ID   SYV_BACSU               Reviewed;         880 AA.
AC   Q05873;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 3.
DT   07-JUL-2009, entry version 69.
DE   RecName: Full=Valyl-tRNA synthetase;
DE            EC=6.1.1.9;
DE   AltName: Full=Valine--tRNA ligase;
DE            Short=ValRS;
GN   Name=valS; OrderedLocusNames=BSU28090;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, INDUCTION
RP   MECHANISM, OPERON STRUCTURE, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168;
RX   PubMed=9098041;
RA   Luo D., Leautey J., Grunberg-Manago M., Putzer H.;
RT   "Structure and regulation of expression of the Bacillus subtilis
RT   valyl-tRNA synthetase gene.";
RL   J. Bacteriol. 179:2472-2478(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   SEQUENCE REVISION TO 379.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G.,
RA   Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus
RT   subtilis 168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 825-880.
RC   STRAIN=168 / PY79;
RX   MEDLINE=93123172; PubMed=8419299;
RA   Margolis P.S., Driks A., Losick R.;
RT   "Sporulation gene spoIIB from Bacillus subtilis.";
RL   J. Bacteriol. 175:528-540(1993).
CC   -!- FUNCTION: As ValRS can inadvertently accommodate and process
CC       structurally similar amino acids such as threonine, to avoid such
CC       errors, it has a "posttransfer" editing activity that hydrolyzes
CC       mischarged Thr-tRNA(Val) in a tRNA-dependent manner (By
CC       similarity). Catalyzes the attachment of valine to tRNA(Val).
CC   -!- CATALYTIC ACTIVITY: ATP + L-valine + tRNA(Val) = AMP + diphosphate
CC       + L-valyl-tRNA(Val).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- INDUCTION: By valine starvation. Is transcribed by itself and in
CC       an operon with folC. A GUC triplet (Val, the specifier codon) 190
CC       nucleotides upstream of the initiator codon confers induction upon
CC       valaine starvation; replacing it with ACC (Thr) confers induction
CC       upon threonine starvation, replacing it with UAA (stop), renders
CC       the gene uninducible. Negatively regulates its own transcription;
CC       this depends on the presence of the GUC specifier codon.
CC   -!- DOMAIN: ValRS has two distinct active sites: one for
CC       aminoacylation and one for editing. The misactivated threonine is
CC       translocated from the active site to the editing site (By
CC       similarity).
CC   -!- DOMAIN: The C-terminal coiled-coil domain is crucial for
CC       aminoacylation activity (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene grow normally,
CC       suggesting there is a second functional gene with valine-tRNA
CC       synthetase activity in B.subtilis.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. ValS type 1 subfamily.
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DR   EMBL; X77239; CAA54458.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14769.2; -; Genomic_DNA.
DR   EMBL; L04520; AAB59020.1; -; Genomic_DNA.
DR   PIR; S41420; S41420.
DR   RefSeq; NP_390687.1; -.
DR   HSSP; P96142; 1IVS.
DR   GeneID; 937491; -.
DR   GenomeReviews; AL009126_GR; BSU28090.
DR   KEGG; bsu:BSU28090; -.
DR   NMPDR; fig|224308.1.peg.2812; -.
DR   SubtiList; BG10321; valS.
DR   HOGENOM; Q05873; -.
DR   OMA; Q05873; TDQWYVS.
DR   BioCyc; BSUB224308:BSU2805-MON; -.
DR   BRENDA; 6.1.1.9; 150.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004832; F:valine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_02004; -; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR013155; V/L/I-tRNA-synth_anticodon-bd.
DR   InterPro; IPR002303; Val-tRNA_synth_Ia.
DR   InterPro; IPR011321; Val-tRNA_synth_Ia_C.
DR   InterPro; IPR019754; Val-tRNA_synth_Ia_N.
DR   InterPro; IPR019499; Val-tRNA_synth_Ia_tRNA-bd.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   Gene3D; G3DSA:1.10.287.380; Val-tRNA_synth_Ia_C; 1.
DR   PANTHER; PTHR11946:SF5; tRNA-synt_val; 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   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;
KW   Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW   Protein biosynthesis; Repressor.
FT   CHAIN         1    880       Valyl-tRNA synthetase.
FT                                /FTId=PRO_0000106214.
FT   COILED      809    879       Potential.
FT   MOTIF        49     59       "HIGH" region.
FT   MOTIF       525    529       "KMSKS" region.
FT   BINDING     528    528       ATP (By similarity).
FT   CONFLICT    379    379       Q -> E (in Ref. 1; CAA54458).
SQ   SEQUENCE   880 AA;  101745 MW;  EAA0A4508F6283D7 CRC64;
     METNEQTMPT KYDPAAVEKD RYDFWLKGKF FEAGSDQTKE PYSVVIPPPN VTGRLHLGHA
     WDTTLQDIVT RMKRMQGYDV LWLPGMDHAG IATQAKVEAK LREEGKSRYD LGREKFLEET
     WKWKEEYADF IRSQWAKLGL GLDYSRERFT LDEGLSKAVR EVFVKLYEKG LIYRGEYIIN
     WDPATKTALS DIEVIYKDVQ GAFYHMSYPL ADGSGSIEIA TTRPETMLGD TAVAVHPEDE
     RYKHLIGKTV ILPIVNREIP IVGDDYVDME FGSGAVKITP AHDPNDFELG NRHNLERILV
     MNEDGTMNEN ALQYQGMDRF ECRKKLVKDL QEAGVLFKIE DHMHSVGHSE RSGAVVEPYL
     STQWFVRMQP LADAAIELQK KEEKVNFVPD RFEKTYLHWM ENIRDWCISR QLWWGHRIPA
     WYHKETGELY VGLEAPEDSE NWEQDTDVLD TWFSSALWPF STMGWPDVTA EDFKRYYPTD
     VLVTGYDIIF FWVSRMIFQG IEFTGERPFK DVLIHGLIRD EQGRKMSKSL GNGVDPMDVI
     DKYGADSLRY FLATGSSPGQ DLRFSYEKVE STWNFANKIW NASRFALMNM DGMTYDELDL
     SGEKSVADKW ILTRLNETIE HVTQLADRYE FGEVGRHLYN FIWDDFCDWY IEMAKLPLYG
     EDEAAKKTTR SILAYVLDQT MRLLHPFMPF LTEEIWQHLP HQGESITVSQ WPAVVPEHTD
     TEAAADMKLL VELIRSVRNI RSEVNTPMSK QVELYIKTST DEIASRLEAN RSYVERFTNP
     SVLKIGTDIE AVDKAMTAVV SGAEVILPLE GLINIDEEIA RLQKEFDKLT KEVERVQKKL
     GNEGFMKKAP AHVIDEEREK EKDYVAKRDA VQKRMAELKG
//