Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Leucine--tRNA ligase

Gene

leuS

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu).UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei622 – 6221ATPUniRule annotation

GO - Molecular functioni

  • aminoacyl-tRNA editing activity Source: InterPro
  • ATP binding Source: UniProtKB-HAMAP
  • leucine-tRNA ligase activity Source: EcoCyc

GO - Biological processi

  • leucyl-tRNA aminoacylation Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:LEUS-MONOMER.
ECOL316407:JW0637-MONOMER.
MetaCyc:LEUS-MONOMER.
BRENDAi6.1.1.4. 2026.
SABIO-RKP07813.

Names & Taxonomyi

Protein namesi
Recommended name:
Leucine--tRNA ligaseUniRule annotation (EC:6.1.1.4UniRule annotation)
Alternative name(s):
Leucyl-tRNA synthetaseUniRule annotation
Short name:
LeuRSUniRule annotation
Gene namesi
Name:leuSUniRule annotation
Ordered Locus Names:b0642, JW0637
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10532. leuS.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 860860Leucine--tRNA ligasePRO_0000152012Add
BLAST

Proteomic databases

PaxDbiP07813.
PRIDEiP07813.

2D gel databases

SWISS-2DPAGEP07813.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi851814. 1 interaction.
DIPiDIP-10095N.
IntActiP07813. 21 interactions.
MINTiMINT-1226410.
STRINGi511145.b0642.

Structurei

Secondary structure

1
860
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 2014Combined sources
Turni21 – 244Combined sources
Beta strandi30 – 323Combined sources
Beta strandi34 – 396Combined sources
Beta strandi45 – 473Combined sources
Helixi50 – 6819Combined sources
Beta strandi72 – 743Combined sources
Beta strandi76 – 794Combined sources
Helixi85 – 928Combined sources
Beta strandi93 – 953Combined sources
Helixi97 – 11418Combined sources
Helixi121 – 1233Combined sources
Helixi130 – 14516Combined sources
Beta strandi149 – 1546Combined sources
Turni160 – 1634Combined sources
Beta strandi164 – 1663Combined sources
Helixi168 – 1703Combined sources
Beta strandi177 – 1793Combined sources
Beta strandi188 – 1936Combined sources
Helixi195 – 1984Combined sources
Helixi199 – 2057Combined sources
Helixi206 – 2083Combined sources
Helixi214 – 22411Combined sources
Beta strandi229 – 2368Combined sources
Beta strandi240 – 2489Combined sources
Helixi250 – 2556Combined sources
Beta strandi258 – 2614Combined sources
Helixi266 – 2727Combined sources
Helixi276 – 28712Combined sources
Helixi292 – 2976Combined sources
Beta strandi302 – 3109Combined sources
Turni312 – 3143Combined sources
Beta strandi317 – 3237Combined sources
Beta strandi328 – 3314Combined sources
Beta strandi333 – 3375Combined sources
Turni339 – 3413Combined sources
Helixi343 – 35210Combined sources
Beta strandi371 – 3733Combined sources
Helixi385 – 3873Combined sources
Helixi392 – 40514Combined sources
Beta strandi408 – 4125Combined sources
Beta strandi423 – 4253Combined sources
Beta strandi427 – 4293Combined sources
Beta strandi434 – 4374Combined sources
Beta strandi442 – 4443Combined sources
Helixi447 – 4493Combined sources
Beta strandi462 – 4643Combined sources
Helixi466 – 4694Combined sources
Turni471 – 4744Combined sources
Beta strandi475 – 48511Combined sources
Turni492 – 4943Combined sources
Helixi495 – 4973Combined sources
Helixi499 – 5024Combined sources
Beta strandi510 – 5123Combined sources
Helixi515 – 5217Combined sources
Beta strandi523 – 5286Combined sources
Helixi531 – 5333Combined sources
Turni534 – 5363Combined sources
Helixi537 – 55014Combined sources
Beta strandi559 – 5646Combined sources
Beta strandi569 – 5779Combined sources
Beta strandi579 – 5813Combined sources
Beta strandi583 – 5864Combined sources
Helixi588 – 5903Combined sources
Beta strandi592 – 5954Combined sources
Beta strandi597 – 5993Combined sources
Beta strandi601 – 6055Combined sources
Beta strandi613 – 6197Combined sources
Turni622 – 6254Combined sources
Helixi630 – 6378Combined sources
Helixi639 – 64810Combined sources
Helixi660 – 68223Combined sources
Helixi691 – 6933Combined sources
Helixi696 – 71722Combined sources
Helixi722 – 73716Combined sources
Helixi744 – 76118Combined sources
Turni762 – 7643Combined sources
Helixi766 – 77510Combined sources
Helixi782 – 7843Combined sources
Helixi792 – 7954Combined sources
Beta strandi798 – 8069Combined sources
Beta strandi809 – 8179Combined sources
Helixi822 – 83110Combined sources
Helixi833 – 8364Combined sources
Turni837 – 8415Combined sources
Beta strandi846 – 8505Combined sources
Turni851 – 8533Combined sources
Beta strandi854 – 8585Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AJGX-ray2.00A/B228-413[»]
2AJHX-ray2.40A/B228-413[»]
2AJIX-ray3.20A/B228-413[»]
3ZGZX-ray2.40A/D1-860[»]
3ZJTX-ray2.20A1-860[»]
3ZJUX-ray2.40A1-860[»]
3ZJVX-ray2.31A1-860[»]
4AQ7X-ray2.50A/D1-860[»]
4ARCX-ray2.00A1-860[»]
4ARIX-ray2.08A1-860[»]
4AS1X-ray2.02A1-860[»]
4CQNX-ray2.50A/D1-860[»]
ProteinModelPortaliP07813.
SMRiP07813. Positions 1-860.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07813.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi42 – 5211"HIGH" regionAdd
BLAST
Motifi619 – 6235"KMSKS" region

