ID   SYL_FLAJ1               Reviewed;         954 AA.
AC   A5FMG2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, 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=Fjoh_0565;
OS   Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC
OS   14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=376686;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 /
RC   UW101;
RX   PubMed=19717629; DOI=10.1128/aem.01495-09;
RA   McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G.,
RA   Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R.,
RA   Cheng Y.Q., Stein J.L.;
RT   "Novel features of the polysaccharide-digesting gliding bacterium
RT   Flavobacterium johnsoniae as revealed by genome sequence analysis.";
RL   Appl. Environ. Microbiol. 75:6864-6875(2009).
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; CP000685; ABQ03600.1; -; Genomic_DNA.
DR   RefSeq; WP_012022656.1; NZ_MUGZ01000026.1.
DR   AlphaFoldDB; A5FMG2; -.
DR   SMR; A5FMG2; -.
DR   STRING; 376686.Fjoh_0565; -.
DR   KEGG; fjo:Fjoh_0565; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_10; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000006694; 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   CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   Gene3D; 3.40.50.620; HUPs; 3.
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   NCBIfam; TIGR00396; leuS_bact; 1.
DR   PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   Pfam; PF13603; tRNA-synt_1_2; 1.
DR   PRINTS; PR00985; TRNASYNTHLEU.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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..954
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000074833"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           729..733
FT                   /note="'KMSKS' region"
FT   BINDING         732
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   954 AA;  108655 MW;  D29CBF67221F04B1 CRC64;
     MKYNPNEIEA KWQKYWAENQ TFAAKNNSEK PKHYVLDMFP YPSGAGLHVG HPLGYIASDV
     YSRFKRHQGF NVLHPMGYDS FGLPAEQYAI QTGQRPEDTT RVNIDGGVDK EGKQIAGYRK
     QLDKIGFSFD WAREVRTSNP DYYKHTQWIF IQLFNSWYCR KQGKAFDISE LVTVFEESGN
     ALVEAVCDDN VTIFTADEWK SYSDDQKEKI LLQYRMTYLA ETEVNWCPGL GTVLANDEIV
     NGVSERGGFP VIRKKMTQWS MRISAYAERL LQGLNDIDWS ESIKESQRNW IGKSVGALVT
     FNVKNHDEVI EVFTTRPDTI FGVTFMTLAP EHDLVAKITT PEQKEAVEAY IEKTAKRSER
     ERMADVKTIS GVFTGAYAEH PFTKEAIPVW IGDYVLAGYG TGAVMAVPCG DERDYAFANF
     FKGQNGMQEI KNIFANVDIS EAAYGSKDNV EIAASDFLNG LNYKDATAKA IYKLEEIGQG
     KGKTNYRLRD AVFSRQRYWG EPFPVYYVNG LPKMIDTQHL PIILPEVEKY LPTEDGLPPL
     GNAAVWAWDI KENKVVNTDL VDNVSIFPLE LNTMPGWAGS SWYWMRYMDA HNENEFASKE
     ALAYWENVDL YIGGSEHATG HLLYSRFWNK FLKDKGFAPT EEPFKKLINQ GMILGTTAYV
     YRLEGTNTFV SKNKIKGQNV QPIRVDVHFV NSSDELNIEK FKAWREDFNT AEFIFDENGK
     YIVGREVEKM SKSYYNVVTP DDICAEYGAD TLRLYEMFLG PLEQAKPWNT AGISGVFGFL
     KKLWRLYFDD NGLIVNNDEP TKDNLKSLHK TIKKVAEDIE NFSFNTSVSQ FMICVNELSS
     QNCHSRAILE PLAILVSPYA PHIAEELWAQ LGHKTSISEV AFPVFDAKHL VETNKEYPVS
     FNGKMRFTIE LPLDLTAAQI EEIVMKDERT QKQLDGRIPN KVIIVPGKII NLVG
//