SYL_BORBU
ID SYL_BORBU Reviewed; 840 AA.
AC O51267;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Leucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00049};
DE EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00049};
DE Short=LeuRS {ECO:0000255|HAMAP-Rule:MF_00049};
GN Name=leuS {ECO:0000255|HAMAP-Rule:MF_00049}; OrderedLocusNames=BB_0251;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-
CC tRNA(Leu); Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613, Rhea:RHEA-
CC COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:456215; EC=6.1.1.4;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00049};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00049}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00049}.
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DR EMBL; AE000783; AAB91495.1; -; Genomic_DNA.
DR PIR; C70131; C70131.
DR RefSeq; NP_212385.1; NC_001318.1.
DR RefSeq; WP_010889717.1; NC_001318.1.
DR AlphaFoldDB; O51267; -.
DR SMR; O51267; -.
DR STRING; 224326.BB_0251; -.
DR PRIDE; O51267; -.
DR EnsemblBacteria; AAB91495; AAB91495; BB_0251.
DR KEGG; bbu:BB_0251; -.
DR PATRIC; fig|224326.49.peg.650; -.
DR HOGENOM; CLU_004427_0_0_12; -.
DR OMA; TFMVLAP; -.
DR Proteomes; UP000001807; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.620; -; 2.
DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR002302; Leu-tRNA-ligase.
DR InterPro; IPR025709; Leu_tRNA-synth_edit.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR PANTHER; PTHR43740; PTHR43740; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR PRINTS; PR00985; TRNASYNTHLEU.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00396; leuS_bact; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..840
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000151983"
FT MOTIF 44..55
FT /note="'HIGH' region"
FT MOTIF 617..621
FT /note="'KMSKS' region"
FT BINDING 620
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 840 AA; 98158 MW; 521C76BAF009593E CRC64;
MSKYEFIKIE KKWQEFWDNN KTYKVEEDPS IPKEKRLYIL DMFPYPSANG LHVGHPEGYT
ATDIFGRYKL LNGFHVLHPI GFDSFGLPAE NYAIQTGTHP QKSTEENINK FKKQIKALGF
AYDWDREIRT HEENYYKWTQ WIFLQLYKKG LAYVKEMPVW YCPELGTVLA NEEIIQTSDG
PKSERGSYSV EKKYLRQWVL KITKYAERLL DDLEELEWPE SVKEMQRNWI GKSTGVEIEF
EIEGHSDKIK VFTTRPDTIF GITYLVIAPE NKLIEKITKN NFKQNVLKYV KHEELKSDLN
RTSLEKDKSG VFTGSYAFHP ITNEKIPIWV GSYVLGTYGT GAVMGVPAHD ERDFQFAKKY
QLKILPVISK SGKNEILEKA FVDDGISINS PNEFNNLKNS EVKDKVIKWL TKNKKGKEKV
AYKLRDWIFS RQRYWGEPIP ILFDKLGNAI PLEENDLPLK LPEIANYKPS GTGESPLSRI
KDWVNVKDMG FTRETNTMPQ WAGSCWYYLR YLDPKNSKEF ANKKKIEYWM PVDLYIGGAE
HTVLHLLYSR FWHKVLYDLG YVNTKEPFKK LINQGIITSF SYQKENGVLI PNDQVIEKDN
KFFDKKDNKE VTQVIAKMSK SLKNVINPDD IIKEFGADSM RIYEMFMGPL TDSKPWNTKG
IIGVFRFLNK IWNLREKELS KENPPREIIS ELHKVIKKVT EDTEKLNFNT AISAMMIFIN
ELLKYEKNYL NIFKPFIIIL SPYAPHLAEE LWEYIGELPS LFKNSKWPKF DESLIIKGKK
EIVLQINGKI KDKILLNKET GEKELKEIAM ENSKIKSNLL NKKIVKIIVI KNKLVNIVIK
