ID   SYL_MALP2               Reviewed;         799 AA.
AC   Q8EW18;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 118.
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=MYPE3890;
OS   Malacoplasma penetrans (strain HF-2) (Mycoplasma penetrans).
OC   Bacteria; Tenericutes; Mycoplasmoidales; Mycoplasmoidaceae; Malacoplasma.
OX   NCBI_TaxID=272633;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HF-2;
RX   PubMed=12466555; DOI=10.1093/nar/gkf667;
RA   Sasaki Y., Ishikawa J., Yamashita A., Oshima K., Kenri T., Furuya K.,
RA   Yoshino C., Horino A., Shiba T., Sasaki T., Hattori M.;
RT   "The complete genomic sequence of Mycoplasma penetrans, an intracellular
RT   bacterial pathogen in humans.";
RL   Nucleic Acids Res. 30:5293-5300(2002).
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; BA000026; BAC44178.1; -; Genomic_DNA.
DR   RefSeq; WP_011077214.1; NC_004432.1.
DR   AlphaFoldDB; Q8EW18; -.
DR   SMR; Q8EW18; -.
DR   STRING; 272633.26453847; -.
DR   EnsemblBacteria; BAC44178; BAC44178; BAC44178.
DR   KEGG; mpe:MYPE3890; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_14; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000002522; 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; 2.
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..799
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152049"
FT   MOTIF           39..50
FT                   /note="'HIGH' region"
FT   MOTIF           575..579
FT                   /note="'KMSKS' region"
FT   BINDING         578
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   799 AA;  93330 MW;  33B62E3CD73D06FE CRC64;
     MYNHNLVEKK WRKIWKDSNL HTFKDNLKKP KFYALDMFPY PSGAGLHMGH VKSYTPTDVY
     ARFKRYQGYS VLHPMGWDAF GLPAEQFALA TKNHPATFTD QNINNFKLQI DQLGFWFDWN
     KEVNTTDPNF YKWTQWIFIK LFENGLAEIK DIDVNWCQEL GTVLANEEVL TDEKGNKVSE
     RGKYPVIKKP MKQWVLKITK FADQLIDDLE LTDWTVGLKN IQKKWIGKSI GATVKFKIQN
     SDSEIEVFTS RPDTIFGVSF IGLSSDHELV LKEKTKNKKI EAFLNELSSL KEYERTAINV
     EKKGVLLDIK AIHPITKQLV PVYVCNYVLS NYGNGAIMGV PAGDKRDYDF AKLFNLEIKE
     IIKDHPAPYE EDGIHINSDF LNGLNNEDAI AKIVEYLEKN KIGKKQVNYK LKDWLFSRQR
     YWGEPFPVLF DEKGNIIVEK NLPLLLPETN DIKPSGTGES PLANLTEWVN VKIDSKLYRR
     ETNTMPQWAG SCWYYLAYLL KDGDSYLPLD SKQAYEIFKR WLPVDIYIGG QEHAVLHLLY
     ARFWHKFLHQ INVVPNKEPF YKIINQGMIL VNGEKMSKSK GNVVNPSDFV VSHGADALRL
     YMMFMGPITA SLPWEESGID GMYKWVQRVY RLFETKQIDK NFNDENLEKK YHQFVKKASE
     FMENFDFNLV ISEMMIFINE CYKYEKINYD YMLNFCVILS CFAPFITEEI NEVFLKNKKF
     ISDNLWPKYD EKKIVETTIK IPVQINGKIR EVLEINLGAT QKDVVDLAIK NEKIIKWIEN
     KKIVKEIYIE NKILNLIIK