SYV_ECO57
ID SYV_ECO57 Reviewed; 951 AA.
AC Q8XCB3; Q7A8R1;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02004};
DE EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02004};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02004};
DE Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02004};
GN Name=valS {ECO:0000255|HAMAP-Rule:MF_02004};
GN OrderedLocusNames=Z5870, ECs5235;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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. {ECO:0000255|HAMAP-Rule:MF_02004}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_02004};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02004}.
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. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC activity. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02004}.
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DR EMBL; AE005174; AAG59457.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB38658.1; -; Genomic_DNA.
DR PIR; C91283; C91283.
DR PIR; E86124; E86124.
DR RefSeq; NP_313262.1; NC_002695.1.
DR RefSeq; WP_000416407.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8XCB3; -.
DR SMR; Q8XCB3; -.
DR STRING; 155864.EDL933_5607; -.
DR EnsemblBacteria; AAG59457; AAG59457; Z5870.
DR EnsemblBacteria; BAB38658; BAB38658; ECs_5235.
DR GeneID; 913806; -.
DR KEGG; ece:Z5870; -.
DR KEGG; ecs:ECs_5235; -.
DR PATRIC; fig|386585.9.peg.5472; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_6; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Coiled coil; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..951
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224477"
FT COILED 880..944
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
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:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 951 AA; 108178 MW; B276D5428FCDB9EC 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 EEEVRKENNL GADVALRQDE 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
