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SYL_BRUMB
ID   SYL_BRUMB               Reviewed;         877 AA.
AC   C0RF58;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=BMEA_A1857;
OS   Brucella melitensis biotype 2 (strain ATCC 23457).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=546272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23457;
RA   Setubal J.C., Boyle S., Crasta O.R., Gillespie J.J., Kenyon R.W., Lu J.,
RA   Mane S., Nagrani S., Shallom J.M., Shallom S., Shukla M., Snyder E.E.,
RA   Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., Munk C., Tapia R.,
RA   Han C., Detter J.C., Bruce D., Brettin T.S.;
RT   "Brucella melitensis ATCC 23457 whole genome shotgun sequencing project.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001488; ACO01530.1; -; Genomic_DNA.
DR   RefSeq; WP_002967933.1; NC_012441.1.
DR   AlphaFoldDB; C0RF58; -.
DR   SMR; C0RF58; -.
DR   PRIDE; C0RF58; -.
DR   EnsemblBacteria; ACO01530; ACO01530; BMEA_A1857.
DR   GeneID; 45125090; -.
DR   KEGG; bmi:BMEA_A1857; -.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000001748; 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   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_1000199185"
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;  97863 MW;  56D2AAA6E29FFD95 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 KAAHKAVKAV
     GDDIEKLAFN RGVARLYELV NTLSGALQQA ADGKADAEMK GALREATEML VLMTAPMMPH
     LAEQCLAELG GKVAGKETLV ARAPWPVFDP ALVVENEIVL PVQINGKKRG DLTIARDADQ
     ASIQQAVLEL DFVKAALNGG SPKKIIVVPQ RIVNVVA
 
 
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