ID   SYL_CAUSK               Reviewed;         861 AA.
AC   B0T6E7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=Caul_5030;
OS   Caulobacter sp. (strain K31).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter; unclassified Caulobacter.
OX   NCBI_TaxID=366602;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K31;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., Brettin T.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Stephens C., Richardson P.;
RT   "Complete sequence of chromosome of Caulobacter sp. K31.";
RL   Submitted (JAN-2008) 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; CP000927; ABZ74150.1; -; Genomic_DNA.
DR   RefSeq; WP_012289019.1; NC_010338.1.
DR   AlphaFoldDB; B0T6E7; -.
DR   SMR; B0T6E7; -.
DR   STRING; 366602.Caul_5030; -.
DR   EnsemblBacteria; ABZ74150; ABZ74150; Caul_5030.
DR   KEGG; cak:Caul_5030; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
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; 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.
FT   CHAIN           1..861
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000074827"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           623..627
FT                   /note="'KMSKS' region"
FT   BINDING         626
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   861 AA;  94852 MW;  4626AE1743C9F46D CRC64;
     MARYNPKDTE PKWRAAWASA NTFLTPITPD ARPKYYVLEM FPYPSGRIHM GHVRNYAMGD
     VVARYKRAQG FNVLHPMGWD AFGMPAENAA MERGVHPKGW TYDNIAAMRE QLKALGLSID
     WSREFATCDP EYYGKQQAWF LHLLKRGLVY RKEASVNWDP VDMTVLANEQ VIDGKGWRSG
     ATVEKRKLTQ WFLRITDYAD ALIDGLKTLD RWPEKVRIMQ ENWIGRSKGL RFTFKFDGEA
     PAGHADGLEV YTTRPDTLFG ASFVGIAPEH PLAEQLAAAD PAVAAFVAEC RKGGTSEADI
     EGAEKLGRDT GLRVVHPLDP TLTLPVWIAN FILMDYGTGA IFACPAHDQR DLDFARKYDL
     PVLPVVLPPG EDAATFQVGK EAYVGPGAIF NSEFLDGLDV EAAKTEAVNR IEAMDQGQGA
     TVYRLRDWGV SRQRYWGCPI PVIHCEACGP VGVPEDQLPV VLPDDVAFDK PGNPLLRHPT
     WRHTTCPSCG GKAERETDTL DTFVDSSWYF ARFTDPTAAE PISKAAADHW MPVDQYIGGV
     EHAVLHLLYA RFITRALKDE GLVSVEEPFA GLFTQGMVTH EAYKNAAGEW VEPSDVVIAV
     EGATRSARHA ATGEPITIGD IEKMSKSKKN VVAPEDIFEA YGVDAARLFV MSDSPPERDV
     QWTNSGVEGS WRFTHRVWNE FESQPAGDFA HDDSDAAAVA LRKGAHRLIG FVTDSIEGFR
     FNSGVARLYE FLNMLKAAPA EGASQGVLAA RAEALEILAR LISPFTPHLA EEAWAHLGKA
     GMVVDAPWPK ADAALAADDE RVLPIQINGK RRGEIKVKAG TAEAEVEKIA LADPAVLAHL
     EGLTVRKVIV VKDRIVNIVA G