ID   SYL_HERA2               Reviewed;         814 AA.
AC   A9AZ11;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=Haur_4419;
OS   Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785 / 114-95).
OC   Bacteria; Chloroflexi; Chloroflexia; Herpetosiphonales; Herpetosiphonaceae;
OC   Herpetosiphon.
OX   NCBI_TaxID=316274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23779 / DSM 785 / 114-95;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of chromosome of Herpetosiphon aurantiacus ATCC 23779.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000875; ABX07051.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9AZ11; -.
DR   SMR; A9AZ11; -.
DR   STRING; 316274.Haur_4419; -.
DR   EnsemblBacteria; ABX07051; ABX07051; Haur_4419.
DR   KEGG; hau:Haur_4419; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_0; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000000787; 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; 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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..814
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000199210"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           582..586
FT                   /note="'KMSKS' region"
FT   BINDING         585
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   814 AA;  92643 MW;  18C920705770E083 CRC64;
     MATRYDSSIT EPKWRERWER DGIYRFEPDS DKPKHYAVTM LPYPSGNLHI GHWYAMSPSD
     VHARYMRMRG YNVFFPMGFD AFGLPAENAA IKNNLDPRKW TYSNIEYMRG QLQSMGMMVD
     WDQQIVSADP EYYRWNQWFF IQFFKRGLAY KKFSAVDWCP KCNTTLAREQ VVGDERRCER
     CDSLVTKRDL DQWYFKITSY ADELLNFSEL DWPERITTMQ RNWIGRSEGA EISFKSEAGD
     PITVFSTRPD TLWGATFMVL APEHPLVAKL TSAEQKASVD AYVAEAIRKT EVERQSTDDE
     KPKTGVWIGA YAINPASQER VPIWIADYVL MTYGTGAIMA VPGHDERDFA FAKTFGLAIK
     RVVTQSEQTA ETPLEAAEPA YGTVVNSGQI DGLSSAEAKE AVINWLEAEQ LGKRAINYRL
     RDWLVSRQRY WGTPIPMIYC PTCGTVPVPE DQLPLLLPDS VDFKPTGESP LKLHPTWRFT
     TCPTCGGEAE RDTDTMDTFV DSSWYQVRYL SPHETNAPFT KAIADKWLPV DQYTGGREHA
     VMHLLYTRFW WKAMRDMGLV SANEPMTRLI NQGVILGEDS NKMSKSRGNV IDPDMLVAQY
     GADTVRTFLM FIGPWEQGGP WNNRGIEGCV RFLDRAWRVV TDTPQRHDAV GDASTLERQT
     HRIIKKVGDD LQRFAFNTAI AGLMEFVNEL MKVRETDVYG TTTWRKATET LTLLLAPIAP
     HIAEELWEFL GNSQSVHLQA WPSYDETLLI DESIELPVQI NGKVRGKIQV AATADEPSII
     ATALADEKIA PLVAGKTIVK QIVVPNRLVN IVIK