ID   SYL_NEIMB               Reviewed;         876 AA.
AC   Q9JXT2;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 131.
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=NMB1897;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17038831; DOI=10.4161/hv.1.2.1651;
RA   Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.;
RT   "Characterization of the protein content of a meningococcal outer membrane
RT   vesicle vaccine by polyacrylamide gel electrophoresis and mass
RT   spectrometry.";
RL   Hum. Vaccin. 1:80-84(2005).
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   -!- MISCELLANEOUS: Present in outer membrane vesicle formulations which are
CC       used as vaccines in human.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00049}.
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DR   EMBL; AE002098; AAF42228.1; -; Genomic_DNA.
DR   PIR; G81029; G81029.
DR   RefSeq; NP_274892.1; NC_003112.2.
DR   RefSeq; WP_002225801.1; NC_003112.2.
DR   AlphaFoldDB; Q9JXT2; -.
DR   SMR; Q9JXT2; -.
DR   STRING; 122586.NMB1897; -.
DR   PaxDb; 122586-NMB1897; -.
DR   KEGG; nme:NMB1897; -.
DR   PATRIC; fig|122586.8.peg.2420; -.
DR   HOGENOM; CLU_004427_0_0_4; -.
DR   InParanoid; Q9JXT2; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000000425; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..876
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152054"
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;  98097 MW;  7A53210ED4A823AA CRC64;
     MQEQYRPAAI 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 AAEHPLAAAA AADKPELQAF IAECKAGSVA
     EADMATMEKK GVPTGRYVVN PLNGDKLEVW IANYVLWGYG DGAVMAVPAH DERDFEFATK
     YNLPKKQVIA VGDNAFDENQ WQEWYGDKEN 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
//