ID   SYL_CHLPB               Reviewed;         806 AA.
AC   B3EMN5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=Cphamn1_0551;
OS   Chlorobium phaeobacteroides (strain BS1).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=331678;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BS1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Ovchinnikova G., Li T., Liu Z., Zhao F.,
RA   Overmann J., Bryant D.A., Richardson P.;
RT   "Complete sequence of Chlorobium phaeobacteroides BS1.";
RL   Submitted (JUN-2008) 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; CP001101; ACE03513.1; -; Genomic_DNA.
DR   RefSeq; WP_012474004.1; NC_010831.1.
DR   AlphaFoldDB; B3EMN5; -.
DR   SMR; B3EMN5; -.
DR   STRING; 331678.Cphamn1_0551; -.
DR   KEGG; cpb:Cphamn1_0551; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_10; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
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; 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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..806
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091304"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           576..580
FT                   /note="'KMSKS' region"
FT   BINDING         579
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   806 AA;  91859 MW;  10EA7B28DBCFAFC7 CRC64;
     MRYDFQSIEK KWQAYWNEHQ TFLTKETVDK PKYYVLDMFP YPSGSGLHVG HLEGYTATDI
     ISRYKRSRGH NVLHPMGWDA FGLPAEQFAI KTGTHPKVIT EKNVSSFKDT LMRMGFSYDW
     NREINTTDPG YYAWTQWIFL QLLDRGLAYT SEIDVNWCEE LKTVLANEEV AEKVADGHAV
     VRKPLRQWVL KITAYAERLL SDLDLVDWPE SVKQMQRNWI GRSEGVEIDF QLPCHRTSLK
     VYTTRPDTLF GATYLVISPE HPMAEKLATA EHLIEAKNYI EEAKRKTELE RTGLQKEKTG
     VFTGSFAVNP ANGQALPVWI SDFVLTSYGT GAIMSVPAHD GRDWEFAKKF DLPIVEVIKS
     PHDVEEAVFE EKGSVCINSS NDDISLDGLP FETSFGVMAD WLEKKGTGKR TVKYKLRDWI
     FSRQRYWGEP IPVKYYEDGT LRPESDLPLT LPDIEAYEPT TTGESPLANI SEWLYGTDEN
     GSFRRETNTM PQWAGSCWYY LRFIDPGNTE KPVDPKKEQY WMNVDLYVGG AEHAVLHLLY
     ARFWHKVLFD LGVVSTKEPF QKLFNQGMIL GEDNEKMSKS RGNVIPADQV LGSYGADAVR
     LYEMFLGPLE QVKPWNTNGI EGVSRFLSRV WRLIYPEPGS MAELNEAPLT EDLTRTMHKA
     VKKITDHTEQ LKFNTAISEM MVFVNELHKS GSRNRTAVET LLLLLSPYAP HICEELWEAI
     GHDTSITEEN WPLFDPALAA DNEVTIAVQV NGKLRGTVTA PAGSPKNILL DSARKEESVR
     KFLDGMSIIK EVVVPDRLVN FVVKPG