Reviewed, UniProtKB/Swiss-Prot P0A8M4 (SYT_ECOL6)

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:	c2116

Organism

Escherichia coli O6 [Complete proteome] [HAMAP]

Taxonomic identifier

217992 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	642 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	ThrS is also a translational repressor protein, it controls the translation of its own gene by binding to its mRNA By similarity.
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
Domain	The C-terminal domain recognizes the anticodon bases but the N-terminal contributes also to the precise recognition of tRNA(Thr) by ThrRS By similarity.
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis Translation regulation
Cellular component	Cytoplasm
Ligand	ATP-binding Metal-binding Nucleotide-binding RNA-binding Zinc
Molecular function	Aminoacyl-tRNA synthetase Ligase Repressor
PTM	Acetylation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	regulation of translation Inferred from electronic annotation. Source: UniProtKB-KW threonyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: HAMAP
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP RNA binding Inferred from electronic annotation. Source: UniProtKB-KW 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 – 642	642	Threonyl-tRNA synthetase HAMAP MF_00184		PRO_0000100974
Regions
	Region	243 – 534	292	Catalytic HAMAP MF_00184
Sites
	Metal binding	334	1	Zinc; catalytic By similarity
	Metal binding	385	1	Zinc; catalytic By similarity
	Metal binding	511	1	Zinc; catalytic By similarity
Amino acid modifications
	Modified residue	286	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0A8M4-1 [UniParc]. Last modified June 7, 2005. Version 1. Checksum: 38D8913B19CDAB7B	FASTA	642	74,014
	10 20 30 40 50 60 MPVITLPDGS QRHYDHAVSP MDVALDIGPG LAKACIAGRV NGELVDACDL IENDAQLSII 70 80 90 100 110 120 TAKDEEGLEI IRHSCAHLLG HAIKQLWPHT KMAIGPVIDN GFYYDVDLDR TLTQEDVEAL 130 140 150 160 170 180 EKRMHELAEK NYDVIKKKVS WHEARETFAN RGESYKVSIL DENIAHDDKP GLYFHEEYVD 190 200 210 220 230 240 MCRGPHVPNM RFCHHFKLMK TAGAYWRGDS NNKMLQRIYG TAWADKKALN AYLQRLEEAA 250 260 270 280 290 300 KRDHRKIGKQ LDLYHMQEEA PGMVFWHNDG WTIFRELEVF VRSKLKEYQY QEVKGPFMMD 310 320 330 340 350 360 RVLWEKTGHW DNYKDAMFTT SSENREYCIK PMNCPGHVQI FNQGLKSYRD LPLRMAEFGS 370 380 390 400 410 420 CHRNEPSGSL HGLMRVRGFT QDDAHIFCTE EQIRDEVNGC IRLVYDMYST FGFEKIVVKL 430 440 450 460 470 480 STRPEKRIGS DEMWDRAEAD LAVALEENNI PFEYQLGEGA FYGPKIEFTL YDCLDRAWQC 490 500 510 520 530 540 GTVQLDFSLP SRLSASYVGE DNERKVPVMI HRAILGSMER FIGILTEEFA GFFPTWLAPV 550 560 570 580 590 600 QVVIMNITDS QSEYVNELTQ KLSNAGIRVK ADLRNEKIGF KIREHTLRRV PYMLVCGDKE 610 620 630 640 VESGKVAVRT RRGKDLGSMD VNEVIEKLQQ EIRSRSLKQL EE

References

[1]

"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli." Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R. Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE014075 Genomic DNA. Translation: AAN80575.1.
RefSeq	NP_754010.1.
3D structure databases
SMR	P0A8M4. Positions 2-642.
ModBase	Search...
Genome annotation databases
GeneID	1036459.
GenomeReviews	Gene locus c2116 in contig AE014075_GR.
KEGG	ecc:c2116.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P0A8M4.
Family and domain databases
HAMAP	MF_00184. [Tree]
InterPro	IPR002314. aa-tRNA-synt_IIb. IPR006195. aa-tRNA-synth_II. IPR004154. Anticodon_bd. IPR012675. b-grasp_ferredoxin-like. IPR004095. TGS. IPR002320. Thr-tRNA-synth_IIa. 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_ECOL6

Accession

Primary (citable) accession number: P0A8M4
Secondary accession number(s): P00955, P78166, P78241

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	June 7, 2005
Last modified:	November 4, 2008
This is version 30 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)