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P18256 (SYT2_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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 2
EC=6.1.1.3
Alternative name(s):
Threonyl-tRNA synthetase 2
Short name=ThrRS 2
Gene names
Name:thrZ
Synonyms:thrS2
Ordered Locus Names:BSU37560
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length638 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

Normally not expressed. Its expression is induced when that of thrS is reduced. 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 – 638638Threonine--tRNA ligase 2 HAMAP MF_00184
PRO_0000100939

Regions

Region245 – 535291Catalytic HAMAP MF_00184

Sites

Metal binding3361Zinc; catalytic By similarity
Metal binding3871Zinc; catalytic By similarity
Metal binding5121Zinc; catalytic By similarity

Experimental info

Sequence conflict741L → V in AAA22863. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P18256 [UniParc].

Last modified July 28, 2009. Version 2.
Checksum: A958F85642700450

FASTA63873,388
        10         20         30         40         50         60 
MSKHVHIQLP DGQIQEYPKG ITIKEAAGSI SSSLQKKAAA GQVNGKLVDL SFKLEEDAEL 

        70         80         90        100        110        120 
SIVTLDSQEG LQVLRHTTAH VLAQAVKRLY GEVSLGVGPV ILDGFYYDMK LGKSLASGDL 

       130        140        150        160        170        180 
EAIEKEMKNI INENLEIKRI EVSYEEAEEL FAQKDERLKL EILKDIPRGE DITLYQQGEF 

       190        200        210        220        230        240 
VDLCRGPHLP STGMIKAFKL TRVSGAYWRG DSKNEVLQRV YGVAFQKKKD LDAHLHMLEE 

       250        260        270        280        290        300 
AAKRDHRKLG KQLGLFMFSE EAPGMPFYLP KGQIVRNELE RFSRELQTNA GYDEVRTPFM 

       310        320        330        340        350        360 
MNQRLWEQSG HWDHYRDNMY FSEVDDTRFA MKPMNCPGHM LIFKNSLYSY RDLPIRMAEF 

       370        380        390        400        410        420 
GQVHRHEYSG ALNGMLRVRT FCQDDAHIFV REDQIESEIK EAIRLIDEVY RTFGFEYSVE 

       430        440        450        460        470        480 
LSTRPEDSLG DDSLWEASER ALARVLEELG LSYEINEGDG AFYGPKIDFH IKDALKRSHQ 

       490        500        510        520        530        540 
CATIQLDFQM PEKFDLTYIN ELNEKVRPVV IHRAVFGSID RFFGILIEHY GGAFPVWLAP 

       550        560        570        580        590        600 
IQVQIIPVSH VHLDYCRKVQ AELKQAGIRA GIDERNEKLG YKIRESQVQK IPYVLVLGDH 

       610        620        630 
EEQENAVNVR RFGHQQNEHV PFQTFKDKLV KQVENRGM

« 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 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.
[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 74.
[4]"The Bacillus subtilis genome from gerBC (311 degrees) to licR (334 degrees)."
Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V., Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G., Kunst F., Danchin A., Glaser P.
Microbiology 143:3313-3328(1997) [PubMed: 9353933] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-638.
Strain: 168.
[5]"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		M36593 Genomic DNA. Translation: AAA22863.1.
AL009126 Genomic DNA. Translation: CAB15783.2.
Z80360 Genomic DNA. Translation: CAB02510.1.
PIRYSBST2. A37770.
RefSeqNP_391636.2. NC_000964.3.

3D structure databases

ProteinModelPortalP18256.
SMRP18256. Positions 1-637.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000001943; EBBACP00000001943; EBBACG00000001940.
GeneID937135.
GenomeReviewsGene locus BSU37560 in contig AL009126_GR.
KEGGbsu:BSU37560.
NMPDRfig|224308.1.peg.3762.
PATRIC18979548. VBIBacSub10457_3936.

Organism-specific databases

GenoListBSU37560. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000001167.
HOGENOMHBG352811.
PhylomeDBP18256.
ProtClustDBPRK12444.

Enzyme and pathway databases

BioCycBSUB:BSU37560-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 nameSYT2_BACSU
AccessionPrimary (citable) accession number: P18256
Secondary accession number(s): P70992
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: July 28, 2009
Last modified: January 25, 2012
This is version 109 of the entry and version 2 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