Q05873 (SYV_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Valine--tRNA ligase
EC=6.1.1.9

Alternative name(s):
Valyl-tRNA synthetase
Short name=ValRS

Gene names

Name:	valS
Ordered Locus Names:	BSU28090

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	880 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a "posttransfer" editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner By similarity. Catalyzes the attachment of valine to tRNA(Val). HAMAP MF_02004
Catalytic activity	ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val). HAMAP MF_02004
Subunit structure	Monomer By similarity. HAMAP MF_02004
Subcellular location	Cytoplasm By similarity HAMAP MF_02004.
Induction	By valine starvation. Is transcribed by itself and in an operon with folC. A GUC triplet (Val, the specifier codon) 190 nucleotides upstream of the initiator codon confers induction upon valaine starvation; replacing it with ACC (Thr) confers induction upon threonine starvation, replacing it with UAA (stop), renders the gene uninducible. Negatively regulates its own transcription; this depends on the presence of the GUC specifier codon. Ref.1
Domain	ValRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated threonine is translocated from the active site to the editing site By similarity. HAMAP MF_02004 The C-terminal coiled-coil domain is crucial for aminoacylation activity By similarity. HAMAP MF_02004
Disruption phenotype	Cells lacking this gene grow normally, suggesting there is a second functional gene with valine-tRNA synthetase activity in B.subtilis. Ref.1
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase Repressor
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	valyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW valine-tRNA ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 880	880	Valine--tRNA ligase HAMAP MF_02004		PRO_0000106214
Regions
	Coiled coil	809 – 879	71	Potential
	Motif	49 – 59	11	"HIGH" region HAMAP MF_02004
	Motif	525 – 529	5	"KMSKS" region HAMAP MF_02004
Sites
	Binding site	528	1	ATP By similarity
Experimental info
	Sequence conflict	379	1	Q → E in CAA54458. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q05873 [UniParc]. Last modified July 7, 2009. Version 3. Checksum: EAA0A4508F6283D7	FASTA	880	101,745
	10 20 30 40 50 60 METNEQTMPT KYDPAAVEKD RYDFWLKGKF FEAGSDQTKE PYSVVIPPPN VTGRLHLGHA 70 80 90 100 110 120 WDTTLQDIVT RMKRMQGYDV LWLPGMDHAG IATQAKVEAK LREEGKSRYD LGREKFLEET 130 140 150 160 170 180 WKWKEEYADF IRSQWAKLGL GLDYSRERFT LDEGLSKAVR EVFVKLYEKG LIYRGEYIIN 190 200 210 220 230 240 WDPATKTALS DIEVIYKDVQ GAFYHMSYPL ADGSGSIEIA TTRPETMLGD TAVAVHPEDE 250 260 270 280 290 300 RYKHLIGKTV ILPIVNREIP IVGDDYVDME FGSGAVKITP AHDPNDFELG NRHNLERILV 310 320 330 340 350 360 MNEDGTMNEN ALQYQGMDRF ECRKKLVKDL QEAGVLFKIE DHMHSVGHSE RSGAVVEPYL 370 380 390 400 410 420 STQWFVRMQP LADAAIELQK KEEKVNFVPD RFEKTYLHWM ENIRDWCISR QLWWGHRIPA 430 440 450 460 470 480 WYHKETGELY VGLEAPEDSE NWEQDTDVLD TWFSSALWPF STMGWPDVTA EDFKRYYPTD 490 500 510 520 530 540 VLVTGYDIIF FWVSRMIFQG IEFTGERPFK DVLIHGLIRD EQGRKMSKSL GNGVDPMDVI 550 560 570 580 590 600 DKYGADSLRY FLATGSSPGQ DLRFSYEKVE STWNFANKIW NASRFALMNM DGMTYDELDL 610 620 630 640 650 660 SGEKSVADKW ILTRLNETIE