ID   SYL_MARMM               Reviewed;         865 AA.
AC   Q0AKF5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=Mmar10_2957;
OS   Maricaulis maris (strain MCS10).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Maricaulales; Maricaulaceae;
OC   Maricaulis.
OX   NCBI_TaxID=394221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCS10;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Viollier P.,
RA   Stephens C., Richardson P.;
RT   "Complete sequence of Maricaulis maris MCS10.";
RL   Submitted (AUG-2006) 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; CP000449; ABI67238.1; -; Genomic_DNA.
DR   RefSeq; WP_011644882.1; NC_008347.1.
DR   AlphaFoldDB; Q0AKF5; -.
DR   SMR; Q0AKF5; -.
DR   STRING; 394221.Mmar10_2957; -.
DR   EnsemblBacteria; ABI67238; ABI67238; Mmar10_2957.
DR   KEGG; mmr:Mmar10_2957; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001964; 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; 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; Reference proteome.
FT   CHAIN           1..865
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009368"
FT   MOTIF           44..54
FT                   /note="'HIGH' region"
FT   MOTIF           625..629
FT                   /note="'KMSKS' region"
FT   BINDING         628
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   865 AA;  95991 MW;  BD003E6FD3A8A8E8 CRC64;
     MTRYNPREAE PKWQSAWDAC DAFKAIGPSA SNNKPKYYVL EMFPYPSGRI HVGHSRNYTM
     GDVVARYKRA RGFDVLHPMG WDAFGLPAEN AARDRGVHPG AWTHDNIDAM RGQLQRLGLA
     LDWSREIATC DPSYYRHQQA IFLRLMERGL LHRKTAKVNW DPVDQTVLAN EQVIDGRGWR
     SGALVVQREL DQWFFKITEY ADELTDALEE LDRWPDKVRT MQSNWIGRSR GAEVSFPLTD
     SGLAEQFGAT IDVFTTRPDT LFGASFLALA PDHPIVKALA ADDPEIDRFM HECARMGTTA
     EEIEKAPKRG VDLGITVRHP FDENWELPVW SANFVLSGYG TGAIFGSPAG DQRDLDFARK
     YDLAVQPVVL PPEASADTHV IEDEAYTGPG TSYNSRFLDG LSTADALERA ITELEARKLG
     KGATSYRLRD WLVSRQRYWG CPIPVIHCAD CGVVPVPEDQ LPVVLPEDVT FDHPSNPLER
     HPTWKNADCP KCGKAGRRET DTLDTFVCSS WYFLRFTSPW SEDTPFLASD AEHWMPVDQY
     VGGIEHAILH LLYARFFTRA LNDAGLMNMK SGEPFAGLFT QGMVTHETYK SADGKWLSPE
     EVDLRKDGAV EMSTGKPVSV GAIEKMSKSK KNVVDLDAFI ESYGADAVRW FVLSDSPPER
     DVEYTDSGVE GVWRFVQRLW STVTSLPEGA PGPLTVAADA SGPALEIRRA AHKALHAVTD
     AIEGFRFNSA VAQVHDLVNV LRKYVPSDDA GIAAKTEALG ILARIIAPFV PHLAEECWEH
     LGGEGLVIDA AWPEADPALL VEDSVTLPVQ VNGKRRTEVT APKGAAQDVV QEMVMADQTV
     QRALEGLTVR KVIVVPDRIV NIVAG