ID   SYL_MYCPN               Reviewed;         793 AA.
AC   P75398;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, 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}; OrderedLocusNames=MPN_384;
GN   ORFNames=MP453;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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; U00089; AAB96101.1; -; Genomic_DNA.
DR   PIR; S73779; S73779.
DR   RefSeq; NP_110072.1; NC_000912.1.
DR   RefSeq; WP_010874740.1; NC_000912.1.
DR   AlphaFoldDB; P75398; -.
DR   SMR; P75398; -.
DR   STRING; 272634.MPN_384; -.
DR   EnsemblBacteria; AAB96101; AAB96101; MPN_384.
DR   KEGG; mpn:MPN_384; -.
DR   PATRIC; fig|272634.6.peg.415; -.
DR   HOGENOM; CLU_004427_0_0_14; -.
DR   OMA; TFMVLAP; -.
DR   BioCyc; MPNE272634:G1GJ3-608-MON; -.
DR   Proteomes; UP000000808; 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   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..793
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152050"
FT   MOTIF           39..50
FT                   /note="'HIGH' region"
FT   MOTIF           569..573
FT                   /note="'KMSKS' region"
FT   BINDING         572
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   793 AA;  91084 MW;  DAD90195932B62D9 CRC64;
     MYNHNLLEEK WLQLWKTKQV NRFFDDKTKP KYYILDMFPY PSAAGLHLGH VRAYTITDVL
     SRYHKAKGFN VIHPIGFDAF GLPAEQYAIA SNKHPGDWTD KNITNFIEQL TAFGFDYDYQ
     LSLKTTDPRY YQYTQWIFGQ LFEAGLAEVK EIDVNWCAEL GTVLANEEVL IDSNGNAVSE
     RGEFPVTKRK MKQWVLKITA FAESLLNGLA ELDWHQSIKE MQTNWIGKSE GVEVTFDIEN
     SKETITIFTT KVQTIFGVTF LALSNSHPLV KEVAKTNPKI AQFLQKQAQK TTTVKQPETL
     HDGVDLKLKA INPATNTAIP LYVANYVVEG YGTDAVMGVP AHNENDNFFA RKQKLPIITV
     IDKQERLQHS GQFSGLNSQT ANTQITQMLV ERQKAKKTTV YKLRDWIFSR QRYWGEPFPI
     LFDENNQPHL VKELPVTLPA LANYQPDGST NPPLWRNQEW AKVKQGNQTF TRETSTMPQW
     AGSCWYYLGY LMLINNENFW PIDSREAKDL FERYLPVDLY VGGAEHAVLH LLYARFWHQF
     LYQKGIVTTK EPFKKLINQG MVLGPDGKKM SKSKGNTINP TPLIDSHGAD ALRLYLMFMG
     PISAALTWLD DGLNGMRRWL DRVHNFFHKE NIIKETVDQE TVYGYNLFLK RSFEHLEKQE
     LNLVISQMMI FLNLLYKTKQ LTLAYAKGFL TVLSFFAPYL AEELNAKLGM EPFIVHAQLP
     NVDNSVLETD KVKIILSVNG RFKGTKEFAK GVDEQTVLKA FKTDPEFQAL FDQPLARVVF
     VPNRIINVLL KSE