Sequence similaritiesi

Belongs to the class-I aminoacyl-tRNA synthetase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0495.
HOGENOMiHOG000200747.
InParanoidiP07813.
KOiK01869.
OMAiEGAHRFI.
OrthoDBiEOG63Z74X.
PhylomeDBiP07813.

Family and domain databases

Gene3Di1.10.730.10. 1 hit.
3.40.50.620. 3 hits.
3.90.740.10. 1 hit.
HAMAPiMF_00049_B. Leu_tRNA_synth_B.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002302. Leu-tRNA-ligase.
IPR025709. Leu_tRNA-synth_edit.
IPR013155. M/V/L/I-tRNA-synth_anticd-bd.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
IPR009008. Val/Leu/Ile-tRNA-synth_edit.
[Graphical view]
PANTHERiPTHR11946:SF7. PTHR11946:SF7. 1 hit.
PfamiPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 3 hits.
PF13603. tRNA-synt_1_2. 1 hit.
[Graphical view]
PRINTSiPR00985. TRNASYNTHLEU.
SUPFAMiSSF47323. SSF47323. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsiTIGR00396. leuS_bact. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P07813-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQEQYRPEEI ESKVQLHWDE KRTFEVTEDE SKEKYYCLSM LPYPSGRLHM
60 70 80 90 100
GHVRNYTIGD VIARYQRMLG KNVLQPIGWD AFGLPAEGAA VKNNTAPAPW
110 120 130 140 150
TYDNIAYMKN QLKMLGFGYD WSRELATCTP EYYRWEQKFF TELYKKGLVY
160 170 180 190 200
KKTSAVNWCP NDQTVLANEQ VIDGCCWRCD TKVERKEIPQ WFIKITAYAD
210 220 230 240 250
ELLNDLDKLD HWPDTVKTMQ RNWIGRSEGV EITFNVNDYD NTLTVYTTRP
260 270 280 290 300
DTFMGCTYLA VAAGHPLAQK AAENNPELAA FIDECRNTKV AEAEMATMEK
310 320 330 340 350
KGVDTGFKAV HPLTGEEIPV WAANFVLMEY GTGAVMAVPG HDQRDYEFAS
360 370 380 390 400
KYGLNIKPVI LAADGSEPDL SQQALTEKGV LFNSGEFNGL DHEAAFNAIA
410 420 430 440 450
DKLTAMGVGE RKVNYRLRDW GVSRQRYWGA PIPMVTLEDG TVMPTPDDQL
460 470 480 490 500
PVILPEDVVM DGITSPIKAD PEWAKTTVNG MPALRETDTF DTFMESSWYY
510 520 530 540 550
ARYTCPQYKE GMLDSEAANY WLPVDIYIGG IEHAIMHLLY FRFFHKLMRD
560 570 580 590 600
AGMVNSDEPA KQLLCQGMVL ADAFYYVGEN GERNWVSPVD AIVERDEKGR
610 620 630 640 650
IVKAKDAAGH ELVYTGMSKM SKSKNNGIDP QVMVERYGAD TVRLFMMFAS
660 670 680 690 700
PADMTLEWQE SGVEGANRFL KRVWKLVYEH TAKGDVAALN VDALTENQKA
710 720 730 740 750
LRRDVHKTIA KVTDDIGRRQ TFNTAIAAIM ELMNKLAKAP TDGEQDRALM
760 770 780 790 800
QEALLAVVRM LNPFTPHICF TLWQELKGEG DIDNAPWPVA DEKAMVEDST
810 820 830 840 850
LVVVQVNGKV RAKITVPVDA TEEQVRERAG QEHLVAKYLD GVTVRKVIYV
860
PGKLLNLVVG
Length:860
Mass (Da):97,234
Last modified:November 1, 1997 - v2
Checksum:i856BBEDECC03C83C
GO

