ID   SYL_RICPR               Reviewed;         828 AA.
AC   Q9ZDB1;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 128.
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=RP421;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
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; AJ235271; CAA14878.1; -; Genomic_DNA.
DR   PIR; D71700; D71700.
DR   RefSeq; NP_220802.1; NC_000963.1.
DR   RefSeq; WP_004599464.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZDB1; -.
DR   SMR; Q9ZDB1; -.
DR   STRING; 272947.gene:17555501; -.
DR   EnsemblBacteria; CAA14878; CAA14878; CAA14878.
DR   GeneID; 57569546; -.
DR   KEGG; rpr:RP421; -.
DR   PATRIC; fig|272947.5.peg.434; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000002480; 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; 2.20.28.290; -; 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; 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   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; 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; 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; Reference proteome.
FT   CHAIN           1..828
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152075"
FT   MOTIF           36..46
FT                   /note="'HIGH' region"
FT   MOTIF           595..599
FT                   /note="'KMSKS' region"
FT   BINDING         598
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   828 AA;  96472 MW;  43BACB6398191986 CRC64;
     MHKIEKKWQK IWQEEKAFQV SNESSKPKYY VLEMLPYPSG KIHIGHVRNY SIGDVIARFM
     TMQGFNVLHP MGWDAFGLPA ENAAIKNNSR PQDWTYSNIE YMKKQLQSMG FAYDWTREIN
     SCDPEYYKHE QKFFLELYDR NLVYQKESLV NWDPVDNTVL ANEQVVDGRG WRSGAIIEKR
     YLKQWFLKIT DYAEELLNEI QNLKDWPAAV RVMQEEWIGK STGVNFHFKV KYHENTTIEV
     FSTKPETIFG ASFIGIAFNH PIIEQLICKT PEIVNFITKC SYITRSSEID KAEKEGIFSG
     LYVIHPFDAN IFLPVIITNF VLMDYGTGAI FGCPAHDKRD HELAIKMNLP IKQVIETGNI
     QEGILINSDW LNGLTSSEAK QKVIEKFEKL GIGKRSVNYR LKDWSISRQR FWGCPIPMIH
     CKTCGVVPVP YKDLPVTLPD DVSFDSNYNP LEHHSSWKYV NCPKCDNSAI RETDTFDTFF
     ESSWYFTRYC NSNAVEMTDK KACNYWLPVD KYIGGIEHAV MHLLYARFFT KLMNEHNYVS
     IREPFKGLFT QGMVLHATYK DENNNWLYPA EVVKKGNEFF HKENNTRVVQ GRIEKMSKSK
     KNIIDLETIR EQYSADAIRL FVLSDSPPEK DLEWSASGIE GCSRFINKLE NMFEAIFSLK
     DDMKSEINKD LNRLIHLTIK HVADDIKTFS LNRAIARMRT LTNAIYYEIS KDRIDVRTIK
     YGFNVLVQLL NPFIPHITEE IWQKLGNKER LYKSVFAEFD ESILELSTYI MAVQVNGKLR
     DTYEFDVDIS EDEVKQITVN LPKVQKFLAG KEPRNIILVP RKIVNIIV
//