ID   SYL_STRMK               Reviewed;         880 AA.
AC   B2FPR7;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=Smlt3485;
OS   Stenotrophomonas maltophilia (strain K279a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=522373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K279a;
RX   PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA   Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA   Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA   Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA   Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA   Parkhill J., Thomson N.R., Avison M.B.;
RT   "The complete genome, comparative and functional analysis of
RT   Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT   resistance determinants.";
RL   Genome Biol. 9:R74.1-R74.13(2008).
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; AM743169; CAQ46908.1; -; Genomic_DNA.
DR   RefSeq; WP_012480931.1; NC_010943.1.
DR   AlphaFoldDB; B2FPR7; -.
DR   SMR; B2FPR7; -.
DR   STRING; 522373.Smlt3485; -.
DR   PRIDE; B2FPR7; -.
DR   EnsemblBacteria; CAQ46908; CAQ46908; Smlt3485.
DR   KEGG; sml:Smlt3485; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000008840; 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; 3.
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..880
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091368"
FT   MOTIF           46..56
FT                   /note="'HIGH' region"
FT   MOTIF           638..642
FT                   /note="'KMSKS' region"
FT   BINDING         641
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   880 AA;  98446 MW;  F27102B3E388C6A6 CRC64;
     MTSAETNAYD PQQVESAAQK YWDATRAFEV DETSDKPKYY CLSMLPYPSG ALHMGHVRNY
     TIGDVISRYK RMTGHNVLQP MGWDAFGLPA ENAAIKNKTA PAAWTYKNIE HMRGQFKAMG
     YAVDWSREFA TCRPDYYVHE QRMFTRLMRK GLAYRRNAVV NWDPVDQTVL ANEQVIDGRG
     WRSGALVEKR EIPQWFLRIT DYAQELLDGL DELDGWPDSV KTMQRNWIGR SEGLEIQFDV
     RDVDGTALDP LRVFTTRPDT VMGVTFVSIA AEHPLALHAA KNNPELAALL SEMKQGGVSE
     AELETQEKRG MDTGLRAIHP VTGEKVPVWV ANFVLMGYGT GAVMAVPGHD QRDNEVANKY
     GLPIKQVIAL KDPRNDDERT WDGARWQDWY SDKNRAFELV NSAEFDGLDF QGAFEALAER
     FERKAQGQRR VNYRLRDWGV SRQRYWGCPI PVIYCDKCGA VPVPEEQLPV VLPEDVAFSG
     TGSPIKTDPE WRKTTCPECG GAAERETDTF DTFMESSWYY ARYTSPGARD AVDKRGNYWL
     PVDQYIGGIE HAILHLMYFR FYHKLLRDAR MVDSNEPARN LLCQGMVIAE TYYRPNPDGS
     KDWINPADVE VQRDERGRIT GATLIADGQP VVVGGTEKMS KSKNNGVDPQ AMVDKYGADT
     VRLFSMFAAP PEQSLEWNEA GVDGMARFLR RLWAQVQKHA ADGAAPALDV AALDANQKAL
     RRKTHETIGK VGDDYGRRHS FNTAIAAVME LMNALAKFED GSEQGRAVRQ EALQAIVLLL
     NPITPHASHA LWQVLGHGET LLEDQPFPQA DAGALVRDAL TLAVQVNGKL RGTIEVAADA
     AREQVEALAL AEPNAAKFME GLTVRKIIIV PGKIVNIVAA