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P18255 (SYT1_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Threonine--tRNA ligase 1
EC=6.1.1.3
Alternative name(s):
Threonyl-tRNA synthetase 1
Short name=ThrRS 1
Gene names
Name:thrS
Synonyms:thrSV
Ordered Locus Names:BSU28950
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length643 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr). HAMAP MF_00184

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_00184

Subunit structure

Homodimer By similarity. HAMAP MF_00184

Subcellular location

Cytoplasm HAMAP MF_00184.

Developmental stage

Expressed during vegetative growth. HAMAP MF_00184

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processthreonyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

threonine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 643643Threonine--tRNA ligase 1 HAMAP MF_00184
PRO_0000100938

Regions

Region245 – 542298Catalytic HAMAP MF_00184

Sites

Metal binding3381Zinc; catalytic By similarity
Metal binding3891Zinc; catalytic By similarity
Metal binding5191Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
P18255 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: 11DFF31CF5800ADE

FASTA64373,515
        10         20         30         40         50         60 
MSDMVKITFP DGAVKEFAKG TTTEDIAASI SPGLKKKSLA GKLNGKEIDL RTPINEDGTV 

        70         80         90        100        110        120 
EIITEGSEEG LQIMRHSAAH LLAQAIKRIY KDVKFGVGPV IENGFYYDVE MDEAITPEDL 

       130        140        150        160        170        180 
PKIEKEMKKI VNANLPIVRK EVSREEAKAR FAEIGDDLKL ELLDAIPEGE TVSIYEQGEF 

       190        200        210        220        230        240 
FDLCRGVHVP STGKIKEFKL LSLAGAYWRG DSKNQMLQRV YGTAFFKKAD LEEHLRMLEE 

       250        260        270        280        290        300 
AKERDHRKLG KELKLFANSQ KVGQGLPLWL PKGATIRRVI ERYIVDKEIS LGYEHVYTPV 

       310        320        330        340        350        360 
LGSKELYETS GHWDHYQEGM FPPMEMDNET LVLRPMNCPH HMMIYKQDIH SYRELPIRIA 

       370        380        390        400        410        420 
ELGTMHRYEM SGALSGLQRV RGMTLNDAHI FVRPDQIKDE FIRTVRLIQD VYEDFGLSDY 

       430        440        450        460        470        480 
TFRLSYRDPE DTEKYFDDDE MWNKAQSMLK EAMDEIGHDY YEAEGEAAFY GPKLDVQVKT 

       490        500        510        520        530        540 
AIGKEETLST VQLDFLLPER FDLTYIGEDG KQHRPVVIHR GVVSTMERFV AFLIEEHKGA 

       550        560        570        580        590        600 
LPTWLAPVQF QVIPVSPAVH LDYAKKVQER LQCEGLRVEV DSRDEKIGYK IREAQMQKIP 

       610        620        630        640 
YMLVVGDQEA ENGAVNVRKY GEQNSETISL DEFVKKAVAE AKK

« Hide

References

« Hide 'large scale' references
[1]"Independent genes for two threonyl-tRNA synthetases in Bacillus subtilis."
Putzer H., Brakhage A., Grunberg-Manago M.
J. Bacteriol. 172:4593-4602(1990) [PubMed: 2115870] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis chromosome containing genes responsible for stress responses, the utilization of plant cell walls and primary metabolism."
Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J., Emmerson P.T., Harwood C.R.
Microbiology 142:3067-3078(1996) [PubMed: 8969504] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[3]"Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region."
Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.
Microbiology 143:3431-3441(1997) [PubMed: 9387221] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[4]"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. expand/collapse author list , 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.
[5]"Nucleotide sequence and organization of dnaB gene and neighbouring genes on the Bacillus subtilis chromosome."
Ogasawara N., Moriya S., Mazza P.G., Yoshikawa H.
Nucleic Acids Res. 14:9989-9999(1986) [PubMed: 3027671] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-180.
[6]"Co-ordinate expression of the two threonyl-tRNA synthetase genes in Bacillus subtilis: control by transcriptional antitermination involving a conserved regulatory sequence."
Putzer H., Gendron N., Grunberg-Manago M.
EMBO J. 11:3117-3127(1992) [PubMed: 1379177] [Abstract]
Cited for: EXPRESSION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M36594 Genomic DNA. Translation: AAA22864.1.
Z75208 Genomic DNA. Translation: CAA99608.1.
AF008220 Genomic DNA. Translation: AAC00362.1.
AL009126 Genomic DNA. Translation: CAB14855.1.
X04963 Genomic DNA. Translation: CAA28636.1.
PIRYSBST1. B37770.
RefSeqNP_390773.1. NC_000964.3.

3D structure databases

ProteinModelPortalP18255.
SMRP18255. Positions 5-642.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000003316; EBBACP00000003316; EBBACG00000003309.
GeneID937410.
GenomeReviewsGene locus BSU28950 in contig AL009126_GR.
KEGGbsu:BSU28950.
NMPDRfig|224308.1.peg.2898.
PATRIC18977682. VBIBacSub10457_3029.

Organism-specific databases

GenoListBSU28950. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000001167.
HOGENOMHBG352811.
OMAGRKWQLG.
PhylomeDBP18255.
ProtClustDBPRK00413.

Enzyme and pathway databases

BioCycBSUB:BSU28950-MONOMER.

Family and domain databases

HAMAPMF_00184. Thr_tRNA_synth.
[Tree]
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR012675. Beta-grasp_ferredoxin-type.
IPR004095. TGS.
IPR012676. TGS-like.
IPR002320. Thr-tRNA-synth_IIa.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view]
Gene3DG3DSA:3.40.50.800. Anticodon_bd. 1 hit.
G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
KOK01868.
PfamPF03129. HGTP_anticodon. 1 hit.
PF02824. TGS. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSPR01047. TRNASYNTHTHR.
SMARTSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMSSF52954. Anticodon_bd. 1 hit.
SSF81271. TGS-like. 1 hit.
SSF55186. Thr/Ala-tRNA-synth_IIc_edit. 1 hit.
TIGRFAMsTIGR00418. ThrS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYT1_BACSU
AccessionPrimary (citable) accession number: P18255
Secondary accession number(s): P06570
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: November 1, 1990
Last modified: January 25, 2012
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents