SYL_BORPE
ID SYL_BORPE Reviewed; 885 AA.
AC Q7VWY7;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=BP2044;
OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257313;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
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; BX640417; CAE42323.1; -; Genomic_DNA.
DR RefSeq; NP_880711.1; NC_002929.2.
DR RefSeq; WP_003818515.1; NZ_CP039022.1.
DR AlphaFoldDB; Q7VWY7; -.
DR SMR; Q7VWY7; -.
DR STRING; 257313.BP2044; -.
DR KEGG; bpe:BP2044; -.
DR PATRIC; fig|257313.5.peg.2196; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_4; -.
DR OMA; TFMVLAP; -.
DR Proteomes; UP000002676; 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 Gene3D; 3.90.740.10; -; 1.
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; Reference proteome.
FT CHAIN 1..885
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000151982"
FT MOTIF 48..58
FT /note="'HIGH' region"
FT MOTIF 639..643
FT /note="'KMSKS' region"
FT BINDING 642
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 885 AA; 98964 MW; D160F6425F433A1C CRC64;
MQERYQPNSV EAAAQQTWQA RDAYLVHEHA KNPDGSEKPK FYACSMLPYP SGKLHMGHVR
NYTINDMMAR QLRMRGYNVL MPMGWDAFGM PAENAAIKSK VPPAKWTYDN IAYMKKQMKA
MGLAIDWSRE MCACDPKYYK WNQWLFLKML EKGIAYRKTQ VVNWDPVDQT VLANEQVIDG
RGWRSGAPVE KREIPGYYLR ITDYAEELLD QVSTNLPGWP ERVRLMQENW IGKSEGLRFA
FPHRIAGADG KLIQDGKLYV FTTRADTIMG VTFCAVAPEH PLATHAAQSN PALAAFVEQC
KLGGTTEAEM ATREKEGMPT GLTVTHPLTG AEIDVWVGNY VLMTYGDGAV MGVPAHDERD
FAFARKYGLP IRQVVALEGK TYSTDAWQEW YGDKQAGRTV NSGKYDGLAY QAAVDAIAAD
LAAQGVGEKQ TTWRLRDWGI SRQRYWGTPI PIIHCADCGP VPVPEQDLPV VLPDDLIPDG
SGNPLAKNEA FLSCSCPRCG KPARRETDTM DTFVDSSWYF MRYTSPDNDQ AMVDARNDYW
MPMDQYIGGI EHAVLHLLYA RFWTKVMRDL GLLNFDEPFT KLLCQGMVLN HIYSRKTPQG
GIEYFWPEEV DNVYDAKGAI VGAKLQRDGS EVNYGGVGTM SKSKNNGVDP QSLIDTLGAD
TARLFVMFAS PPEQTLEWSD SGVEGANRFL RRLWALGYAQ REAVGRGLAT GADWAQAPAP
VKELRREVYG LLKQADYDYQ RIQYNTVVSA CMKMLNAIDD APLPEGPAAD AARAETLGLL
LRVLYPVVPH ITWHLWQDLG YAEHLGDLLD APWPHVDEAA LVADEIELML QVNGKLRGSI
RVAAKAPKED IERIAAAQEE VARFLEGRPP KRVIVVPGKL VNVVG
