P0A8M3 (SYT_ECOLI) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

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-Rule MF_00184
Catalytic activity	ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr). HAMAP-Rule MF_00184
Cofactor	Binds 1 zinc ion per subunit.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm HAMAP-Rule 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-Rule 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 PubMed 3930755. Source: EcoCyc threonyl-tRNA aminoacylation Inferred from direct assay PubMed 2676521. Source: EcoCyc
Cellular_component	cytoplasm Inferred from direct assay PubMed 330505. Source: EcoliWiki
Molecular_function	ATP binding Inferred from direct assay Ref.8. Source: EcoliWiki RNA binding Inferred from direct assay Ref.8. Source: EcoliWiki drug binding Inferred from direct assay PubMed 330505. Source: EcoliWiki threonine-tRNA ligase activity Inferred from direct assay PubMed 2676521. Source: EcoCyc translation repressor activity, nucleic acid binding Inferred from direct assay PubMed 2207165. Source: EcoCyc zinc ion binding Inferred from mutant phenotype Ref.8. 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-Rule MF_00184

PRO_0000100973

Regions

Region

243 – 534

292

Catalytic HAMAP-Rule 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.7

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

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642

Helix Strand Turn

Details...

Beta strand

3 – 5

3

Beta strand

11 – 13

3

Helix

20 – 27

8

Helix

29 – 34

6

Beta strand

37 – 40

4

Beta strand

43 – 46

4

Beta strand

55 – 60

6

Helix

65 – 86

22

Beta strand

101 – 107

7

Helix

114 – 128

15

Beta strand

135 – 138

4

Helix

141 – 150

10

Helix

154 – 163

10

Beta strand

171 – 175

5

Beta strand

178 – 183

6

Helix

190 – 192

3

Beta strand

196 – 205

10

Helix

206 – 208

3

Beta strand

214 – 222

9

Helix

226 – 240

15

Helix

244 – 250

7

Helix

268 – 287

20

Beta strand

297 – 300

4

Helix

301 – 306

6

Helix

309 – 312

4

Helix

314 – 316

3

Beta strand

319 – 322

4

Beta strand

325 – 329

5

Beta strand

331 – 333

3

Helix

334 – 341

8

Helix

348 – 350

3

Beta strand

352 – 362

11

Helix

367 – 369

3

Turn

372 – 374

3

Beta strand

377 – 388

12

Helix

390 – 392

3

Helix

393 – 409

17

Turn

410 – 412

3

Beta strand

417 – 421

5

Helix

431 – 447

17

Beta strand

453 – 455

3

Beta strand

465 – 471

7

Beta strand

477 – 488

12

Helix

489 – 492

4

Beta strand

502 – 505

4

Beta strand

508 – 517

10

Helix

518 – 529

12

Turn

535 – 537

3

Beta strand

542 – 548

7

Helix

549 – 551

3

Helix

552 – 564

13

Beta strand

569 – 572

4

Helix

578 – 587

10

Beta strand

591 – 596

6

Helix

598 – 603

6

Beta strand

605 – 610

6

Beta strand

615 – 620

6

Helix

621 – 633

13

Sequences

	Sequence		Length	Mass (Da)
	P0A8M3 [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

	« 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] [Europe PMC] [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. , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-47, MECHANISM OF TRANSLATION REGULATION.
[6]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[7]	"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] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-286, MASS SPECTROMETRY. Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[8]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
[9]	"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] [Europe PMC] [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.
YP_489981.1. NC_007779.1.

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.

STRING

511145.b1719.

Proteomic databases

PaxDb

P0A8M3.

PRIDE

P0A8M3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74789; AAC74789; b1719.
BAA15498; BAA15498; BAA15498.

GeneID

12933199.
946222.

KEGG

ecj:Y75_p1694.
eco:b1719.

PATRIC

32118742. VBIEscCol129921_1789.

Organism-specific databases

EchoBASE

EB0994.

EcoGene

EG11001. thrS.

Phylogenomic databases

eggNOG

COG0441.

HOGENOM

HOG000003880.

KO

K01868.

OMA

KITYKIR.

ProtClustDB

PRK00413.

Enzyme and pathway databases

BioCyc

EcoCyc:THRS-MONOMER.
ECOL316407:JW1709-MONOMER.
MetaCyc:THRS-MONOMER.

SABIO-RK

P0A8M3.

Gene expression databases

Genevestigator

P0A8M3.

Family and domain databases

Gene3D

3.10.20.30. 1 hit.
3.40.50.800. 1 hit.

HAMAP

MF_00184. Thr_tRNA_synth.

InterPro

IPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR012675. Beta-grasp_dom.
IPR004095. TGS.
IPR012676. TGS-like.
IPR002320. Thr-tRNA-ligase_IIa.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view]

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...

Other

EvolutionaryTrace

P0A8M3.

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:	May 1, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program