ID   SYL_PSEU2               Reviewed;         868 AA.
AC   Q4ZN90;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 121.
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=Psyr_4352;
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a;
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT   syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000075; AAY39382.1; -; Genomic_DNA.
DR   RefSeq; WP_011268980.1; NC_007005.1.
DR   RefSeq; YP_237420.1; NC_007005.1.
DR   AlphaFoldDB; Q4ZN90; -.
DR   SMR; Q4ZN90; -.
DR   STRING; 205918.Psyr_4352; -.
DR   EnsemblBacteria; AAY39382; AAY39382; Psyr_4352.
DR   KEGG; psb:Psyr_4352; -.
DR   PATRIC; fig|205918.7.peg.4492; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000000426; 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   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; 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; PF00133; tRNA-synt_1; 2.
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..868
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009401"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           627..631
FT                   /note="'KMSKS' region"
FT   BINDING         630
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   868 AA;  96923 MW;  58F1A797A5E213A8 CRC64;
     MHELYQPREI EAAAQTFWDE QKSFEVSEQP GKDTFYCLSM FPYPSGKLHM GHVRNYTIGD
     VISRYQRMLG KNVLQPLGWD AFGMPAENAA IDNNVAPAKW TYENIDYMKT QLKSLGLAVD
     WSREVTTCKP DYYRWEQWLF TRLFEKGVIY RKNGTVNWDP IDQTVLANEQ VIDGRGWRSG
     ALIEKREIPM YYFKITAYAD ELLESLDELP GWPEQVKTMQ RNWIGRSRGM EVQFPYDQAS
     IGEAGALKVF TTRPDTLMGA TYVAVAAEHP LATLAAQGNP ALQAFIDECK GGSVAEADVA
     TQEKKGQATS LFVEHPLTGE KLPVWVANYV LMHYGDGAVM AVPAHDERDF EFATQYGLPI
     KPVVRTSAGD QTPAPWQPAY GEHGELINSG EFTGLTFQDA FDAIEAALVK KSLGQSRTQF
     RLRDWGISRQ RYWGCPIPIV HCDTCGDVPV PEDQLPVVLP EDVVPDGAGS PLARMPEFYE
     CSCPKCGAPA KRETDTMDTF VESSWYYARY ASPHYEGGLV EPNAANHWLP VDQYIGGIEH
     AILHLLYARF FHKLMRDEGL VTSNEPFKNL LTQGMVNAET YFRMETSGKK TWINPADVTL
     ERDAKAKVIS ARLTSDGLPV EIGGTEKMSK SKKNGIDPQT MIDQYGADTC RLFMMFASPP
     DMSLEWSDSG VEGSHRFLRR VWRLAQAHVT QGPSTGLDVA ALSDEQKAIR RAIHQAIRQA
     SQDIGQNQKF NTAVAQVMTL MNVLEKAPQD TPQDRALMQE GVETVALLLA PITPHISHEL
     WKQLGHNEPV IDAGWPAFDA SALVQDSLQL VIQVNGKLRG HIEMPASASR EEVEAAARVN
     ENVLRFTDGL TIRKVIVVPG KLVNIVAS