ID   SYL_LARHH               Reviewed;         866 AA.
AC   C1DA02;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=LHK_00119;
OS   Laribacter hongkongensis (strain HLHK9).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Laribacter.
OX   NCBI_TaxID=557598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLHK9;
RX   PubMed=19283063; DOI=10.1371/journal.pgen.1000416;
RA   Woo P.C.Y., Lau S.K.P., Tse H., Teng J.L.L., Curreem S.O., Tsang A.K.L.,
RA   Fan R.Y.Y., Wong G.K.M., Huang Y., Loman N.J., Snyder L.A.S., Cai J.J.,
RA   Huang J.-D., Mak W., Pallen M.J., Lok S., Yuen K.-Y.;
RT   "The complete genome and proteome of Laribacter hongkongensis reveal
RT   potential mechanisms for adaptations to different temperatures and
RT   habitats.";
RL   PLoS Genet. 5:E1000416-E1000416(2009).
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; CP001154; ACO73115.1; -; Genomic_DNA.
DR   RefSeq; WP_012695610.1; NC_012559.1.
DR   AlphaFoldDB; C1DA02; -.
DR   SMR; C1DA02; -.
DR   STRING; 557598.LHK_00119; -.
DR   PRIDE; C1DA02; -.
DR   EnsemblBacteria; ACO73115; ACO73115; LHK_00119.
DR   KEGG; lhk:LHK_00119; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_4; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000002010; 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; 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; Reference proteome.
FT   CHAIN           1..866
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000199211"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           630..634
FT                   /note="'KMSKS' region"
FT   BINDING         633
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   866 AA;  96345 MW;  788FA95730AC2446 CRC64;
     MHEQYQPRDI EVAAQQKWEK TAAFKAVEDA SRPKYYCLSM FPYPSGKLHM GHVRNYTIGD
     VLSRYMALKG YNVLQPMGWD AFGMPAENAA LKNQVAPAAW TYSNIEYMKT QLKSLGFAID
     WEREVTTCKP DYYRWEQWLF TRLFEKGVIY RKNGVVNWDP VDQTVLANEQ VIDGRGWRSG
     ALVEKREIPM YYFGITQYAD ELLADLDTLD WPPQVATMQR NWIGKSFGAD VRFAYDEASI
     GSAGELTVYT TRPDTLMGAT YVAVAAEHPL ATQAAANDPA LQAFIAKCKA GSVAEADMAT
     MEKEGMPTGL FVVHPLTGAK LPVWVANYVL MSYGSGAVMA VPAHDERDFA FANKYALPIQ
     QVIALKEGDA TFDASTWQDW YATKDDSTRL VNSGKYDGLD FQGAFDAIVA DLAAKAAGEK
     KTQYRLRDWG ISRQRYWGCP IPIIHCDSCG DVPVPADQLP VVLPENVVPD GSGNPLAKMP
     EFYETTCPCC GKPARRETDT MDTFVESSWY FARYASPDCA TGMVDDRARY WLNVDQYIGG
     IEHAILHLLY ARFFNKLMRD EGLLANDEPF QRLLTQGMVV CETFYRDLDN GSKEWITPAD
     VVIERDGKGK IIAATHKADG LPVVVGGIEK MSKSKNNGVD PQALIEQYGA DTARLFMMFA
     APPSQSLEWS DAGVEGAYRF LKRLYKIVSE YVAGGVAERF VAGELTADEK ALRLKLHTTI
     QKVSDDFGVR QQFNTAIAAV MELLNLFDRT EASRAVRQEV LESVVVLLSP IVPHICETLW
     SALKPGSELL AQRWPEVDPA ALVQDEIELV VQVNGKLRGS VRVAADAGRD VIEAAALAHE
     QVRKFMDGQP AKKVIVVPGR LVNIVV