ID   SYL_NEIMA               Reviewed;         910 AA.
AC   Q9JW39; A1IQ09;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 130.
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=NMA0559;
OS   Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS   Z2491).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15465 / Z2491;
RX   PubMed=10761919; DOI=10.1038/35006655;
RA   Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA   Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA   Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA   Barrell B.G.;
RT   "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT   Z2491.";
RL   Nature 404:502-506(2000).
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; AL157959; CAM07834.1; -; Genomic_DNA.
DR   PIR; F81974; F81974.
DR   RefSeq; WP_002246442.1; NC_003116.1.
DR   AlphaFoldDB; Q9JW39; -.
DR   SMR; Q9JW39; -.
DR   EnsemblBacteria; CAM07834; CAM07834; NMA0559.
DR   KEGG; nma:NMA0559; -.
DR   HOGENOM; CLU_004427_0_0_4; -.
DR   Proteomes; UP000000626; 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   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 2.20.28.290; -; 1.
DR   Gene3D; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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; 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   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; 2.
DR   Pfam; PF13603; tRNA-synt_1_2; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 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..910
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152053"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           668..672
FT                   /note="'KMSKS' region"
FT   BINDING         671
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   910 AA;  101506 MW;  0609FDE0E39C0DE6 CRC64;
     MQEQYQPAAI EPAAQKKWDD ARIFNVSEDA SKPKYYCLSM FPYPSGKLHM GHVRNYTIGD
     VLSRFKLLNG FNVMQPMGWD AFGMPAENAA MKNNVAPAAW TYDNIEYMKT QLKSLGFAID
     WARETATCKP EYYRWEQWLF TKLFEKGIVY RKNGTVNWDP VDQTVLANEQ VIDGRGWRSG
     ALIEKREIPM YYFKITDYAE ELLNDLDKLE HWPEQVKTMQ RNWIGKSRGM TVRFAVSDDS
     KQGLEGDYAK FLQVYTTRPD TLMGATYVAV AAEHPLATAA AADKPELQAF IAECKAGSVA
     EADMATMEKK GVPTGRYVVN PLNGDKLEVW IANYVLWGYG DGAVMAVPAH DERDFEFAAK
     YSLPKKQVLQ RVTIGLSPEQ EEAMGFGGGS GCGAGYGDGS GSDSRDLPFM PNKWQAWYGV
     KDDFMVLINS GELDGMNYQT AFDAVAAKLQ AIGAGEPKTQ YRLRDWGISR QRYWGCPIPI
     VHCEQCGDVP VPADQLPVVL PENVVPDGMG SPLAKMPEFY ETTCPCCGGA AKRETDTMDT
     FMESSWYFFR YMSPKFSDGM VDPAAAKYWG AVDQYIGGIE HAILHLLYAR FFTKLMRDEG
     LVNVDEPFER LLTQGMVVCE TYYRENDKGG KDWINPADVE LTFDDKGRPV SAVLKVDGLP
     VVISGTEKMS KSKNNGVDPQ ELINAYGADT ARLFMMFAAP PEQSLEWSDS GVEGAHRFLR
     RLWRTVYEYL KQGEAVNAFA GSQDGLSKEL KDLRHKLHST IAKVSDDYGR RQQFNTAIAA
     VMELLNQYDK TDTGSEQGRT VAQEVLEAAV RLLWPIVPHI CETLWSELNG AKLWEAGWPA
     VDEAALVKSE IEVMVQVNGK LRGKITVAAD ASKADLEAAA LATEGAVKFM EGKPAKKIIV
     VPGRLVNIVV
//