SYL_BRUA1
ID SYL_BRUA1 Reviewed; 877 AA.
AC B2S7N1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=BAbS19_I16960;
OS Brucella abortus (strain S19).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=430066;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S19;
RX PubMed=18478107; DOI=10.1371/journal.pone.0002193;
RA Crasta O.R., Folkerts O., Fei Z., Mane S.P., Evans C., Martino-Catt S.,
RA Bricker B., Yu G., Du L., Sobral B.W.;
RT "Genome sequence of Brucella abortus vaccine strain S19 compared to
RT virulent strains yields candidate virulence genes.";
RL PLoS ONE 3:E2193-E2193(2008).
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; CP000887; ACD73178.1; -; Genomic_DNA.
DR RefSeq; WP_002969611.1; NC_010742.1.
DR AlphaFoldDB; B2S7N1; -.
DR SMR; B2S7N1; -.
DR EnsemblBacteria; ACD73178; ACD73178; BAbS19_I16960.
DR GeneID; 3788315; -.
DR KEGG; bmc:BAbS19_I16960; -.
DR HOGENOM; CLU_004427_0_0_5; -.
DR OMA; TFMVLAP; -.
DR Proteomes; UP000002565; Chromosome 1.
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; 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.
FT CHAIN 1..877
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000091295"
FT MOTIF 43..53
FT /note="'HIGH' region"
FT MOTIF 628..632
FT /note="'KMSKS' region"
FT BINDING 631
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 877 AA; 97890 MW; D7910B19450827B4 CRC64;
MAAERYNPRV AEAHWQKVWE ENRTFETDNS DSREKYYVLE MFPYPSGRIH MGHVRNYAMG
DVVARYKRAK GFNVLHPMGW DAFGMPAENA AMQNKVHPKE WTYQNIATMK RQLKSMGLSL
DWSREFATCD VEYYHRQQML FIDLYEKGLV TRKTSKVNWD PVDNTVLANE QVVDGRGWRS
GALVEQRELT QWFFKITDFS EELLAGLDTL DQWPEKVRLM QRNWIGKSEG LQVRFALAAG
TAPAGFSEVE VYTTRPDTLF GAAFVAISAD HPLAKKLSEG NAALSSFIEE CHQQGTSLAA
LETAEKKGFD TGIKVKHPFD DNWELPVYVA NFVLMEYGTG AVFGCPAHDQ RDLDFANKYK
LKVTPVVLPK GEDAASFSIG ETAYTDDGVM INSRFLDGMT PEAAFNEVAS RLEKTDLVGR
PQAVRKVQFR LRDWGISRQR YWGCPIPMIH CESCGVNPVP RADLPVKLPD DVEFDRPGNP
LDRHATWRHV KCPKCGGDAR RETDTMDTFV DSSWYYTRFT APWENEPTNR KAADHWLPVD
QYIGGIEHAI LHLLYSRFFT RAMKVAGHVG VDEPFKGLFT QGMVVHETYK ANGQWVSPAD
IRIEEIDGKR VATMLDSGAP VEIGSIEKMS KSKKNVVDPD DIIASYGADT ARWFVLSDSP
PERDVIWTEA GAEGAHRFVQ RIWRLVAEAA PALKDVAPKA GTQGEALGVS KAVHKAVKAV
GDDIEKLAFN RGVARLYELV NTLSGALQQA ADGKADAEMK GALREATEML VLMTAPMMPH
LAEQCLAELG GKVAGKETLV ARAPWPVFDP ALVVENEIVL PVQINGKKRG DLTIARDADQ
ASIQQAVLEL DFVKAALNGG SPKKIIVVPQ RIVNVVA