ID   SYL_CHLAB               Reviewed;         820 AA.
AC   Q5L5Q6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 119.
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=CAB585;
OS   Chlamydia abortus (strain DSM 27085 / S26/3) (Chlamydophila abortus).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=218497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27085 / S26/3;
RX   PubMed=15837807; DOI=10.1101/gr.3684805;
RA   Thomson N.R., Yeats C., Bell K., Holden M.T.G., Bentley S.D.,
RA   Livingstone M., Cerdeno-Tarraga A.-M., Harris B., Doggett J., Ormond D.,
RA   Mungall K., Clarke K., Feltwell T., Hance Z., Sanders M., Quail M.A.,
RA   Price C., Barrell B.G., Parkhill J., Longbottom D.;
RT   "The Chlamydophila abortus genome sequence reveals an array of variable
RT   proteins that contribute to interspecies variation.";
RL   Genome Res. 15:629-640(2005).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR848038; CAH64033.1; -; Genomic_DNA.
DR   RefSeq; WP_011097182.1; NC_004552.2.
DR   AlphaFoldDB; Q5L5Q6; -.
DR   SMR; Q5L5Q6; -.
DR   EnsemblBacteria; CAH64033; CAH64033; CAB585.
DR   KEGG; cab:CAB585; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_0; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001012; 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; 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.
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.
FT   CHAIN           1..820
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009319"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           601..605
FT                   /note="'KMSKS' region"
FT   BINDING         604
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   820 AA;  93863 MW;  8FD3378BD6A2FBF3 CRC64;
     MRYDPSLIEK KWQQFWKEHK SFKADETADK PKYYVLDMFP YPSGAGLHVG HLIGYTATDI
     VARYKRAKGF SVLHPMGWDS FGLPAEQYAV RTGTHPRETT KKNIENFRKQ LSAMGFSYDE
     AREFATSDPE YYRWTQKLFL FLYEKGLAYM ADMAVNYCEE LGTVLANEEV ENGLSIEGGY
     PVERRMLRQW ILRITAYADQ LLQGLEDLDW PENVKQLQRN WIGKSEGALL RFVVDKDKCL
     EVFTTRPDTL CGVSFLVMAP EHPEIQQLVS EEQRSAVESY IRCAQSKSER ERISETKVKS
     GVFTGAYAKH AITGAALPIW VSDYVIMGYG SGVVMGVPAH DERDREFANA FALPIDEVLD
     ENEHCINSNH GDFLLNGLQG KEASDYVIAY LQKRNLGEAK VMYKLHDWLF SRQRYWGEPI
     PIIHFEDGTC RPLEDDELPL LPPEIQDYRP KGFGQGPLAK VKEWVDIHDV KTQRPGRRET
     HTMPQWAGSC WYYLRFCDAH NSQAPWSHEN ERYWMPVDLY IGGAEHAVLH LLYSRFWHRV
     FYEAGLVSTP EPFKKLINQG LVLATSYRIP GKGYVHPEDA REDNGKWTTA SGEELEVRQE
     KMSKSKLNGV DPQILIDEFG ADALRMYAMF SGPLDKNKLW CNQGVSGCRR FLNRFYELAT
     SSAVQDIDDP KGMALAHRLV HKVGEDIEKM SLNTIPSSFM EFINEFAKLD TYSKSALSMV
     VRALAPIAPH ISEELWTVLG YAPGIDNAGW PEVDPKYLED TSVTFVIQVN GKLRARLDMD
     KNTSQEDILS AARESVAKYL EDKEIKKEVF VPNRLVNFVL