ID   SYL_ROSS1               Reviewed;         904 AA.
AC   A5V1W3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=RoseRS_4535;
OS   Roseiflexus sp. (strain RS-1).
OC   Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Roseiflexineae;
OC   Roseiflexaceae; Roseiflexus.
OX   NCBI_TaxID=357808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Bryant D.A., Richardson P.;
RT   "Complete sequence of Roseiflexus sp. RS-1.";
RL   Submitted (APR-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; CP000686; ABQ92866.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5V1W3; -.
DR   SMR; A5V1W3; -.
DR   STRING; 357808.RoseRS_4535; -.
DR   PRIDE; A5V1W3; -.
DR   EnsemblBacteria; ABQ92866; ABQ92866; RoseRS_4535.
DR   KEGG; rrs:RoseRS_4535; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_0; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000006554; 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   Gene3D; 3.90.740.10; -; 1.
DR   HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
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; 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; 2.
DR   Pfam; PF13603; tRNA-synt_1_2; 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; Reference proteome.
FT   CHAIN           1..904
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334807"
FT   MOTIF           49..59
FT                   /note="'HIGH' region"
FT   MOTIF           663..667
FT                   /note="'KMSKS' region"
FT   BINDING         666
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   904 AA;  101693 MW;  D820E78E06A50E46 CRC64;
     MSETGAKRRM DRFDPSIEPK WREFWAREGI FKAGRRAGAP RRYILEMFPY PSGDLHIGHL
     KNYVIGDALT RYYVIRGYDV LHPFGWDAFG LPAENAAIKY GRHPREWTYS NIAESKKSLE
     IAGIMYDWSR EVTTCNPDYY RWNQWLFLLL YRKGLAYRAK ATVNWDPVDQ TVLANEQVDA
     EGRSWRSGAK VEKRELEQWF FRITAYAERL LNDLDKLDRW PENVKTMQRN WIGRSEGAEV
     TFLALPPGAD LYAPPPPDAE PLVVFTTRPD TLWGATFMVL APEHPLAPKL TAPERRAEVE
     AYIARARMES EIERTSATRE KSGVFLGSYA INPVNDERIP IWIADYVLMG YGTGAIMAVP
     AHDQRDFEFA RQFGLPVRVV VQPPGETLDG DTMTEAWPGD GVMVNSGPIN GIPVGKGEGQ
     SVKAAIAWLE AQGKGKGTVT YRLRDWLISR QRYWGTPIPM LHLPDGTIKP VPEDQLPVLL
     PEVQDYLPKG KSPLAAAEHW VNTIDPETGQ PARRDTDTMD TFVDSSWYFL RFCDAQNDRE
     IFSREAARQW MPVDQYIGGV EHAILHLLYA RFITKVLYDE GLVPEDEPFK ALFTQGMVQR
     RVRTPLDIVA PGMVRFPEEL RRKLELPAEA QTVDQARALL KERGYTLEEE SDGGLTAVSG
     PVTMSKSAGN GIPVGPFVRQ YGSDVARIVV LFAAPPENSM EWTDEGVAGA QRFLNRIVAL
     FGPDRDEIAA MVRSGNGAAP EGEDRALYRK LHETIRKVTL DTEQFRFNTA IAALMELLNE
     ASRYRAEVGR VTPVFAQTAA TFARLLSPFA PHLAEEVHSW CGGTGSVYDA GWPEWDESAL
     VLDEVEIVLQ VNGKLRGKIM APAGADEEQL REWALTNPRV LSFVGDKTVR KVIVVPGKLV
     NVVV