ID   SYL_SYNP2               Reviewed;         852 AA.
AC   B1XP90;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 99.
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};
GN   OrderedLocusNames=SYNPCC7002_A1694;
OS   Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS   quadruplicatum).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=32049;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA   Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA   Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA   Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT   "Complete sequence of Synechococcus sp. PCC 7002.";
RL   Submitted (FEB-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; CP000951; ACA99683.1; -; Genomic_DNA.
DR   RefSeq; WP_012307306.1; NC_010475.1.
DR   AlphaFoldDB; B1XP90; -.
DR   SMR; B1XP90; -.
DR   STRING; 32049.SYNPCC7002_A1694; -.
DR   PRIDE; B1XP90; -.
DR   EnsemblBacteria; ACA99683; ACA99683; SYNPCC7002_A1694.
DR   KEGG; syp:SYNPCC7002_A1694; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_3; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000001688; 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; 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..852
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091374"
FT   REGION          586..606
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           614..618
FT                   /note="'KMSKS' region"
FT   BINDING         617
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   852 AA;  95642 MW;  0E88E0B0431A3D66 CRC64;
     METRYSAADI EAKWQQQWLE LGLDKTPSQS DKPKFYALSM FPYPSGKLHM GHVRNYVITD
     VIARYKRMQG YRVLHPMGWD AFGLPAENAA IDRGIPPAKW TYQNIAQMRE QLKQLGLSID
     WDREVATCSP DYYKWTQWLF LQFYKAGLAY QKEAAVNWDP IDQTVLANEQ VDAEGRSWRS
     GAIVEKKLLR QWFLKITDYA EELLQDLNTL DGWPERVKLM QENWIGKSTG AHLEFPVVGS
     DEKVAVFTTR LDTVFGVTYV VLAPEHPLVA QVTTPAQKAA VDAFIAEVSQ ESEQDRTADD
     KPKKGVATGG MVTNPFTGEE VPILIANYVL YEYGTGAVMG VPAHDSRDCK FAKENNLPIK
     MVIIPEGGDA TAVLTEAYTE AGIMVNSGQF DGLVSTEGKK AIAKFAAENG FGREQIQYRL
     RDWLISRQRY WGCPIPMIYC DDCGVVPVPD SDLPVVLPED VEFSARGGSP LAQMADWQAV
     DCPCCGKAAR RETDTMDTFI DSSWYFLRYT DANNTEKPFA LDPVNDWMAV DQYVGGIEHA
     ILHLLYSRFF TKVVRDRQLV SVDEPFKRLL TQGMVQALTY KNPRTNKYVP ADQVDPNDPK
     DPETGEPLTG FYEKMSKSKY NGVDPALVLD KYGADTARMF ILFKAPPEKD LEWDDADVEG
     QFRFLNRIWN LVAGYEAAET SVKATGELSK AEKDLRRAVH TAIKEIQEDL EGDYQFNTAI
     AELMKLNNAI KDVKCVDSPV YKEAIETLIL LLAPFAPHIA DELWSNLGHS ESIHTVPFPQ
     LDETALTVDE ITIVIQILGK TRGTIQVPAG ISKADLEKTA TASDIAQRYI AGKEIKKVIV
     VPNKLVNFVI PK