ID   SYL_SALAI               Reviewed;         952 AA.
AC   A8LX93;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=Sare_3451;
OS   Salinispora arenicola (strain CNS-205).
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Salinispora.
OX   NCBI_TaxID=391037;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNS-205;
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., Foster B., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., Penn K., Jenkins C.,
RA   Udwary D., Xiang L., Gontang E., Richardson P.;
RT   "Complete sequence of Salinispora arenicola CNS-205.";
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; CP000850; ABV99253.1; -; Genomic_DNA.
DR   RefSeq; WP_012183545.1; NC_009953.1.
DR   AlphaFoldDB; A8LX93; -.
DR   SMR; A8LX93; -.
DR   STRING; 391037.Sare_3451; -.
DR   EnsemblBacteria; ABV99253; ABV99253; Sare_3451.
DR   GeneID; 5708200; -.
DR   KEGG; saq:Sare_3451; -.
DR   PATRIC; fig|391037.6.peg.3479; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_11; -.
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; -; 3.
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; IPR006605; G2_nidogen/fibulin_G2F.
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..952
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334810"
FT   MOTIF           65..76
FT                   /note="'HIGH' region"
FT   MOTIF           727..731
FT                   /note="'KMSKS' region"
FT   BINDING         730
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   952 AA;  106026 MW;  37BD1C3CAC796EE6 CRC64;
     MTEAAASDIP PFRYTAALAD EIERRWQDIW EREGTFHAPN PTGPLADPEH PRAGAEKLYV
     LDMFPYPSGA GLHVGHPLGY IGTDCFARYQ RMAGRNVLHA MGFDAFGLPA EQYAVQTGTH
     PRTTTEANIA RYKAQLRRLG LAHDERRSVA TIDADFYRWT QWVFLQIYNA WYDREAKRAR
     PIAELIAEFS GGVRRTPDGR PWRELTDVER RSVVDEYRLA YVSQAPVNWC PGLGTVLANE
     EVTADGRSER GNFPVFKRNL KQWMMRITAY GDRLLDDLDK LDWPEPIKLM QRNWIGRSIG
     AHIEFPTSAG DSSAVGEPRI NVFTTRPDTI FGATYLVLAP EHALVDDLVP TAWPSGTRDA
     WTGGQASPRA AVAGYRKVAA AKTDMERQAE TKEKTGVFIG AYATNPVTGA QIPIFIADYV
     LAGYGTGAIM AVPGQDERDW AFAEVFDLPI VRTVRPAEGF DGKAYTGEGP AINSAAPERG
     LNLDGLGVAE AKARTTAWLE ASGHGSGAVT YRLRDWLFSR QRYWGEPFPI VYDETGAAIA
     LPEDMLPVEL PEVDDFSPRT FDPADAGSNP ETPLSRRRDW VEVELDLGDG PKRYTRETNV
     MPQWAGSCWY ELRYLDPTNA DRFVDPDTER YWMGPRGEGD CGGTDLYVGG AEHAVLHLLY
     ARFWHKVLYD LGHVSSFEPF RKLFNQGYIQ AYAYTDARGA YVPAEEVVER SGAYYLGDVE
     VSREYGKMGK SLRNVVTPDE MCAAYGADTF RVYEMSMGPL EVSRPWETRA VVGSFRFLQR
     VWRAIVDERS GASRVVDAPA DEATRRLLHR IVDGVRGDME AMRFNTSVAK LIELTNALTR
     LPATPREVAE PLVLMVAPFA PHVAEELWRR MGHPTSLAYA DFPVADPDLL VAESVTYPVQ
     VNGKVRGRVQ VPADASEEVV RAAALDAVAT ALEGREPRKV IVVPGRMVSV VR