SYV_BACSU
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 03-AUG-2022, entry version 149.
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=BSU28090;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, INDUCTION MECHANISM,
RP OPERON STRUCTURE, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=9098041; DOI=10.1128/jb.179.8.2472-2478.1997;
RA Luo D., Leautey J., Grunberg-Manago M., Putzer H.;
RT "Structure and regulation of expression of the Bacillus subtilis valyl-tRNA
RT synthetase gene.";
RL J. Bacteriol. 179:2472-2478(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., 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., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., 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., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 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 PubMed=8419299; DOI=10.1128/jb.175.2.528-540.1993;
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 similarity).
CC Catalyzes the attachment of valine to tRNA(Val). {ECO:0000250}.
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 -!- INDUCTION: By valine starvation. Is transcribed by itself and in an
CC 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 upon
CC threonine starvation, replacing it with UAA (stop), renders the gene
CC uninducible. Negatively regulates its own transcription; this depends
CC on the presence of the GUC specifier codon.
CC {ECO:0000269|PubMed:9098041}.
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 -!- DISRUPTION PHENOTYPE: Cells lacking this gene grow normally, suggesting
CC there is a second functional gene with valine-tRNA synthetase activity
CC in B.subtilis. {ECO:0000269|PubMed:9098041}.
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; 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_390687.2; NC_000964.3.
DR RefSeq; WP_004398606.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; Q05873; -.
DR SMR; Q05873; -.
DR STRING; 224308.BSU28090; -.
DR jPOST; Q05873; -.
DR PaxDb; Q05873; -.
DR PRIDE; Q05873; -.
DR EnsemblBacteria; CAB14769; CAB14769; BSU_28090.
DR GeneID; 937491; -.
DR KEGG; bsu:BSU28090; -.
DR PATRIC; fig|224308.179.peg.3051; -.
DR eggNOG; COG0525; Bacteria.
DR InParanoid; Q05873; -.
DR OMA; FATKLWN; -.
DR PhylomeDB; Q05873; -.
DR BioCyc; BSUB:BSU28090-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central.
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; Reference proteome; Repressor.
FT CHAIN 1..880
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000106214"
FT COILED 809..879
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 49..59
FT /note="'HIGH' region"
FT MOTIF 525..529
FT /note="'KMSKS' region"
FT BINDING 528
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT CONFLICT 379
FT /note="Q -> E (in Ref. 1; CAA54458)"
FT /evidence="ECO:0000305"
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
