ID   SYL_CELJU               Reviewed;         864 AA.
AC   B3PIB4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=CJA_0454;
OS   Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS   cellulosa).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Cellvibrio.
OX   NCBI_TaxID=498211;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ueda107;
RX   PubMed=18556790; DOI=10.1128/jb.01701-07;
RA   DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA   Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA   Nelson K.E.;
RT   "Insights into plant cell wall degradation from the genome sequence of the
RT   soil bacterium Cellvibrio japonicus.";
RL   J. Bacteriol. 190:5455-5463(2008).
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; CP000934; ACE83294.1; -; Genomic_DNA.
DR   RefSeq; WP_012486134.1; NC_010995.1.
DR   AlphaFoldDB; B3PIB4; -.
DR   SMR; B3PIB4; -.
DR   STRING; 498211.CJA_0454; -.
DR   EnsemblBacteria; ACE83294; ACE83294; CJA_0454.
DR   KEGG; cja:CJA_0454; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001036; 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; -; 1.
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; 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..864
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091301"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           622..626
FT                   /note="'KMSKS' region"
FT   BINDING         625
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   864 AA;  97610 MW;  EBC31552266D6203 CRC64;
     MQEQYNPAEV EAQAQQYWEE HQSFNVIEDP GKEKFYCLAM FPYPSGKLHM GHVRNYTITD
     VIARYQRMQG KNVLHPMGWD AFGLPAENAA LKHNTAPAKW TYSNTDHMRN QLKQLGFGFD
     WSRELTTCKP EYYQWEQWFF TRLYEKGLVY KKMSTVNWDP IDQTVLANEQ VIDGRGWRSG
     ALVERKEIPQ WFIKITDYAE ELLNDLDKLP NWPEQVKTMQ RNWIGKSRGL EMRFDLQSPV
     GEFTSFDIYT TRPDTLMGVT YVSLAAEHPI AKYLADSNPA LAQFIADCKV QSVAEADMAT
     MEKKGMDTGI KALHPITGEP VAVWVANYVL MDYGSGAVMA VPAHDQRDYE FAQKYHLGIT
     QVIAPQNGET IDLSQAAFTD KGVLVNSGEY DGLDFNAAFD AIASTLEMAN KGRVKTNYRL
     RDWGVSRQRY WGAPIPMFNL PEGGEIPVPA HKLPILLPEE VVMNGVQSPI KADPEWKKDE
     LDGQYVERET DTFDTFMESS WYYARYTCPN FTDGMINKAA ADYWLPVDQY VGGIEHAILH
     LLYSRFFHKL MRDEGLVSGD EPFERLLCQG MVNAESFFIK SEGKENWIEP ENVVIERDDK
     GRFIAAKHKI TGDAVEFGGV IKMSKSKANG VDPESVINQY GADTVRLFTM FAAPPEQSLE
     WSDSGVEGAS RFLRRLWKAV EGHINAGTPG KLDAASLPQQ QKDLRRKTHE TIQKVSDDYG
     RRQTFNTAIA AVMELLNETS KLSDRANPQG LAVEREALEA AILLLAPIVP HITQALWIEL
     GNSGIPLNQP WPTLDESALV RSTIEVVVQV NGKLRGKIDA AVDAPKELLE QIAVQQENVQ
     KFLEGVTVRK VIVVPNKLVN IVAN