HVTQLADRYE FGEVGRHLYN FIWDDFCDWY IEMAKLPLYG 670 680 690 700 710 720 EDEAAKKTTR SILAYVLDQT MRLLHPFMPF LTEEIWQHLP HQGESITVSQ WPAVVPEHTD 730 740 750 760 770 780 TEAAADMKLL VELIRSVRNI RSEVNTPMSK QVELYIKTST DEIASRLEAN RSYVERFTNP 790 800 810 820 830 840 SVLKIGTDIE AVDKAMTAVV SGAEVILPLE GLINIDEEIA RLQKEFDKLT KEVERVQKKL 850 860 870 880 GNEGFMKKAP AHVIDEEREK EKDYVAKRDA VQKRMAELKG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and regulation of expression of the Bacillus subtilis valyl-tRNA synthetase gene." Luo D., Leautey J., Grunberg-Manago M., Putzer H. J. Bacteriol. 179:2472-2478(1997) [PubMed: 9098041] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, INDUCTION MECHANISM, OPERON STRUCTURE, DISRUPTION PHENOTYPE. Strain: 168.
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later." Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A. Microbiology 155:1758-1775(2009) [PubMed: 19383706] [Abstract] Cited for: SEQUENCE REVISION TO 379.
[4]	"Sporulation gene spoIIB from Bacillus subtilis." Margolis P.S., Driks A., Losick R. J. Bacteriol. 175:528-540(1993) [PubMed: 8419299] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 825-880. Strain: 168 / PY79.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X77239 Genomic DNA. Translation: CAA54458.1. AL009126 Genomic DNA. Translation: CAB14769.2. L04520 Genomic DNA. Translation: AAB59020.1.
PIR	S41420.
RefSeq	NP_390687.2. NC_000964.3.
3D structure databases
ProteinModelPortal	Q05873.
SMR	Q05873. Positions 9-746.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000000914; EBBACP00000000914; EBBACG00000000912.
GeneID	937491.
GenomeReviews	Gene locus BSU28090 in contig AL009126_GR.
KEGG	bsu:BSU28090.
NMPDR	fig|224308.1.peg.2812.
PATRIC	18977492. VBIBacSub10457_2935.
Organism-specific databases
GenoList	BSU28090. [Micado]
Phylogenomic databases
GeneTree	EBGT00070000031886.
HOGENOM	HBG577712.
PhylomeDB	Q05873.
ProtClustDB	PRK05729.
Enzyme and pathway databases
BioCyc	BSUB:BSU28090-MONOMER.
Family and domain databases
HAMAP	MF_02004. Val_tRNA_synth_type1. [Tree]
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR002300. aa-tRNA-synth_Ia. IPR014729. Rossmann-like_a/b/a_fold. IPR010978. tRNA-bd_arm. IPR009080. tRNAsynth_1a_anticodon-bd. IPR013155. V/L/I-tRNA-synth_anticodon-bd. IPR011321. Val-tRNA_synth_Ia_C. IPR019499. Val-tRNA_synth_Ia_tRNA-bd. IPR009008. Val/Leu/Ile-tRNA-synth_edit. IPR002303. Valyl-tRNA_synthetase. [Graphical view]
Gene3D	G3DSA:3.90.740.10. G3DSA:3.90.740.10. 1 hit. G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits. G3DSA:1.10.287.380. Val-tRNA_synth_Ia_C. 1 hit.
KO	K01873.
PANTHER	PTHR11946:SF5. tRNA-synt_val. 1 hit.
Pfam	PF08264. Anticodon_1. 1 hit. PF00133. tRNA-synt_1. 1 hit. PF10458. Val_tRNA-synt_C. 1 hit. [Graphical view]
PRINTS	PR00986. TRNASYNTHVAL.
SUPFAM	SSF46589. tRNA_binding_arm. 1 hit. SSF47323. tRNAsyn_1a_bind. 1 hit. SSF50677. ValRS_IleRS_edit. 1 hit.
TIGRFAMs	TIGR00422. ValS. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYV_BACSU

Accession

Primary (citable) accession number: Q05873

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	July 7, 2009
Last modified:	January 25, 2012
This is version 91 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program