SYL_BORAP
ID SYL_BORAP Reviewed; 840 AA.
AC Q0SNR0; G0IR93;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
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};
GN OrderedLocusNames=BAPKO_0261, BafPKo_0253;
OS Borreliella afzelii (strain PKo) (Borrelia afzelii).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=390236;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PKo;
RX PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J.,
RA Wilske B., Platzer M.;
RT "Comparative genome analysis: selection pressure on the Borrelia vls
RT cassettes is essential for infectivity.";
RL BMC Genomics 7:211-211(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PKo;
RX PubMed=22123755; DOI=10.1128/jb.05951-11;
RA Casjens S.R., Mongodin E.F., Qiu W.G., Dunn J.J., Luft B.J.,
RA Fraser-Liggett C.M., Schutzer S.E.;
RT "Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii
RT Lyme disease agent isolates.";
RL J. Bacteriol. 193:6995-6996(2011).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000395; ABH01518.1; -; Genomic_DNA.
DR EMBL; CP002933; AEL69479.1; -; Genomic_DNA.
DR RefSeq; WP_011600919.1; NC_017238.1.
DR AlphaFoldDB; Q0SNR0; -.
DR SMR; Q0SNR0; -.
DR STRING; 390236.BafPKo_0253; -.
DR EnsemblBacteria; AEL69479; AEL69479; BafPKo_0253.
DR KEGG; baf:BAPKO_0261; -.
DR KEGG; bafz:BafPKo_0253; -.
DR PATRIC; fig|390236.22.peg.247; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_12; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000005216; 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; 1.
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.
FT CHAIN 1..840
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000009299"
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; 98167 MW; B488A7FF899B0BB3 CRC64;
MSKYEFIKIE KKWQEFWDNN KTYKVIEDPN IPKEKRLYIL DMFPYPSANG LHVGHPEGYT
ATDIFARYKI LNGFHVLHPI GFDSFGLPAE NYAIQTGTHP KKSTEENINK FKKQIKALGF
AYDWDREIRT HDENYYKWTQ WIFLQLYKKG LAYAKEMPVW YCPELGTVLA NEEIIQTPNG
PKSERGFHNV EKKYLRQWVL KITKYAERLL NDLEELEWPE SVKEMQRNWI GKSTGVEIDF
EIEGYNDKIK VFTTRPDTIF GITYLVIAPE NKLVEKITKD NFKSNVLKYI KQEELKSDLK
RTSLEKDKSG VFTGSYAFHP ITNVKIPIWV GSYVLGTYGS GAVMGVPAHD ERDFQFAKKY
KLKILPVISK SGKNEILEKA FINDGISINS PDEFNNLKNS EVKDKVIKWL TKNKKGKETV
TYKLRDWVFS RQRYWGEPIP ILFDKLGNAI PLEKNDLPLK LPETANYKPS GTGESPLSRI
KNWVNVKDTD FTRETNTMPQ WAGSCWYYLR YLDPKNSKEF ANHKKIEYWM PVDLYIGGAE
HTVLHLLYSR FWHKVLYDLG HVNTKEPFKK LINQGIITAF SYQKENGVLI PNDQVIEKDN
KFFDKKDNKE VTQVIAKMSK SLKNVINPDG IIKEFGADSI RIYEMFMGPL TDSKPWNTKG
IIGVFRFLNK IWNLREKELS KDNPPKEIMS QLHKVIKKVT EDTEKLNFNT AISAMMIFIN
ELSKYEKNYL NIFKPFIIIL SPYAPHLAEE LWEYIGETPS LFKNSKWPKF DETLIIKETK
EIVLQINGKI KDKILLNKET DEEELKEIAM ENSKIKSNLF NKKIVKIIVI KNKLVNIVIK