Sequence cautioni

The sequence AAB40843.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti67 – 671R → H in CAA29642 (PubMed:3320963).Curated
Sequence conflicti196 – 1961T → N in CAA29642 (PubMed:3320963).Curated
Sequence conflicti262 – 2621A → R (PubMed:3320963).Curated
Sequence conflicti262 – 2621A → R (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06331 Genomic DNA. Translation: CAA29642.1.
U82598 Genomic DNA. Translation: AAB40843.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73743.1.
AP009048 Genomic DNA. Translation: BAA35289.1.
PIRiH64798. SYECL.
RefSeqiNP_415175.1. NC_000913.3.
WP_001340834.1. NZ_CP010445.1.

Genome annotation databases

EnsemblBacteriaiAAC73743; AAC73743; b0642.
BAA35289; BAA35289; BAA35289.
GeneIDi947497.
KEGGieco:b0642.
PATRICi32116467. VBIEscCol129921_0673.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06331 Genomic DNA. Translation: CAA29642.1.
U82598 Genomic DNA. Translation: AAB40843.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73743.1.
AP009048 Genomic DNA. Translation: BAA35289.1.
PIRiH64798. SYECL.
RefSeqiNP_415175.1. NC_000913.3.
WP_001340834.1. NZ_CP010445.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AJGX-ray2.00A/B228-413[»]
2AJHX-ray2.40A/B228-413[»]
2AJIX-ray3.20A/B228-413[»]
3ZGZX-ray2.40A/D1-860[»]
3ZJTX-ray2.20A1-860[»]
3ZJUX-ray2.40A1-860[»]
3ZJVX-ray2.31A1-860[»]
4AQ7X-ray2.50A/D1-860[»]
4ARCX-ray2.00A1-860[»]
4ARIX-ray2.08A1-860[»]
4AS1X-ray2.02A1-860[»]
4CQNX-ray2.50A/D1-860[»]
ProteinModelPortaliP07813.
SMRiP07813. Positions 1-860.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi851814. 1 interaction.
DIPiDIP-10095N.
IntActiP07813. 21 interactions.
MINTiMINT-1226410.
STRINGi511145.b0642.

2D gel databases

SWISS-2DPAGEP07813.

Proteomic databases

PaxDbiP07813.
PRIDEiP07813.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73743; AAC73743; b0642.
BAA35289; BAA35289; BAA35289.
GeneIDi947497.
KEGGieco:b0642.
PATRICi32116467. VBIEscCol129921_0673.

Organism-specific databases

EchoBASEiEB0527.
EcoGeneiEG10532. leuS.

Phylogenomic databases

eggNOGiCOG0495.
HOGENOMiHOG000200747.
InParanoidiP07813.
KOiK01869.
OMAiEGAHRFI.
OrthoDBiEOG63Z74X.
PhylomeDBiP07813.

Enzyme and pathway databases

BioCyciEcoCyc:LEUS-MONOMER.
ECOL316407:JW0637-MONOMER.
MetaCyc:LEUS-MONOMER.
BRENDAi6.1.1.4. 2026.
SABIO-RKP07813.

Miscellaneous databases

EvolutionaryTraceiP07813.
PROiP07813.

Family and domain databases

Gene3Di1.10.730.10. 1 hit.
3.40.50.620. 3 hits.
3.90.740.10. 1 hit.
HAMAPiMF_00049_B. Leu_tRNA_synth_B.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002302. Leu-tRNA-ligase.
IPR025709. Leu_tRNA-synth_edit.
IPR013155. M/V/L/I-tRNA-synth_anticd-bd.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
IPR009008. Val/Leu/Ile-tRNA-synth_edit.
[Graphical view]
PANTHERiPTHR11946:SF7. PTHR11946:SF7. 1 hit.
PfamiPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 3 hits.
PF13603. tRNA-synt_1_2. 1 hit.
[Graphical view]
PRINTSiPR00985. TRNASYNTHLEU.
SUPFAMiSSF47323. SSF47323. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsiTIGR00396. leuS_bact. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and nucleotide sequence of the gene for Escherichia coli leucyl-tRNA synthetase."
    Haertlein M., Madern D.
    Nucleic Acids Res. 15:10199-10210(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "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.
  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.

Entry informationi

Entry nameiSYL_ECOLI
AccessioniPrimary (citable) accession number: P07813
Secondary accession number(s): P77110, P78292
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: November 1, 1997
Last modified: July 22, 2015
This is version 150 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.