ID   SYL_PORGI               Reviewed;         925 AA.
AC   Q7MW49;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 127.
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=PG_0796;
OS   Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=242619;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-308 / W83;
RX   PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA   Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA   Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA   Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA   Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA   Fraser C.M.;
RT   "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT   gingivalis strain W83.";
RL   J. Bacteriol. 185:5591-5601(2003).
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; AE015924; AAQ65957.1; -; Genomic_DNA.
DR   RefSeq; WP_005873926.1; NC_002950.2.
DR   AlphaFoldDB; Q7MW49; -.
DR   SMR; Q7MW49; -.
DR   STRING; 242619.PG_0796; -.
DR   EnsemblBacteria; AAQ65957; AAQ65957; PG_0796.
DR   KEGG; pgi:PG_0796; -.
DR   PATRIC; fig|242619.8.peg.731; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_10; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   BioCyc; PGIN242619:G1G02-734-MON; -.
DR   Proteomes; UP000000588; 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; -; 3.
DR   HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
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; Reference proteome.
FT   CHAIN           1..925
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152062"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           700..704
FT                   /note="'KMSKS' region"
FT   BINDING         703
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   925 AA;  106106 MW;  E068D5CE1CC249A2 CRC64;
     MEYNFQEIEK RVQGQWRKDK VYRVAEDTSK KPFYVLDMFP YPSGAGLHVG HPLGYIASDI
     FSRYKRLRGF NVLHPMGYDA FGLPAEQYAI QTGQHPEKTT EENTARYREQ LDKIGFSYDW
     EREIRTCDPN YYKWTQWAFL KMFDSYYCNQ AQQARPISEL IEVFARQGND GLNVACGEGV
     RFTAEEWTAM SEKEQQEILM NYRLAYLGDT MVNWCPALGT VLANDEVKDG VSERGGHPVE
     QKKMRQWCLR VSAYAERLLH DLETLDWTES LKETQRNWIG RSEGAEMEFR LAGKDCTFTI
     FTTRADTIFG VTFMVLAPES ELVEEVTTEE QRAAVETYLT ETKRRTERER ISDKRVSGVF
     SGSYAINPLT GKEIPIWISD YVLAGYGTGA IMAVPAHDTR DFAFARHFDL PIVQVVVPEG
     EPATDPATWE DAKDSKSGIM VNSDFLNGLS VEDAIAQTKE YIREKHLGCV KVNYRLRDAI
     FSRQRYWGEP FPIYYKEGMP HALDEDRLPL RLPEVDKFLP TESGEPPLGR ATGWHTAEGY
     PYELSTMPGF AGSSAYYLRY MDPQNDTALV SRSANEYWRH VDLYIGGTEH ATGHLIYSRF
     WNKFLFDLGI VCEAEPFRKL VNQGMIQGRS NFVYRIKNTN TFVSYGLREQ YEVTPLHVDV
     NIVSNDQLDI DRFRAWRPEY TSAEFILEDG KYICGWAIEK MSKSMFNVVN PDDIIARYGA
     DTLRLYEMFL GPLEQSKPWD TNGIDGVHRF LKKFWALYYN TDGIRVTDTA PTKEELKSLH
     KLIKKVGQDI ESFSFNTSIP AFMICVNELT AAKTTSRAIL CPLLTVLSPF APHITEWLWQ
     ELGVEGSIVT ATWPEYNEEY LVESCVRYPV SFNGKVRFNI ELPADMSKED VEQAALIAPE
     AARWLEGKSP KKVIVVPGRI VNVVV