Threonine--tRNA ligase - Escherichia coli (strain K12)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Threonine--tRNA ligase
EC=6.1.1.3

Alternative name(s):
Threonyl-tRNA synthetase
Short name=ThrRS

Gene names

Name:	thrS
Ordered Locus Names:	b1719, JW1709

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	642 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	ThrS is also a translational repressor protein, it controls the translation of its own gene by binding to its mRNA. HAMAP MF_00184
Catalytic activity	ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr). HAMAP MF_00184
Cofactor	Binds 1 zinc ion per subunit.
Subunit structure	Homodimer.
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. HAMAP MF_00184
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	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	negative regulation of translational initiation Inferred from mutant phenotype. Source: EcoCyc threonyl-tRNA aminoacylation Inferred from direct assay. Source: EcoCyc
Cellular component	cytoplasm Inferred from direct assay. Source: EcoliWiki
Molecular function	ATP binding Inferred from direct assay Ref.7. Source: EcoliWiki RNA binding Inferred from direct assay Ref.7. Source: EcoliWiki drug binding Inferred from direct assay. Source: EcoliWiki protein binding Inferred from physical interaction. Source: IntAct threonine-tRNA ligase activity Inferred from direct assay. Source: EcoCyc translation repressor activity, nucleic acid binding Inferred from direct assay. Source: EcoCyc zinc ion binding Inferred from mutant phenotype Ref.7. Source: EcoliWiki
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
rplA	P0A7L0	2	EBI-551254,EBI-543771

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 642

642

Threonine--tRNA ligase HAMAP MF_00184

PRO_0000100973

Regions

Region

243 – 534

292

Catalytic HAMAP MF_00184

Sites

Metal binding

334

1

Zinc; catalytic

Metal binding

385

1

Zinc; catalytic

Metal binding

511

1

Zinc; catalytic

Amino acid modifications

Modified residue

286

1

N6-acetyllysine Ref.6

Experimental info

Mutagenesis

334

1

C → S: Activity very strongly affected.

Mutagenesis

385

1

H → A or N: Activity very strongly affected.

Mutagenesis

511

1

H → A or N: Activity very strongly affected.

Sequence conflict

195

1

H → R in CAA23560. Ref.1

Secondary structure

1

.

642

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A8M3 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: 38D8913B19CDAB7B
Show »

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

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural and transcriptional evidence for related thrS and infC expression." Mayaux J.-F., Fayat G., Fromant M., Springer M., Grunberg-Manago M., Blanquet S. Proc. Natl. Acad. Sci. U.S.A. 80:6152-6156(1983) [PubMed: 6353409] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. Horiuchi T. DNA Res. 3:363-377(1996) [PubMed: 9097039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Genetic definition of the translational operator of the threonine-tRNA ligase gene in Escherichia coli." Springer M., Graffe M., Butler J.S., Grunberg-Manago M. Proc. Natl. Acad. Sci. U.S.A. 83:4384-4388(1986) [PubMed: 3086882] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-47, MECHANISM OF TRANSLATION REGULATION.
[6]	"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y. Mol. Cell. Proteomics 8:215-225(2009) [PubMed: 18723842] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-286, MASS SPECTROMETRY. Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[7]	"The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site." Sankaranarayanan R., Dock-Bregeon A.-C., Romby P., Caillet J., Springer M., Rees B., Ehresmann C., Ehresmann B., Moras D. Cell 97:371-381(1999) [PubMed: 10319817] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
[8]	"Zinc ion mediated amino acid discrimination by threonyl-tRNA synthetase." Sankaranarayanan R., Dock-Bregeon A.-C., Rees B., Bovee M., Caillet J., Romby P., Francklyn C.S., Moras D. Nat. Struct. Biol. 7:461-465(2000) [PubMed: 10881191] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 242-642.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

V00291 Genomic DNA. Translation: CAA23560.1.
U00096 Genomic DNA. Translation: AAC74789.1.
AP009048 Genomic DNA. Translation: BAA15498.1.
M13549 Genomic DNA. Translation: AAA24674.1.

PIR

SYECTT. G64930.

RefSeq

NP_416234.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EVK	X-ray	2.00	A/B	242-642	[»]
1EVL	X-ray	1.55	A/B/C/D	242-642	[»]
1FYF	X-ray	1.65	A/B	242-642	[»]
1KOG	X-ray	3.50	A/B/C/D/E/F/G/H	242-642	[»]
1QF6	X-ray	2.90	A	1-642	[»]
1TJE	X-ray	1.50	A	1-224	[»]
1TKE	X-ray	1.46	A	1-224	[»]
1TKG	X-ray	1.50	A	1-224	[»]
1TKY	X-ray	1.48	A	1-224	[»]

ProteinModelPortal

P0A8M3.

SMR

P0A8M3. Positions 2-642.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35823N.

IntAct

P0A8M3. 48 interactions.

MINT

MINT-1229097.

2D gel databases

ECO2DBASE

G065.0. 6TH EDITION.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000003656; EBESCP00000003656; EBESCG00000002989.
EBESCT00000003657; EBESCP00000003657; EBESCG00000002989.
EBESCT00000017300; EBESCP00000016591; EBESCG00000016357.

GeneID

946222.

GenomeReviews

Gene locus JW1709 in contig AP009048_GR.
Gene locus b1719 in contig U00096_GR.

KEGG

ecj:JW1709.
eco:b1719.

PATRIC

32118742. VBIEscCol129921_1789.

Organism-specific databases

EchoBASE

EB0994.

EcoGene

EG11001. thrS.

Phylogenomic databases

eggNOG

COG0441.

GeneTree

EBGT00050000008980.

HOGENOM

HBG352811.

OMA

MIIRNIL.

PhylomeDB

P0A8M3.

ProtClustDB

PRK00413.

Enzyme and pathway databases

BioCyc

EcoCyc:THRS-MONOMER.
MetaCyc:THRS-MONOMER.

Gene expression databases

Genevestigator

P0A8M3.

Family and domain databases

HAMAP

MF_00184. Thr_tRNA_synth.
[Tree]

InterPro

IPR002314. 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]

Gene3D

G3DSA:3.40.50.800. Anticodon_bd. 1 hit.
G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.

KO

K01868.

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.

SMART

SM00863. tRNA_SAD. 1 hit.
[Graphical view]

SUPFAM

SSF52954. Anticodon_bd. 1 hit.
SSF81271. TGS-like. 1 hit.
SSF55186. Thr/Ala-tRNA-synth_IIc_edit. 1 hit.

TIGRFAMs

TIGR00418. ThrS. 1 hit.

PROSITE

PS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

SYT_ECOLI

Accession

Primary (citable) accession number: P0A8M3
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:	January 25, 2012
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents