Reviewed, UniProtKB/Swiss-Prot Q6FZZ7 (SYT_BARQU)

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:	BQ05510

Organism

Bartonella quintana (Rochalimaea quintana) [Complete proteome] [HAMAP]

Taxonomic identifier

803 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bartonellaceae › Bartonella

Protein attributes

Sequence length	658 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 – 658	658	Threonyl-tRNA synthetase HAMAP MF_00184		PRO_0000100942
Regions
	Region	246 – 549	304	Catalytic HAMAP MF_00184
Sites
	Metal binding	343	1	Zinc; catalytic By similarity
	Metal binding	394	1	Zinc; catalytic By similarity
	Metal binding	526	1	Zinc; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6FZZ7-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 5BC8837055C7045C	FASTA	658	75,704
	10 20 30 40 50 60 MSCSVSLSFP DGSKRDYPNE MTGLELAASI SKSLAKKAVA YSLNGITRDL SDPLGQSGQI 70 80 90 100 110 120 EIITREDPRA LELIRHDCAH VLAEAVQELF PETQVTIGPV IENGFYYDFA RQQPFTLNDL 130 140 150 160 170 180 TIIEKKMHEI IQRNKPFRKE IWSRKKAREI FSEKNELYKV ELIDSIPDNQ DLKIYYQGDW 190 200 210 220 230 240 FDLCRGPHMQ STGQIGNAFK LMKVAGAYWR GDAHNPMLTR IYGTAFANEN DLKAYLHMLE 250 260 270 280 290 300 EAEKRDHRRL GREMDLFHFQ EDGPGMIFWH QKGWKMFQNL ISYMRRRLDD HQYSEVNAPQ 310 320 330 340 350 360 VLDKSLWELS GHWGWYKENM FKAIPAIEDW DDKCIYALKP MNCPGHVQIF KHSLKSYRDL 370 380 390 400 410 420 PVRLAEFGVV HRYEPSGALH GLMRVRSFTQ DDAHIFCTDE QLADECLNIN DLILSTYADF 430 440 450 460 470 480 GFKEISLKLS TRPEKRVGSD SLWDHAENIM ESVLKTIETK FAGQIKTSIL PGEGAFYGPK 490 500 510 520 530 540 FEYTLKDAIG REWQCGTTQV DFNLPERFDA FYIDKDSEKR QPVMIHRAIF GSMERFLGIL 550 560 570 580 590 600 IENFAGHMPL WLAPEQVVVA AITSEANEYA KKITARLKAV GLSAKSDLRN EKINYKIREH 610 620 630 640 650 SLQKVPVILV CGKREAETNS VSMRRLGSTD QVFLSIEETI EQLKNEAMSP DLRRSING

References

[1]

"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae." Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E. Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed: 15210978] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Toulouse.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX897700 Genomic DNA. Translation: CAF26046.1.
RefSeq	YP_032213.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2866969.
GenomeReviews	Gene locus BQ05510 in contig BX897700_GR.
KEGG	bqu:BQ05510.
NMPDR	fig|283165.1.peg.483.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q6FZZ7.
OMA	ELELFMF.
Enzyme and pathway databases
BioCyc	BQUI283165:BQ05510-MON.
BRENDA	6.1.1.3. 292235.
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_BARQU

Accession

Primary (citable) accession number: Q6FZZ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	July 19, 2004
Last modified:	November 3, 2009
This is version 35 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)