ID   SYL_XANCB               Reviewed;         885 AA.
AC   B0RR06;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
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};
GN   OrderedLocusNames=xcc-b100_1541;
OS   Xanthomonas campestris pv. campestris (strain B100).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=509169;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B100;
RX   PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA   Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T.,
RA   Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K.,
RA   Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K.,
RA   Puehler A.;
RT   "The genome of Xanthomonas campestris pv. campestris B100 and its use for
RT   the reconstruction of metabolic pathways involved in xanthan
RT   biosynthesis.";
RL   J. Biotechnol. 134:33-45(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAP50891.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AM920689; CAP50891.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; B0RR06; -.
DR   SMR; B0RR06; -.
DR   KEGG; xca:xcc-b100_1541; -.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000001188; 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.
FT   CHAIN           1..885
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334838"
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   885 AA;  99140 MW;  DB659533B2B83BA0 CRC64;
     MSTVEPNAYD PQQVETSAQQ FWDATRAFQV DENSDKPKFY CLSMLPYPSG ALHMGHVRNY
     TISDVVSRYK RMTGHNVLQP MGWDAFGLPA ENAAIKNKTA PAKWTYANIE HMRAQLKSLG
     YAIDWSREFA TCTPDYYVHE QRMFTRLMRK GLAYRRNAVV NWDPIDQTVL ANEQVIDGRG
     WRSGALVEKR EIPQWFLRIT DYAQELLDGL DQLDGWPDSV KTMQRNWIGR SEGLEIQFDV
     RDTTGAALDP LRVFTTRPDT LMGVTFVSIA AEHPLAQHAA KSNPELASML ETLKHGGVSE
     AELETQEKRG MATGLTAVHP ISGEEVPVWV ANFVLMGYGT GAVMAVPGHD QRDFEFANKY
     GLPIVQVVKL REPRNDDEQA WDATQWRDWY TDKSRELELI NSAEFDGLDY HGAFEALAER
     FERKGQGQRR INYRLRDWGV SRQRYWGCPI PVIYCAKCGA VPVPEDQLPV VLPENVEFAG
     TGSPIKTDPT WRQTTCPECG GPAERETDTF DTFMESSWYV ARYTSPNARD MVDRRANYWM
     PADLYVGGIE HAILHLMYFR FYHKLMRDAR LVDSDEPVTN LLTQGMVIAE TFYRDADNGG
     KDWINPADVE IQRDERGRVV GASLIADGQP VHIGGTEKMS KSKNNGVDPQ AMVAKYGADT
     VRLFSMFAAP PEQSLEWNEA GVDGMARFMR RLWVQVHKHV GEGIDDELTK IVALGGPLSA
     EQKAIRRKTH ETIGKVDDDY GRRHSFNTAI AAVMELSNAL AKFDDASAQG RAVRQEALEA
     MVLLLNPITP HASHALWQVL GRGETLLENV PFPQVDAAAL VRDALTLAIQ VNGKLRGTIE
     VAADAAREQI EALALAEPNA AKFLDGLSVR KIIIVPGKIV NIVAG