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR InterPro; IPR019499; Val-tRNA_synth_tRNA-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR002303; Valyl-tRNA_ligase.
DR PANTHER; PTHR11946; PTHR11946; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR Pfam; PF10458; Val_tRNA-synt_C; 1.
DR PRINTS; PR00986; TRNASYNTHVAL.
DR SUPFAM; SSF46589; SSF46589; 1.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00422; valS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Ligase; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..951
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000106224"
FT COILED 880..944
FT /evidence="ECO:0000255"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 554..558
FT /note="'KMSKS' region"
FT BINDING 557
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MUTAGEN 222
FT /note="T->P: Produces mischarged Thr-tRNA(Val) and Cys-
FT tRNA(Val)."
FT /evidence="ECO:0000269|PubMed:11313495"
FT MUTAGEN 277
FT /note="K->A: Reduces posttransfer Thr-tRNA(Val) editing
FT rate significantly and alters amino acid discrimination in
FT the editing site, resulting in hydrolysis of the correctly
FT charged cognate product."
FT /evidence="ECO:0000269|PubMed:12475234"
FT CONFLICT 107
FT /note="R -> A (in Ref. 2; AAA24657)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="G -> D (in Ref. 6; AAP43521)"
FT /evidence="ECO:0000305"
FT CONFLICT 452
FT /note="D -> E (in Ref. 6; AAP43521)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="V -> A (in Ref. 6; AAP43521)"
FT /evidence="ECO:0000305"
FT CONFLICT 694
FT /note="S -> T (in Ref. 1; CAA29322)"
FT /evidence="ECO:0000305"
FT CONFLICT 833
FT /note="A -> R (in Ref. 2; AAA24657)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 951 AA; 108192 MW; 3FBE09CF1E7D40BC CRC64;
MEKTYNPQDI EQPLYEHWEK QGYFKPNGDE SQESFCIMIP PPNVTGSLHM GHAFQQTIMD
TMIRYQRMQG KNTLWQVGTD HAGIATQMVV ERKIAAEEGK TRHDYGREAF IDKIWEWKAE
SGGTITRQMR RLGNSVDWER ERFTMDEGLS NAVKEVFVRL YKEDLIYRGK RLVNWDPKLR
TAISDLEVEN RESKGSMWHI RYPLADGAKT ADGKDYLVVA TTRPETLLGD TGVAVNPEDP
RYKDLIGKYV ILPLVNRRIP IVGDEHADME KGTGCVKITP AHDFNDYEVG KRHALPMINI
LTFDGDIRES AQVFDTKGNE SDVYSSEIPA EFQKLERFAA RKAVVAAVDA LGLLEEIKPH
DLTVPYGDRG GVVIEPMLTD QWYVRADVLA KPAVEAVENG DIQFVPKQYE NMYFSWMRDI
QDWCISRQLW WGHRIPAWYD EAGNVYVGRN EDEVRKENNL GADVVLRQDE DVLDTWFSSA
LWTFSTLGWP ENTDALRQFH PTSVMVSGFD IIFFWIARMI MMTMHFIKDE NGKPQVPFHT
VYMTGLIRDD EGQKMSKSKG NVIDPLDMVD GISLPELLEK RTGNMMQPQL ADKIRKRTEK
QFPNGIEPHG TDALRFTLAA LASTGRDINW DMKRLEGYRN FCNKLWNASR FVLMNTEGQD
CGFNGGEMTL SLADRWILAE FNQTIKAYRE ALDSFRFDIA AGILYEFTWN QFCDWYLELT
KPVMNGGTEA ELRGTRHTLV TVLEGLLRLA HPIIPFITET IWQRVKVLCG ITADTIMLQP
FPQYDASQVD EAALADTEWL KQAIVAVRNI RAEMNIAPGK PLELLLRGCS ADAERRVNEN
RGFLQTLARL ESITVLPADD KGPVSVTKII DGAELLIPMA GLINKEDELA RLAKEVAKIE
GEISRIENKL ANEGFVARAP EAVIAKEREK LEGYAEAKAK LIEQQAVIAA L
