ID   SYL_PETMO               Reviewed;         828 AA.
AC   A9BF22;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 102.
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=Pmob_0344;
OS   Petrotoga mobilis (strain DSM 10674 / SJ95).
OC   Bacteria; Thermotogota; Thermotogae; Petrotogales; Petrotogaceae;
OC   Petrotoga.
OX   NCBI_TaxID=403833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10674 / SJ95;
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., Meincke L., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Noll K., Richardson P.;
RT   "Complete sequence of Petroga mobilis SJ95.";
RL   Submitted (NOV-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; CP000879; ABX31086.1; -; Genomic_DNA.
DR   RefSeq; WP_012208193.1; NC_010003.1.
DR   AlphaFoldDB; A9BF22; -.
DR   SMR; A9BF22; -.
DR   STRING; 403833.Pmob_0344; -.
DR   KEGG; pmo:Pmob_0344; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_0; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000000789; 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   CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
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   NCBIfam; TIGR00396; leuS_bact; 1.
DR   PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF13603; tRNA-synt_1_2; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 2.
DR   PRINTS; PR00985; TRNASYNTHLEU.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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..828
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000199217"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           582..586
FT                   /note="'KMSKS' region"
FT   BINDING         585
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   828 AA;  96100 MW;  F65300E294F9C3E0 CRC64;
     MEKTYNPQEI ERKWQRNWQE KDAFKVSNEE YHKKYYDLVM FPYPSGTLHV GHVKNYVIGD
     VIARYKRMRG YNVMHPFGFD AFGLPAENAA IEKGNIHPED WTMQNINIIR NQIKKLGISY
     NWEREVITCK EDYYKWTQWI FLQLYKNGLA YKKKAPVNWC PNCKTVLANE QVVNGKCERC
     GTVVEIKQLE QWYFKITDYA EKLLYDLEKL SGWPENVKIM QKNWIGKSVG AEVEFNLDNG
     KGSLRVFTTR PDTLWGVTFM ALAPESPLVE ELTTPENSEK VNQFLQRVSL QDRFKRTAEG
     AEKEGVFTGS YAINPVNGEK IPIYVANYIL YEYGTGAIMA VPAHDQRDFE FAKKYDLPIR
     IVIMPEGDEL TEENLEKAYI GEGVLVNSGE FTGLDNQTAI REVSQWLEDK KIGKVVTQYK
     LRDWLISRQR YWGAPIPVVY CEKCGVVPVP EKDLPVKLPR DVAFEPTGKS PLIDHPDFKE
     TTCPKCGGKA KREVDTMDTF VDSSWYYLRY VNPKLEDKPF NKEDVDNWLP VDQYIGGVEH
     AILHLLYSRF ITKVLKDLGY VSFDEPFKNL FTQGMIYRNG AKMSKSKGNV VSPEEMIEKY
     GTDALRTYIL FMAPPERDAE WNDSGIEGTY RFLNKVWNTY MKIQDKIIHL ENKPNYPLKN
     KSEKDLRRKL HQTIEKITSD IEGNFQFNTA VSSLMELLNE LNSYLNNTDD KDWNLNLLKE
     FSEDFVLMLS PIAPHISEEL WKNFGKDEFI FKASWPEIDK NALKAEEITL AVQINGKLRA
     QITVDVSLNE DEVKSYALED DKVQKYISGK KIQKIIYVPK KIINIVVK
//