ID   SYL_SYNJB               Reviewed;         882 AA.
AC   Q2JHX0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=CYB_2881;
OS   Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium
OS   Yellowstone B-Prime).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=321332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA-2-3B'a(2-13);
RX   PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA   Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N.,
RA   Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT   "Population level functional diversity in a microbial community revealed by
RT   comparative genomic and metagenomic analyses.";
RL   ISME J. 1:703-713(2007).
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; CP000240; ABD03801.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2JHX0; -.
DR   SMR; Q2JHX0; -.
DR   STRING; 321332.CYB_2881; -.
DR   KEGG; cyb:CYB_2881; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_3; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000001938; 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; 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   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..882
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009456"
FT   MOTIF           43..53
FT                   /note="'HIGH' region"
FT   MOTIF           632..636
FT                   /note="'KMSKS' region"
FT   BINDING         635
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   882 AA;  99521 MW;  6ED220A8B591A861 CRC64;
     MDARYNPQAI ESKWQAHWRE IGLDRTPELK DGSRKFYALS MFPYPSGNLH MGHVRNYTIT
     DVIARHKRMQ GYAVLHPMGW DAFGLPAENA AIDRGIPPAK WTYQNIAQMR EQLQRLGLSY
     DWEREITTCA PDYYKWTQWL FLQFFKAGLA YQKEAPVNWD PVDQTVLANE QVDAEGRSWR
     SGALVEKRML KQWFFKITAY ADQLLADLEK LSGWPERVRT MQENWIGQSV GAKVIFKTEA
     GDELAVFTTR PDTLWGATFM VMSPEHPLVD KLTTAEQLQA VRAYQAQAAA RSEIERSAED
     REKTGVWTGS YAINPVNQER IPIWIADYVL MGYGTGAIMA VPAHDQRDFE FARKFGLPIK
     RVVQPPEGSL SSTDRASGTE SSELQAAWTG EGVMINSGPL DGIPVGKGPG QSVERAIAWL
     EAQGLGEKQI NYRLRDWLIS RQRYWGCPIP VIHCPHCGIV PVPEKDLPVL LPEDVELTGR
     GGSPLAQLED WVKVKCPTCG AEARRETDTM DTFICSSWYF LRFSDARNDR EIFRKDRVNA
     WLPVDQYVGG IEHAILHLLY SRFFTKVLRD RGLLDFDEPF LRLLTQGMVQ GRTYYNPNKS
     GKDRWIPAAL VKDPDNPTDP ETGEPLEVIY ATMSKSKGNG VDPEEVLAHY GADTARMFIL
     FKAPPEKDLE WDDADVEGQF RFLNRVWRQV YEFVVRGGGT ESWRGRVSEL LPAKVEVGSL
     TKAEKDLRRA IHTAIKEVSE DLENDYQFNT AIAELMKLSN ALGEAGIPDS PVYAEGIRTL
     VLLMAPFAPH IAEELWQALG GADSVHRQSW PSYDPAALVA DTVTIVIQVN GKLRGSFEAP
     AEVTPEEQEQ LALRSEAAQK YLEGATPKKV VVVPKKLVNF VL