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P36430 (SYL_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Leucine--tRNA ligase

EC=6.1.1.4
Alternative name(s):
Leucyl-tRNA synthetase
Short name=LeuRS
Gene names
Name:leuS
Ordered Locus Names:BSU30320
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length804 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu). HAMAP-Rule MF_00049

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00049.

Sequence similarities

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

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processleucyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

aminoacyl-tRNA editing activity

Inferred from electronic annotation. Source: InterPro

leucine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 804804Leucine--tRNA ligase HAMAP-Rule MF_00049
PRO_0000151973

Regions

Motif40 – 5112"HIGH" region HAMAP-Rule MF_00049
Motif576 – 5805"KMSKS" region HAMAP-Rule MF_00049

Sites

Binding site5791ATP By similarity

Experimental info

Sequence conflict1861P → L in AAA22571. Ref.1
Sequence conflict1951T → N in AAA22571. Ref.1
Sequence conflict247 – 28135RPDTL…AVEAY → DQIRCLALHTLSLPRNTHWW KTSQRQSKKKLLKLI Ref.1

Sequences

Sequence LengthMass (Da)Tools
P36430 [UniParc].

Last modified July 15, 1998. Version 3.
Checksum: 306FD5A98FE5C47E

FASTA80491,543
        10         20         30         40         50         60 
MSFQHKEIEK KWQTYWLENK TFATLDNNEK QKFYALDMFP YPSGAGLHVG HPEGYTATDI 

        70         80         90        100        110        120 
LSRMKRMQGY DVLHPMGWDA FGLPAEQYAL DTGNDPAVFT KQNIDNFRRQ IQALGFSYDW 

       130        140        150        160        170        180 
DREINTTDPE YYKWTQWIFL KLYEKGLAYV DEVPVNWCPA LGTVLANEEV IDGKSERGGH 

       190        200        210        220        230        240 
PVERRPMKQW MLKITAYADR LLEDLEELDW PESIKDMQRN WIGRSEGAHV HFAIDGHDDS 

       250        260        270        280        290        300 
FTVFTTRPDT LFGATYTVLA PEHALVENIT TAEQKEAVEA YIKEIQSKSD LERTDLAKTK 

       310        320        330        340        350        360 
TGVFTGAYAI NPVNGEKLPI WIADYVLASY GTGAVMAVPG HDERDFEFAK TFGLPVKEVV 

       370        380        390        400        410        420 
KGGNVEEAAY TGDGEHVNSD FLNGLHKQEA IEKVIAWLEE TKNGEKKVTY RLRDWLFSRQ 

       430        440        450        460        470        480 
RYWGEPIPVI HWEDGTSTAV PEEELPLILP KTDEIKPSGT GESPLANIKE WVEVTDPETG 

       490        500        510        520        530        540 
KKGRRETNTM PQWAGSCWYF LRYIDPHNPD QLASPEKLEK WLPVDMYIGG AEHAVLHLLY 

       550        560        570        580        590        600 
ARFWHKFLYD IGVVPTKEPF QKLYNQGMIL GENNEKMSKS KGNVVNPDEI VASHGADTLR 

       610        620        630        640        650        660 
LYEMFMGPLD ASIAWSESGL DGARRFLDRV WRLFIEDSGE LNGKIVEGAG ETLERVYHET 

       670        680        690        700        710        720 
VMKVTDHYEG LRFNTGISQL MVFINEAYKA TELPKEYMEG FVKLLSPVAP HLAEELWEKL 

       730        740        750        760        770        780 
GHSGTIAYEA WPVYDETKLV DDEVEIVVQL NGKVKAKLQV PADATKEQLE QLAQADEKVK 

       790        800 
EQLEGKTIRK IIAVPGKLVN IVAN 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and nucleotide sequence of the leucyl-tRNA synthetase gene of Bacillus subtilis."
Vander Horn P.B., Zahler S.A.
J. Bacteriol. 174:3928-3935(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region."
Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.
Microbiology 143:3431-3441(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[3]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M88581 Genomic DNA. Translation: AAA22571.1.
AF008220 Genomic DNA. Translation: AAC00259.1.
AL009126 Genomic DNA. Translation: CAB15010.1.
PIRD69650.
RefSeqNP_390910.1. NC_000964.3.

3D structure databases

ProteinModelPortalP36430.
SMRP36430. Positions 2-803.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP36430. 1 interaction.
MINTMINT-8365963.
STRING224308.BSU30320.

Proteomic databases

PaxDbP36430.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB15010; CAB15010; BSU30320.
GeneID938102.
KEGGbsu:BSU30320.
PATRIC18977966. VBIBacSub10457_3171.

Organism-specific databases

GenoListBSU30320. [Micado]

Phylogenomic databases

eggNOGCOG0495.
HOGENOMHOG000200748.
KOK01869.
OMAGIEHACM.
OrthoDBEOG63Z74X.
ProtClustDBPRK00390.

Enzyme and pathway databases

BioCycBSUB:BSU30320-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPMF_00049_B. Leu_tRNA_synth_B.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002302. Leu-tRNA-ligase_bac/mito.
IPR025709. Leu_tRNA-synth_edit.
IPR015413. Methionyl/Leucyl_tRNA_Synth.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
IPR013155. V/L/I-tRNA-synth_anticodon-bd.
IPR009008. Val/Leu/Ile-tRNA-synth_edit.
[Graphical view]
PANTHERPTHR11946:SF7. PTHR11946:SF7. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
PF13603. tRNA-synt_1_2. 1 hit.
PF09334. tRNA-synt_1g. 1 hit.
[Graphical view]
PRINTSPR00985. TRNASYNTHLEU.
SUPFAMSSF47323. SSF47323. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00396. leuS_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYL_BACSU
AccessionPrimary (citable) accession number: P36430
Secondary accession number(s): O34465
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: July 15, 1998
Last modified: April 16, 2014
This is version 112 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries