ID   SYL_MARN8               Reviewed;         861 AA.
AC   A1U4A0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   03-AUG-2022, entry version 96.
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=Maqu_2744;
OS   Marinobacter nauticus (strain ATCC 700491 / DSM 11845 / VT8) (Marinobacter
OS   aquaeolei).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Marinobacteraceae; Marinobacter.
OX   NCBI_TaxID=351348;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700491 / DSM 11845 / VT8;
RX   PubMed=21335390; DOI=10.1128/aem.01866-10;
RA   Singer E., Webb E.A., Nelson W.C., Heidelberg J.F., Ivanova N., Pati A.,
RA   Edwards K.J.;
RT   "Genomic potential of Marinobacter aquaeolei, a biogeochemical
RT   'opportunitroph'.";
RL   Appl. Environ. Microbiol. 77:2763-2771(2011).
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=ABM19819.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000514; ABM19819.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041656989.1; NC_008740.1.
DR   AlphaFoldDB; A1U4A0; -.
DR   SMR; A1U4A0; -.
DR   STRING; 351348.Maqu_2744; -.
DR   EnsemblBacteria; ABM19819; ABM19819; Maqu_2744.
DR   KEGG; maq:Maqu_2744; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000000998; 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; -; 1.
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..861
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334770"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           620..624
FT                   /note="'KMSKS' region"
FT   BINDING         623
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   861 AA;  97230 MW;  0C308BF782455E9A CRC64;
     MDEQYNPREV EQTARTFWET NETFKVKEEP GKPKYYCLSM FPYPSGKLHM GHVRNYTIGD
     VISRYQRMQG KNVMQPMGWD AFGLPAENAA IANKSAPAKW TRSNIDYMKN QLKQLGFGYD
     WSRELATCDP EYYRWEQWFF ARLYEKGLVY KKMSTVNWDP VDQTVLANEQ VVDGRGWRSG
     ALVEQKKIPQ WFIRITDYAE ELLNDLEDME GWPEQVKTMQ RNWIGKSVGT ELTFPLKEQE
     GGLTVYTTRP DTLMGVSYMA VAAEHPLAKA AAERHRDVAE FVDQCRNSKV AEAELATMEK
     KGIDTGFKAI HPLTQEEIPV WVANFVLMDY GTGALMAVPG HDERDHEFAV KYKLPIKQVI
     APNDSRDIDI QEQAFTEKGV LVSSGKYSGL TSEEAFEEIA DYLEAQGIGK RTVNYRLRDW
     GVSRQRYWGA PIPMMTLEDG TEMPVPDDQL PVRLPEDVEM DGVQSPIKAD PEWCKTEYNG
     QPATLETDTF DTFMESSWYY ARFCSPNYDK GMLDPAAANY WLPVDQYIGG IEHAILHLLY
     ARFFHKLLRD VGLVNSSEPF KRLLTQGMVL AETYYRNEAN GGKTWYNPAD VTVERDGKGQ
     VVRAVLKSDG EPVEIGGVTK MSKSKNNGID PQAIIDQHGA DTVRLFMMFA APPEQSLEWS
     DSGVEGAHRF LKRLWRMVNE HTAGGDAPAV DPANLNGAQK DLRRKTHETI AKVSDDISRR
     LTFNTAIAAV MELLNEVGRL SDDEPQSRAV RQEALDTAVL VLSPIVPHIC HNLWQALGHS
     DAVVDASWPV ADESAMVRSE IEVVLQVNGK VRAKENVPAD IGKADLEKLA LENENVMRFT
     DGKTVRKVIV VPGKLVNVVA N