Reviewed, UniProtKB/Swiss-Prot Q7WKF7 (SYT_BORBR)

Names and origin

Protein names

Recommended name:
    Threonyl-tRNA synthetase
    EC=6.1.1.3
Alternative name(s):
    Threonine--tRNA ligase
      Short name=ThrRS

Gene names

Name:	thrS
Ordered Locus Names:	BB2150

Organism

Bordetella bronchiseptica (Alcaligenes bronchisepticus) [Complete proteome] [HAMAP]

Taxonomic identifier

518 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	649 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm. HAMAP MF_00184
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	threonyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP threonine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 649	649	Threonyl-tRNA synthetase HAMAP MF_00184		PRO_1000020347
Regions
	Region	247 – 538	292	Catalytic HAMAP MF_00184
Sites
	Metal binding	338	1	Zinc; catalytic By similarity
	Metal binding	389	1	Zinc; catalytic By similarity
	Metal binding	515	1	Zinc; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7WKF7-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: D67226AFDF415101	FASTA	649	73,324
	10 20 30 40 50 60 MVQITLPDGS QRQYPGPVTV AEVAQSIGAG LAKAALAGRV AFDGAEPRLV DTSFRIDNDA 70 80 90 100 110 120 QLAIVTAKDA DGLDLIRHST AHLLAYAVKS LFPDAQVTIG PVIDNGFYYD FSYKRPFTPE 130 140 150 160 170 180 DLQAIEKKMA ELARKDEVVT REEWSRDEAV AYFKGIGEVY KAEIIASIPS NETLSLYREG 190 200 210 220 230 240 DFIDLCRGPH VPSTGKLKVF KLMKVAGAYW RGDSKNEMLQ RIYGTAWASK DDQDAYLHML 250 260 270 280 290 300 EEAERRDHRK IGRELDLFHF QDEAPGLIFW HPKGWALWQQ VEQYMRKVYQ DNGYQEVKAP 310 320 330 340 350 360 QILDLTLWKK TGHWDNYREN MFTTESENRV YGLKPMNCPG HVQIFNAGLH SYRELPLRYG 370 380 390 400 410 420 EFGQCHRNEP SGSLHGMMRV RGFTQDDGHI FCTEDQLQDE CAAFTALLQK VYKDFGFTEV 430 440 450 460 470 480 LYKVATRPEK RIGSDEIWDK AETALMESLR RTGCEFEISP GEGAFYGPKV EYTLKDAIGR 490 500 510 520 530 540 HWQCGTIQVD FSMPVRLGAE YVDQNDQRRP PVMLHRAILG SLERFIGMLI ENHAGAMPPW 550 560 570 580 590 600 LAPLQAVVCC ISEHSAEYAA QITQSLKKQG FRVQADLRGE KITRKIREHS LQKIPYLLVV 610 620 630 640 GDKEMQNGTV AVRGLGGLDL GVIALDDFIA RLAEDISTRR NVTQLASAA

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RB50 / ATCC BAA-588 / NCTC 13252.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX640443 Genomic DNA. Translation: CAE32646.1.
RefSeq	NP_888693.1.
3D structure databases
HSSP	HSSP built from PDB template 1EVL based on UniProtKB P00955.
ModBase	Search...
Genome annotation databases
GeneID	2661457.
GenomeReviews	Gene locus BB2150 in contig BX470250_GR.
KEGG	bbr:BB2150.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q7WKF7.
OMA	NTKIAIG.
Enzyme and pathway databases
BioCyc	BBRO257310:BB2150-MON.
BRENDA	6.1.1.3. 413.
Family and domain databases
HAMAP	MF_00184. [Tree]
InterPro	IPR002314. aa-tRNA-synt_IIb_cons-reg. IPR006195. aa-tRNA-synth_II_cons-reg. IPR004154. Anticodon_bd. IPR012675. b-grasp_ferredoxin-like. IPR004095. TGS. IPR002320. Thr-tRNA-synth_IIa. IPR018158. Thr-tRNA-synth_IIa_cons-reg. IPR012947. tRNA_SAD. [Graphical view]
Gene3D	G3DSA:3.40.50.800. Anticodon_bd. 1 hit. G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
Pfam	PF03129. HGTP_anticodon. 1 hit. PF02824. TGS. 1 hit. PF00587. tRNA-synt_2b. 1 hit. PF07973. tRNA_SAD. 1 hit. [Graphical view]
PRINTS	PR01047. TRNASYNTHTHR.
TIGRFAMs	TIGR00418. thrS. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYT_BORBR

Accession

Primary (citable) accession number: Q7WKF7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	October 1, 2003
Last modified:	November 3, 2009
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)