ID   SYL_NEIMF               Reviewed;         876 AA.
AC   A1KS07;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=NMC0326;
OS   Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM
OS   15464 / FAM18).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=272831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700532 / DSM 15464 / FAM18;
RX   PubMed=17305430; DOI=10.1371/journal.pgen.0030023;
RA   Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C.,
RA   Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K.,
RA   Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S.,
RA   Quail M.A., Achtman M., Barrell B.G., Saunders N.J., Parkhill J.;
RT   "Meningococcal genetic variation mechanisms viewed through comparative
RT   analysis of serogroup C strain FAM18.";
RL   PLoS Genet. 3:230-240(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; AM421808; CAM09636.1; -; Genomic_DNA.
DR   RefSeq; WP_002248137.1; NC_008767.1.
DR   AlphaFoldDB; A1KS07; -.
DR   SMR; A1KS07; -.
DR   EnsemblBacteria; CAM09636; CAM09636; NMC0326.
DR   KEGG; nmc:NMC0326; -.
DR   HOGENOM; CLU_004427_0_0_4; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000002286; 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; 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.
FT   CHAIN           1..876
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009377"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           634..638
FT                   /note="'KMSKS' region"
FT   BINDING         637
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   876 AA;  97997 MW;  9C7BF627B10C836C CRC64;
     MQEHYQPAAI EPAAQKKWDD ARIFNVSEDA SKPKYYCLSM FPYPSGKLHM GHVRNYTIGD
     VLSRFKLLNG FNVMQPMGWD AFGMPAENAA MKNNVAPAAW TYDNIEYMKT QLKSLGFAID
     WARETATCKP EYYRWEQWLF TKLFEKGIVY RKNGTVNWDP VDQTVLANEQ VIDGRGWRSG
     ALIEKREIPM YYFKITDYAE ELLNDLDKLE HWPEQVKTMQ RNWIGKSRGM TVRFAVSDDS
     KQGLEGDYAK LLQVYTTRPD TLMGATYVAV AAEHPLAAAA AADKPELQAF IAECKAGSVA
     EADMATMEKK GVPTGRYVVN PLNGDKLEVW IANYVLWGYG DGAVMAVPAH DERDFEFAAK
     YNLPKKQVIA VGDNAFDANR WQEWYADKEN GVLVNSGDLD GLDFQTAFDA VAAKLQSQGA
     GEPKTQYRLR DWGISRQRYW GCPIPIVHCE QCGDVPVPAD QLPVVLPENV VPDGMGSPLA
     KMPEFYETAC PCCGGAAKRE TDTMDTFMES SWYFFRYMSP KFSDGMVDPA AAKYWGAVDQ
     YIGGIEHAIL HLLYARFFTK LMRDEGLVNV DEPFERLLTQ GMVVCETYYR ENDKGGKDWI
     NPADVELTFD DKGRPISAVL KADGLPVVIS GTEKMSKSKN NGVDPQELIN AYGADTARLF
     MMFAAPPEQS LEWSDSGVEG AHRFLRRLWR TVYEYLKQGE AVKAFAGSQD GLSKELKDLR
     HKLHATTAKV SDDYGRRQQF NTAIAAVMEL LNQYDKTDTG GEQGRAVAQE VLETAVRLLW
     PIVPHICETL WSELNGAKLW EAGWPTVDEA ALVKSEIEVM VQVNGKLRGK ITVAADASKA
     DLEAAALATE GAVKFMEGKP AKKIIVVPGR LVNIVV