ID   SYL_HAHCH               Reviewed;         861 AA.
AC   Q2SBE7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 113.
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=HCH_05355;
OS   Hahella chejuensis (strain KCTC 2396).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Hahellaceae; Hahella.
OX   NCBI_TaxID=349521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 2396;
RX   PubMed=16352867; DOI=10.1093/nar/gki1016;
RA   Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA   Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA   Oh T.K., Kim J.F.;
RT   "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT   algicidal agent.";
RL   Nucleic Acids Res. 33:7066-7073(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; CP000155; ABC32027.1; -; Genomic_DNA.
DR   RefSeq; WP_011399091.1; NC_007645.1.
DR   AlphaFoldDB; Q2SBE7; -.
DR   SMR; Q2SBE7; -.
DR   STRING; 349521.HCH_05355; -.
DR   EnsemblBacteria; ABC32027; ABC32027; HCH_05355.
DR   KEGG; hch:HCH_05355; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000000238; 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..861
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009351"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           620..624
FT                   /note="'KMSKS' region"
FT   BINDING         623
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   861 AA;  98380 MW;  F240E4CD127901D7 CRC64;
     MEELYHPKKV EQEAQKFWEE TDAFKVDEEP GKEKFYCLSM FPYPSGKLHM GHVRNYTIGD
     VISRYQRMQG KNVLQPMGWD AFGLPAENAA LKNNVAPAKW TYENIAYMKN QLKLLGFGYD
     WNRELATCRP EYYKWEQWFF TRLYEKGLVY KKMSTVNWDP VDETVLANEQ VIDGKGWRSG
     AVVERREIPQ WFIKITDYAE QLLNDLDKLE NWPEQVKTMQ RNWINKSEGV EFHFKLKDHD
     GDLQVYTTRP DTIMGVTYVA IAPQHPLALE AAASNPQLAK FLDECKNTKV AEADMATMEK
     RGMDTGFFVI HPLTNEPAPI WVANFVLMDY GSGAVMSVPG HDERDHEFAL KYGLPIKQVI
     SVIDADEVDI QEKAITEKGI LVNSGEFTGM TSQEAFDAVA EKLTAMGIGE KKINYRLRDW
     GVSRQRYWGA PIPMMTQEDG TEVPVPLADL PVRLPEDVEM DGVKSPIKAD PNWSKRSYNG
     QPATQETDTF DTFMESSWYY ARFCCPNLES AMLDPAAANY WLPVDYYVGG IEHAILHLLY
     SRFFHKLLRD EGLVDSDEPF KKLLCQGMVI AETFYREDPS SKKTYFNPRD VRVELDTQGN
     SPKAFLIEDG QPVIIGPKEK MSKSKNNGVD PQELIDKYGA DTVRLFTMFA APPEQSLEWS
     ESGVEGQHRF LRRLWKLVHT HVEKKGAAPL NVAELNETQR TLRRKTHETI KKMTDEFNHR
     MAINTGIAMV MELLNELSRF EDDSPQGLAV VQEALETAVL VLAPIVPHIS HGLWRELGHE
     DVVMNAPWPQ LDEKALEKDS IELVVQVNGK LRARIQAAAS ANKDELEKLA FDDENVQRFM
     EDKTVVKVIV VPGKLVNIVV K