ID   SYL_NITMU               Reviewed;         866 AA.
AC   Q2YBQ2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=Nmul_A0511;
OS   Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosospira.
OX   NCBI_TaxID=323848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25196 / NCIMB 11849 / C 71;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC
RT   25196.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000103; ABB73819.1; -; Genomic_DNA.
DR   RefSeq; WP_011379873.1; NZ_FNVK01000001.1.
DR   AlphaFoldDB; Q2YBQ2; -.
DR   SMR; Q2YBQ2; -.
DR   STRING; 323848.Nmul_A0511; -.
DR   EnsemblBacteria; ABB73819; ABB73819; Nmul_A0511.
DR   KEGG; nmu:Nmul_A0511; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_4; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000002718; 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; 1.
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; Reference proteome.
FT   CHAIN           1..866
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009380"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           624..628
FT                   /note="'KMSKS' region"
FT   BINDING         627
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   866 AA;  97239 MW;  9D6E9F9C850663CF CRC64;
     MQEKYHPQEI ESEAQQYWQQ TAAFKAVEAP EKRKYYCLSM FPYPSGKLHM GHVRNYTIGD
     VLSRYHRMQG YNVLQPMGWD AFGLPAENAA MQNNVPPAKW TYDNIAYMRK QLQSLGLAMD
     WDRELATCQP DYYRWNQWLF LRMLEKGLAY RTTGIVNWDP VDQTVLANEQ VIDGRGWRTG
     ALVEKHEIPM YYMKITAYAD ELLEALNALP GWPERVRTMQ ANWIGKSFGV EVRFPADAES
     GMPQDLKVFT TRADTLFGVT YVAVAAEHPV AQHAAKSNPA LAAFIEECRQ GAMMEAELAT
     QEKKGRDTGL YVIHPLTGAR LPVWIANYVL MGYGEGAVMA VPAHDERDFE FATQYSLPIR
     AVIKPVDSGL TVPLAQAYVE HGITFDSGEF SGLAFQPAVD AIAVALQQKG LGEKRVHYRL
     RDWGISRQRY WGCPIPLIYC DACGVVPVPD EQLPVVLPED LVPDGSGNPL AKTPSFYECS
     CPRCGQSARR ETDTMDTFVD SSWYYIRYAC TDQHRAMVDA RVDYWLPVDQ YIGGIEHAIL
     HLLYSRFWSK VMRDLGLVLF DEPFANLLTQ GMVLNEIMFR KTGSGRIVYF NPADVDIQTD
     EQGRRIGAVL RADGQPVEAG GIGTMSKSRN NGVDPQKLVE QYGADTARLF MMFASPPEQT
     LEWADAGVEG AFRFLKRLWK QVYDHLQQSG VANGPIPVAG LGPELKALRF QLHQTIAKVG
     DDLGRRHTFN TAIAAVMELM NALGKLQDSS PSARGLMQEA LENIVLLLSP IVPHICHVLW
     RELRPGTELL DQPWPQADVA ALVQDEIELI VQVNGKLRGK IRVAADTKPV IVEQLALENE
     QVRRFIDGKA VKKVVMVPGK LVNIVI