ID   SYL_ORITB               Reviewed;         838 AA.
AC   A5CCT4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-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}; OrderedLocusNames=OTBS_0468;
OS   Orientia tsutsugamushi (strain Boryong) (Rickettsia tsutsugamushi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Orientia.
OX   NCBI_TaxID=357244;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Boryong;
RX   PubMed=17483455; DOI=10.1073/pnas.0611553104;
RA   Cho N.-H., Kim H.-R., Lee J.-H., Kim S.-Y., Kim J., Cha S., Kim S.-Y.,
RA   Darby A.C., Fuxelius H.-H., Yin J., Kim J.H., Kim J., Lee S.J., Koh Y.-S.,
RA   Jang W.-J., Park K.-H., Andersson S.G.E., Choi M.-S., Kim I.-S.;
RT   "The Orientia tsutsugamushi genome reveals massive proliferation of
RT   conjugative type IV secretion system and host-cell interaction genes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:7981-7986(2007).
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; AM494475; CAM79534.1; -; Genomic_DNA.
DR   RefSeq; WP_011944500.1; NC_009488.1.
DR   AlphaFoldDB; A5CCT4; -.
DR   SMR; A5CCT4; -.
DR   EnsemblBacteria; CAM79534; CAM79534; OTBS_0468.
DR   KEGG; ots:OTBS_0468; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000001565; 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; 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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..838
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334786"
FT   MOTIF           38..48
FT                   /note="'HIGH' region"
FT   MOTIF           608..612
FT                   /note="'KMSKS' region"
FT   BINDING         611
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   838 AA;  96655 MW;  F8757CA6ACA4175C CRC64;
     MNLVKIEKKW QKIWEQNEVF KVKEILNKIK RYILPMFPYP SGKAHVGHVR NYTICDVIAR
     FERSQGHNVL HAMGWDAFGL PAENAAMQNN TYPNSWVSSN VDVMRQQLKA IGLSYDWSRE
     IITCSSQYYV HEQRFFLEML KKGLVYQKES LVNWDPIDQT VLANEQVING KGWRSGAIIE
     YRNLKQWFIK ITNYADALLK GLDSLKGWPE SVKTMQKKWI GQSTGININF QLKGIEASVK
     VFSTRPETLF GASFIALSYN HNLVQQYVNT TPETQKFIDK CSNVGTSNVN IDKMKIAVLT
     NLKVIHPLNS SIELPVILSN FVLMDYGTGA LFGCPAHDER DHEIAKLLKL NIKQVITSTE
     RNIDVLKEAY VGDGIMINSF HLNGLTTTEA RQKVINELQH KNIGQQVTNY KLKDWGISRQ
     RFWGCPIPII HCKSCGAVPV PYEDLPVILP EHGVEFTGKG NPLDNHHSWK YVKCPKCHLD
     AVRETDTFDT FFESSWYFAR FCNPTSDDMV DAKAAKYWLP VDQYIGGIEH AVMHLLYARF
     ITRVMYDLKY IDIQEPFTSL ITQGMVLHRT YQDKSNNWLY PNEVEVDSNG QLRCKADLQY
     VTVGKLEKMS KSKKNVVDLE LVLKLYGADV ARMFVLSDTP PEKDLEWSTE GIEGCYKFIQ
     KLYNFALKLK NINLTDNKID KVLLSKTHKT IKNVTQDIIS CRLNKAIARL RELYNLIFKM
     SELTVQIKES FLILIRLFNP FIPHLSEEIW SLLSGRGEML VELPWPKYEE KYIHEEEHIT
     IAIQINGKLR SLYNCLIDTP EHDVQSAILK LEQVKKHIGD KEVRKCIFVP NKLINIII