ID   SYV_LACPL               Reviewed;         889 AA.
AC   Q88UX7; F9UQM9;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 106.
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}; OrderedLocusNames=lp_2322;
OS   Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS   (Lactobacillus plantarum).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=220668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA   Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA   Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA   Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA   Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA   Siezen R.J.;
RT   "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=22156394; DOI=10.1128/jb.06275-11;
RA   Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA   Kleerebezem M., van Hijum S.A.;
RT   "Complete resequencing and reannotation of the Lactobacillus plantarum
RT   WCFS1 genome.";
RL   J. Bacteriol. 194:195-196(2012).
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; AL935263; CCC79518.1; -; Genomic_DNA.
DR   RefSeq; WP_011101712.1; NC_004567.2.
DR   RefSeq; YP_004890032.1; NC_004567.2.
DR   AlphaFoldDB; Q88UX7; -.
DR   SMR; Q88UX7; -.
DR   STRING; 220668.lp_2322; -.
DR   PRIDE; Q88UX7; -.
DR   EnsemblBacteria; CCC79518; CCC79518; lp_2322.
DR   KEGG; lpl:lp_2322; -.
DR   PATRIC; fig|220668.9.peg.1963; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_9; -.
DR   OMA; FATKLWN; -.
DR   PhylomeDB; Q88UX7; -.
DR   BioCyc; LPLA220668:G1GW0-2002-MON; -.
DR   Proteomes; UP000000432; 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; -; 1.
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; 2.
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..889
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224491"
FT   COILED          816..889
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           50..60
FT                   /note="'HIGH' region"
FT   MOTIF           532..536
FT                   /note="'KMSKS' region"
FT   BINDING         535
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   889 AA;  101526 MW;  9D875D34447942EA CRC64;
     MSEEPTTDMP TKYDPTAVEA GRYQTWLDQD LFKPSGDKKA KPYSIVIPPP NVTGKLHLGH
     AWDTTLQDII IRQKRMQGFD TLWLPGMDHA GIATQAKVEA KLREQGISRY DLGREKFIQQ
     VWDWKDEYAS IIKQQWAKMG LSLDYSRERF TMDDGLSDAV KKVFVDLYNK GLIYRGEYII
     NWDPQARTAL SDIEVIHKDD KGAFYHVKYP FADKDYTFNG KHYIEIATTR PETMMGDTAV
     AVNPSDDRYK ELVGKKVILP LAEREIPIIA DAYVDPEFGT GMVKITPAHD PNDFKVGNRH
     DLKRINTMND DASMNANAGK YEGMDRFEAR KAMVKDLEDQ DLMIKIDPIV HSVGHSERTD
     VQVEARLSTQ WFVKMKPLAE QALKNQEGDD AVDFIPKRFE DAFKQWMENI HDWVISRQLW
     WGHRIPAWYN KTTGETYVGV DGPKDPENWE QDPDVLDTWF SSALWPFSTM GWPNTDAEDF
     KRYFPTNTLV TGYDILPFWV SRMIFQSLEF TGRRPFKNVL LHGLIRDEHG VKMSKSLGNG
     IDPMDVIEKY GADALRWFLS NGSTAGQDVR FSYTKMDAAW NFINKIWNAS RYVIMNLGTM
     DKPELPAASD WTLADKWILS RLNATVKQVT TTFDKFDFGE AGRALYNFIW NDFCDWYIEM
     SKEVLTGDDA QAKANTQNVL AYVLDQILRL LHPIMPFVTE KIWLSMPHVG ESLVVAAYPV
     DHPEFDDETA ESDMASLIEL ITAVRSIRAE ANAKMSSAVD LLIKTDNTRL QAVFKANEDY
     IQRFAHPKTL SIGADVVAPK LAMTQVISDA EVYIPLAELV DLDEEVKKLE KEQAKFESEV
     ARATKKLGNE RFVANAPEDV VNSEKEKLAD NQTKLAALKQ RLVDIKAEA