ID   SYV_STAAM               Reviewed;         876 AA.
AC   Q931Q1;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 121.
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=SAV1663;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(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; BA000017; BAB57825.1; -; Genomic_DNA.
DR   RefSeq; WP_000425350.1; NC_002758.2.
DR   AlphaFoldDB; Q931Q1; -.
DR   SMR; Q931Q1; -.
DR   World-2DPAGE; 0002:Q931Q1; -.
DR   PaxDb; Q931Q1; -.
DR   EnsemblBacteria; BAB57825; BAB57825; SAV1663.
DR   KEGG; sav:SAV1663; -.
DR   HOGENOM; CLU_001493_0_2_9; -.
DR   OMA; FATKLWN; -.
DR   PhylomeDB; Q931Q1; -.
DR   BioCyc; SAUR158878:SAV_RS08920-MON; -.
DR   Proteomes; UP000002481; 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; 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.
FT   CHAIN           1..876
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224563"
FT   COILED          805..876
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           44..54
FT                   /note="'HIGH' region"
FT   MOTIF           520..524
FT                   /note="'KMSKS' region"
FT   BINDING         523
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   876 AA;  101772 MW;  F76294F4D0C2055D CRC64;
     MEMKPKYDPR EVEAGRYEEW VKNGYFKPSE DKSKETYTIV IPPPNVTGKL HLGHAWDTTL
     QDIITRMKRM QGYDTLYLPG MDHAGIATQA KVEAKLNEQG ITRYDLGREK FLEQAWDWKE
     EYASFIRAQW AKLGLGLDYS RERFTLDEGL SKAVKKVFVD LYNKGIIYRG ERIINWDPKA
     RTALSDIEVI HEDVQGAFYH FKYPYADGEG FIEIATTRPE TMLGDTAIVV NPNDERYKDV
     IGKTVILPIV GRELPILADE YVDIDFGSGA MKVTPAHDPN DFEIGQRHQL ENIIVMDENG
     KMNDKAGKYE GMDRFDCRKQ LVKDLKEQDL VIKIEDHFHS VGHSERSGAV VEPYLSTQWF
     VRMEDLAKRS LDNQKTDDRI DFYPQRFEHT FNQWMENIRD WTISRQLWWG HQIPAWYHKE
     TGEIYVGEEA PTDIENWQQD EDVLDTWFSS ALWPFSTLGW PDLESEDFKR YYPTNALVTG
     YDIIFFWVAR MIFQGLEFTD RRPFNDVLLH GLVRAEDGRK MSKSLGNGVD PMDVIDEYGA
     DSLRYFLATG SSPGHDLRYS TEKVESVWNF INKIWNGARF SLMNIGEDFK VEDIDLSGNL
     SLADKWILTR LNETIATVTD LSDKYEFGEV GRALYNFIWD DFCDWYIEMS KIPMNSNDEE
     QKQVTRSVLS YTLDNIMRML HPFMPFVTEK IWQSLPHEGD TIVKASWPEV RESLIFEESK
     QTMQQLVEII KSVRQSRVEV NTPLSKEIPI LIQAKDKEIE TTLSQNKDYL IKFCNPSTLN
     ISTDVEIPEK AMTSVVIAGK VVLPLEGLID MDKEISRLEK ELAKLQSELD RVDKKLSNEN
     FVSKAPEKVI NEEKRKKQDY QEKYDGVKAR IEQLKA