ID   SYL_BRUAB               Reviewed;         877 AA.
AC   Q57B80;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 117.
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=BruAb1_1787;
OS   Brucella abortus biovar 1 (strain 9-941).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=262698;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9-941;
RX   PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA   Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA   Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT   "Completion of the genome sequence of Brucella abortus and comparison to
RT   the highly similar genomes of Brucella melitensis and Brucella suis.";
RL   J. Bacteriol. 187:2715-2726(2005).
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; AE017223; AAX75104.1; -; Genomic_DNA.
DR   RefSeq; WP_002964884.1; NC_006932.1.
DR   AlphaFoldDB; Q57B80; -.
DR   SMR; Q57B80; -.
DR   EnsemblBacteria; AAX75104; AAX75104; BruAb1_1787.
DR   KEGG; bmb:BruAb1_1787; -.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   Proteomes; UP000000540; Chromosome I.
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   CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 2.20.28.290; -; 1.
DR   Gene3D; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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   NCBIfam; TIGR00396; leuS_bact; 1.
DR   PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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_1000009303"
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;  97891 MW;  DCE9B90465E6875E 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 APWENEPTDR 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
//