ID   SYL_ACHLI               Reviewed;         803 AA.
AC   A9NET8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=ACL_0242;
OS   Acholeplasma laidlawii (strain PG-8A).
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC   Acholeplasma.
OX   NCBI_TaxID=441768;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG-8A;
RX   PubMed=21784942; DOI=10.1128/jb.05059-11;
RA   Lazarev V.N., Levitskii S.A., Basovskii Y.I., Chukin M.M., Akopian T.A.,
RA   Vereshchagin V.V., Kostrjukova E.S., Kovaleva G.Y., Kazanov M.D.,
RA   Malko D.B., Vitreschak A.G., Sernova N.V., Gelfand M.S., Demina I.A.,
RA   Serebryakova M.V., Galyamina M.A., Vtyurin N.N., Rogov S.I., Alexeev D.G.,
RA   Ladygina V.G., Govorun V.M.;
RT   "Complete genome and proteome of Acholeplasma laidlawii.";
RL   J. Bacteriol. 193:4943-4953(2011).
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; CP000896; ABX80868.1; -; Genomic_DNA.
DR   RefSeq; WP_012242199.1; NC_010163.1.
DR   AlphaFoldDB; A9NET8; -.
DR   SMR; A9NET8; -.
DR   STRING; 441768.ACL_0242; -.
DR   EnsemblBacteria; ABX80868; ABX80868; ACL_0242.
DR   GeneID; 66293237; -.
DR   KEGG; acl:ACL_0242; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_14; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000008558; 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; 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; 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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..803
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334722"
FT   MOTIF           41..52
FT                   /note="'HIGH' region"
FT   MOTIF           581..585
FT                   /note="'KMSKS' region"
FT   BINDING         584
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   803 AA;  92810 MW;  4542359C0C2E5190 CRC64;
     MHKYEHRKIE EKWQKHWLDN KLFKTKNDRF HQKYYVLDMF PYPSASGLHV GHIEGYTATD
     IVSRFKRMQG YNVLHPMGWD AYGLPSEQYA LATGKDPKSF TYQNISNFKR QIIEMGKGVD
     WDKELATTDP EYFKWTQWIF KRLYEKGLAV LKDVEVNWCE GLGTVLANDE IEIINGQMVS
     ERGHYPVIKK PMRQWVLRIT EYADRLLDDL ALVDWPENLK EMQRNWIGKS SGAVIEFEVA
     STDYKFEIFT TRPDTIYGVT YCVLSPEHPL VEKIVTQDEE KDVLRYIEQT KMKSDLDRIA
     DKSKTGVFTG AFAKHPLTNQ LIPIWIGDYV LPQYGMGAVM AVPAHDDRDY EFAMQYGLNI
     IEVIKGGSEG AYTGDGIHHH SGIIDGLYNE EAIEKITKHL EDRKKGYKHY TYKLRDWVFS
     RQRYWGEPFP VIYDEDGQIH LVPDDELPLE LPYLEFIKPS GTGESPLANA RDWLYVDING
     KKGRRDTNTM PQLAGSSWYY IGYILKSNLG YIPLDSKEAK AVLDQFLPVD LYVGGTEHAV
     GHLLYARFWH KFFYDLGFVS SKEPFMKLVN QGMILGADHS KMSKSKGNSV SPDDFIQSHG
     ADALRLFEMF MGPLEAEKPW SNEGLEGAKR FLDRVWRMFD FEITQQPVDA LQTVYHQTVK
     KVTEDYEKLA FNTAISQMMI FVNEVYKTKV IGAAQARGFL KLLNPIAPHL TEEINETVLK
     HHEDLVYSEW PTYDESFLIE TEVEVAIQVN GKLRGRLQVK KDMVEEDLKK LALEHENVIK
     HVEGLTIVKV IVIPNKIVNI VVR