ID   SYL_MYCS2               Reviewed;         953 AA.
AC   A0R7H5; I7FPE6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 120.
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=MSMEG_6917, MSMEI_6729;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
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; CP000480; ABK71384.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP43155.1; -; Genomic_DNA.
DR   RefSeq; WP_011731626.1; NZ_SIJM01000001.1.
DR   RefSeq; YP_891113.1; NC_008596.1.
DR   AlphaFoldDB; A0R7H5; -.
DR   SMR; A0R7H5; -.
DR   STRING; 246196.MSMEG_6917; -.
DR   PaxDb; 246196-MSMEI_6729; -.
DR   GeneID; 66738167; -.
DR   KEGG; msg:MSMEI_6729; -.
DR   KEGG; msm:MSMEG_6917; -.
DR   PATRIC; fig|246196.19.peg.6734; -.
DR   eggNOG; COG0495; Bacteria.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; 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; cd07958; Anticodon_Ia_Leu_BEm; 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; 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; 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..953
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334775"
FT   MOTIF           71..82
FT                   /note="'HIGH' region"
FT   MOTIF           725..729
FT                   /note="'KMSKS' region"
FT   BINDING         728
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   953 AA;  106556 MW;  FE42D3FF49C6681C CRC64;
     MTEPATTPTT PDEQIPRHRY NADLAGQIER AWQETWSDRG TFNVANPVGS LAPTDGSDVP
     ADKMFVQDMF PYPSGDGLHV GHPLGYIATD VYARYYRMLG RNVLHALGFD AFGLPAEQYA
     VQTGTHPRTR TEANIVNFRR QLGRLGLGHD TRRSFSTTDV DYYKWTQWIF LQIYNAWFDR
     DQNKARRISE LVEEFESGKR TLDDGRNWAD LSKGERADVI DGYRLVYRAD SMVNWCPGLG
     TVLANEEVTS EGRSDRGNFP VFRKRLRQWM MRITAYSDRL LEDLDVLDWP EKVKTMQRNW
     IGRSTGASVL FATAADDIEV FTTRPDTLFG ATYLVLAPEH DLVDTLVTDA WPDGTDERWT
     YGAATPREAV AAYRTDIAAK SDLERQENKT KTGVFLGAYA TNPADGKQVP IFIADYVLAG
     YGTGAIMAVP GGDQRDWDFA KEFGLPIIEV VTGGDISEAA YAGDGTMVNS GFLDGMDVAS
     AKEAIIARLE ADGRGKRRVE YKLRDWLFAR QRYWGEPFPI VYDADGRAHP LPESALPVEL
     PDVPDYSPVL FDPDDADSEP SPPLNKATEW VHVELDLGDG LQSYTRDTNV MPQWAGSSWY
     ELRYTDPHNP DEMCAKENEA YWMGPRPDEH GPEDPGGVDL YVGGVEHAVL HLLYSRFWHK
     VLYDLGYVSS REPYRRLVNQ GYIQAFAYTD SRGTYVPAAE VIERDGKFFW PGPDGEIEVN
     QEFGKIGKSL KNSVSPDEIC DNYGADTLRV YEMSMGPLEA SRPWATKDVV GAHRFLQRVW
     RVVIDETSGN VRVVEHEALS DETLRLLHRT IEGVREDYAA LRNNTAAAKL IEYTNHLTKE
     GVAARAAIEP LVLMVAPLAP HLAEELWKRL GHDTSLAHGP FPEADPQYLV EDTIEFPVQV
     NGKVRGKIVV AADADKAALE AAALADEKVQ AFLAGATPKK VIVVPGRLVN LVV
//