ID   SYV_BORPE               Reviewed;         960 AA.
AC   Q7VWK6;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=BP2203;
OS   Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257313;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
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; BX640417; CAE42481.1; -; Genomic_DNA.
DR   RefSeq; NP_880851.1; NC_002929.2.
DR   RefSeq; WP_010930794.1; NZ_CP039022.1.
DR   AlphaFoldDB; Q7VWK6; -.
DR   SMR; Q7VWK6; -.
DR   STRING; 257313.BP2203; -.
DR   GeneID; 45389094; -.
DR   KEGG; bpe:BP2203; -.
DR   PATRIC; fig|257313.5.peg.2377; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_4; -.
DR   OMA; FATKLWN; -.
DR   Proteomes; UP000002676; 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   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..960
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224447"
FT   COILED          893..958
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           61..71
FT                   /note="'HIGH' region"
FT   MOTIF           569..573
FT                   /note="'KMSKS' region"
FT   BINDING         572
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   960 AA;  107381 MW;  DCED70D7A01A7045 CRC64;
     MTDAAPNQPV NESQELSKSF EPAEIETRWY DEWAKRGYFD AGRHVETGTD PQPYVIQFPP
     PNVTGTLHMG HAFNQTIMDG LVRYHRMLGD DTVFVPGTDH AGIATQIVVE RQLDAQKVSR
     HDLGREKFVE KVWEWKEQSG STITGQVRRL GASADWPREY FTMDARMSRG VAETFVRLYQ
     QGLIYRGKRL VNWDPKLLTA VSDLEVQSEE VDGHMWHILY PFVDGPQTIT DQDGNTVTLR
     GMTIATTRPE TMLADGALCV HPDDPRYKHL LGKLVELPLC DRNIPIIADD FVDPDFGTGC
     VKITGAHDFN DYACALRHDI PLIVIFTLDA HINENGPKQF QGLERYEARQ AVVAELQAQQ
     YLVKVEPHKM MQPKGDRTGV VLEPMLTDQW FVAMSKPAPA GTLNPGKSIT EVALEAVADG
     RIAFYPENWT TIYNQWLNNI QDWCISRQLW WGHQIPAWYS EDGQVFVARS EEEAQEQARA
     AGVSGPLTRD PDILDTWFSS ALVPFTTFGW PEDTPDLRRY LPSSVLVTGF DIIFFWVARM
     VMLTMHMTGS VPFKHVYVHG LIRDADGQKM SKSKGNTLDP VDLIDGIDLK GLVRKRTFGL
     MHPKQAGAIE KATRRQYPDG IPAFGTDALR FTMAAYATLG RNINFDLKRC EGYRNFCNKL
     WNATRFVLMN TEGHALDGDG GELSFADRWI VSQLQALEAE VERGFADYRF DNVANALYRY
     VWDEYCDWYL ELAKVQIQQG TPAQQLGTRR TLIRVLEAVL RLAHPVIPFI TEELWQKVAL
     VAGKRTAGAV ASVSVQPYPR ANPQAVDAEA EAAVAELKSQ VEAVRALRGE MNLSPAQRVP
     LVAEGPTDVL SRNTPYLAAL AKLSEVEVVA ALPDAGAPVQ VVGDARLMLH VEIDVAAECA
     RLDKEIARLE GEIAKANGKL GNASFVERAP AAVVEQEKAR LAQFSETLEK VRGQRVKLGV