ID   SYV_STAAN               Reviewed;         876 AA.
AC   Q99TJ8;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 125.
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=SA1488;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N315;
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).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=N315;
RA   Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT   "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT   aureus strain N315.";
RL   Submitted (OCT-2007) to UniProtKB.
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; BA000018; BAB42754.1; -; Genomic_DNA.
DR   PIR; E89949; E89949.
DR   RefSeq; WP_000425353.1; NC_002745.2.
DR   AlphaFoldDB; Q99TJ8; -.
DR   SMR; Q99TJ8; -.
DR   EnsemblBacteria; BAB42754; BAB42754; BAB42754.
DR   KEGG; sau:SA1488; -.
DR   HOGENOM; CLU_001493_0_2_9; -.
DR   OMA; FATKLWN; -.
DR   Proteomes; UP000000751; 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   1: Evidence at protein level;
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_0000224565"
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;  101724 MW;  F7629339DD15155D 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 VIKIEDHVHS 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