ID   SYL_CAMHC               Reviewed;         813 AA.
AC   A7I0M0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=CHAB381_0473;
OS   Campylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 /
OS   CH001A).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360107;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A;
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., Nelson K.E.;
RT   "Complete genome sequence of Campylobacter hominis ATCC BAA-381, a
RT   commensal isolated from the human gastrointestinal tract.";
RL   Submitted (JUL-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; CP000776; ABS52208.1; -; Genomic_DNA.
DR   RefSeq; WP_012108346.1; NC_009714.1.
DR   AlphaFoldDB; A7I0M0; -.
DR   SMR; A7I0M0; -.
DR   STRING; 360107.CHAB381_0473; -.
DR   EnsemblBacteria; ABS52208; ABS52208; CHAB381_0473.
DR   KEGG; cha:CHAB381_0473; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_7; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000002407; 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; 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; 2.
DR   Pfam; PF00133; tRNA-synt_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..813
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334740"
FT   MOTIF           39..49
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   813 AA;  93610 MW;  1022D7D868CF8EEB CRC64;
     MYDSKKLELK WQEIWDKEGI FEPKKDYNLQ KKYILSMFPY PSGRIHMGHV RNYTIGDAIS
     RYYRMQGYNV LQPIGFDSFG MPAENAAIKH KIHPKKWTYD NIDYMTKELF RLGFSFSKNR
     ILATSDPIYT KFEQEFFIKM FEKGLIYRKN AVVNWCEQDQ TVLANEQVED GKCWRCGNEV
     VQKEMPGYYL KITSYADELL SCLKDLQNHW PSQVITMQEN WIGKSFGLEF DFKFDDESSK
     KLGGVKSFKV FTTRPDTIYG MSYAALAPEH AVVKAVLEKN LVSKETADKI KKILNQSPRE
     RQANDKDGAF LNLFAIHPLS GKKIPVWMAN FVLAEYGGGA VMAVPAHDER DFEFAHKFNL
     PIIQSIGAKN GENVKLPYIE SGILVDSAEF SGLENEDAKM KIIEKFEKEK IGKRVTNYKL
     RDWGISRQRY WGAPIPMIKC PKCGLVPEKI KNLPVTLPDD IKITGKGNPL DKHPTWKHCT
     CPKCGAEAER ETDTLDTFFD SSWYFARFTS DENMWQEKGI DEKSANYWMN VDQYIGGIEH
     AILHLLYARF FQKVLRDLGY LRDSEPFANL LTQGMVLKDG AKMSKSKGNV VDPDEIIEKY
     GADTARLFIL FAAPPQKELE WNDSAVEGAY KFLNRLYERS QNVQKTREIP KIDQSSLNKA
     EKYARLKVYE ALQKSSEVYE KTFAFNTLIA ACMEALNALN AQENRQILTE GYFIILNLLD
     PIVPHIACEL SENLFGRANF TPIKILPEVF EKDEIRLAVT VNGKKRAEIE VASDLSQSEI
     LKIAKEQVLK WLENKKIIKE IYIKNKLVNL VVK