ID   SYL_ACTSZ               Reviewed;         860 AA.
AC   A6VMB8;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=Asuc_0743;
OS   Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 /
OS   130Z).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=339671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z;
RX   PubMed=21118570; DOI=10.1186/1471-2164-11-680;
RA   McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A.,
RA   Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L.,
RA   Burkhart K.B., Harkins V., Vieille C.;
RT   "A genomic perspective on the potential of Actinobacillus succinogenes for
RT   industrial succinate production.";
RL   BMC Genomics 11:680-680(2010).
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; CP000746; ABR74115.1; -; Genomic_DNA.
DR   RefSeq; WP_012072494.1; NC_009655.1.
DR   AlphaFoldDB; A6VMB8; -.
DR   SMR; A6VMB8; -.
DR   STRING; 339671.Asuc_0743; -.
DR   PRIDE; A6VMB8; -.
DR   EnsemblBacteria; ABR74115; ABR74115; Asuc_0743.
DR   KEGG; asu:Asuc_0743; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001114; 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; 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; 3.
DR   Pfam; PF13603; tRNA-synt_1_2; 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..860
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000071107"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           619..623
FT                   /note="'KMSKS' region"
FT   BINDING         622
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   860 AA;  97643 MW;  DCAD14949EAB5A53 CRC64;
     MQEQYRPDLI EAEVQKYWQE NKTFKAIKDT NKEKYYCLSM LPYPSGRLHM GHVRNYTIGD
     VVSRYQRMIG KNVLQPMGWD AFGLPAEGAA VKNNTAPAKW TYENIEYMKN QLKVLGFSYD
     WEREVTTCRP EYYKWEQWFF TELYKKGLVY KKTSVVNWCP NDETVLANEQ VHEGCCWRCD
     TPVEQREIPQ WFIKITDYAE QLLGGLDTLP EWPEMVKTMQ RNWIGRSEGV EITFKIENSD
     ETVAVYTTRP DTFYGVSYMA VAAGHPLAER AAQNNPDLAK FIQECKNTKV AEAELATMEK
     KGMATGLNAV HPITGKPVPI WVANFVLMHY GTGAVMAVPA HDQRDFEFAT KYDLPINQVI
     APVNGEDIDL SKAAFTEHGK LVNSAEFDGL DFDAAFNGIA DKLERMGAGK RQVNYRLRDW
     GVSRQRYWGA PIPMLTLENG DVVPAPLQDL PIVLPEDVVM DGVKSPIKAD PDWAKTTYNG
     RPALKETDTF DTFMESSWYY ARYTCPQYHE GMLDSEEANY WLPVDQYIGG IEHATMHLLY
     FRFFHKLLRD AGLVSTDEPT KKLLCQGMVL ADAFYYTSPT NERIWVSPTK VTLERDEKGR
     IVKALDDEGR ELVHAGMTKM SKSKNNGIDP QEMVEKYGAD TVRLFMMFAS PAEMTLEWQE
     SGVEGAKRFL GRLWNLVFEY NKNPAKTALN PTALSGVQKA LRRGVHKTIA KVSDDIGRRQ
     TFNTAIAAIM ELMNKLTRAS LAGEQDRAIM GEALSAVVRM LYPITPHVCF QLWKELGNED
     VIDFAPWVQA DEAAMVEEEK LVVVQVNGKV RGKITVPADM AEDDIKQAAL ADENVQKFLS
     GLNIVKTIYV PGKLFSFVAK