ID   SYL_NEOSM               Reviewed;         831 AA.
AC   Q2GDQ6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   27-MAR-2024, entry version 106.
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=NSE_0506;
OS   Neorickettsia sennetsu (strain ATCC VR-367 / Miyayama) (Ehrlichia
OS   sennetsu).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Neorickettsia.
OX   NCBI_TaxID=222891;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-367 / Miyayama;
RX   PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA   Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA   Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA   Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.C.,
RA   Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C.,
RA   Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D.,
RA   Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA   Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT   "Comparative genomics of emerging human ehrlichiosis agents.";
RL   PLoS Genet. 2:208-222(2006).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABD46464.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000237; ABD46464.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041917503.1; NC_007798.1.
DR   AlphaFoldDB; Q2GDQ6; -.
DR   SMR; Q2GDQ6; -.
DR   STRING; 222891.NSE_0506; -.
DR   KEGG; nse:NSE_0506; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000001942; 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; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   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..831
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334782"
FT   MOTIF           36..46
FT                   /note="'HIGH' region"
FT   MOTIF           607..611
FT                   /note="'KMSKS' region"
FT   BINDING         610
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   831 AA;  94528 MW;  716F59F6F03C73FF CRC64;
     MSNYDFKKIE QFSQSLWDFS SCDFQRKKYY VLSMFPYPSG KLHIGHLRNY VIGDVLARYK
     RSQGYNVLHP IGWDAFGLPA EKAAINSNIH PRIWTEKNIA KMRTSLKSIG LSYDWSRELS
     TCSPKYYEHE QKFFLAFLKA GLAYRKNSEV NWDPIDKTVL ANEQVIDGRG WRSGAVVVKR
     KIPQWFLKIS DFSEELLKGL ESLTGWPEKV KTMQTNWIGK SEGAVIKFSI SGYEERFIEV
     FTTRPETIFG ASFCAISVNH PLVNELNLLS NAEREILRIQ TTCESDHYDD NKNFSGTTNL
     EKVHEQKLGI LTKIKVKHPF SGDELPLYVA NFVFAEYGSG AIFGCPAHDT RDFAFAQQYN
     LPCLRVISAK CTNTALPYCL EEGVMCNSNF LDGMQVIEAR KFIIEKISSI GIGEAKNSYR
     LRDWGISRQR YWGCPIPVVY CEKCSMQPVK VEDLPVTLPE EVEFTVQGNP LEHHPTWKYT
     NCPKCGGPAV RDTDTFDTFF ESSWYFAAFC SKEGGIVKES CKRFLPVDMY IGGIEHAILH
     LLYARFFTRA LNKCGYIDIV EPFRNLLTQG MVCHETYQNS SGEYLYPEEA KSLLEKGEKV
     LVGKIEKMSK SKKNVVDLEE IVSKYGADAA RFFILSDNPP ENSFGWSDRG INASFKFLQR
     IKNLVERYLS SKNSGEVQTG QNVKIQINKI ICDMTKYMDE IKLNCAVAKI HELVNLLSAS
     GALSKETIHV LLRILEPFAP HLAEYLASKL ENNVILYGSP WVAYNEVLTQ SDAVTLMVRK
     NGKFVQLLEV KKDSSEEEII SQAKRLIKNA VVDKVIYVPG KMVNFLCSSP G
//