ID   SYL_EHRCR               Reviewed;         829 AA.
AC   Q2GG41;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 114.
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=ECH_0794;
OS   Ehrlichia chaffeensis (strain ATCC CRL-10679 / Arkansas).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=205920;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC CRL-10679 / Arkansas;
RX   PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA   Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA   Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA   Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.C.,
RA   Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C.,
RA   Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D.,
RA   Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA   Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT   "Comparative genomics of emerging human ehrlichiosis agents.";
RL   PLoS Genet. 2:208-222(2006).
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; CP000236; ABD45082.1; -; Genomic_DNA.
DR   RefSeq; WP_006011277.1; NC_007799.1.
DR   AlphaFoldDB; Q2GG41; -.
DR   SMR; Q2GG41; -.
DR   STRING; 205920.ECH_0794; -.
DR   KEGG; ech:ECH_0794; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000008320; 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; 3.40.50.620; HUPs; 2.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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   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; 1.
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..829
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334753"
FT   MOTIF           34..44
FT                   /note="'HIGH' region"
FT   MOTIF           591..595
FT                   /note="'KMSKS' region"
FT   BINDING         594
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   829 AA;  94868 MW;  936299A00BE200DA CRC64;
     MHYDFKKVEQ DIQGKWNFYT DAKQAQCYVL EMFPYPSGNI HMGHLRNYTI GDVIARYKRA
     CGINVFHPIG WDAFGLPAEN AALSYNINPH TWTESNIDNM RCQLKSIGLS YDWDKELATC
     DPSYYKHEQA FFLDFLKCGL AYRKESLVNW DPVDQTVLAN EQVIDGRGWR SGAVVEKRKL
     FQWFLKITDF AEELLNDLQI LDQWPEKVKL MQEKWIGKSQ GVVIDFEILG INKTLQVFTT
     CPHTLFGAAF IAVSFDHPIL QYVNDSKVIQ LINDFDRKNL ISDVSSTIEK FGIDSGLVVK
     HPLLNVNLPV YIVNFVLMDY ATGAIFGCPA HDQRDFEFAK KYSLPVKQVV FPEVDVNLDK
     EAYVGSGIMK HSDFLDGMTV DEAKKAIVAK LTFLGVCKEI TYYRMHDWGI SRQRYWGCPI
     PIIYCKKCGT VPVDKKDLPV TLPKDVDFTK YGNPLDNHPT WKYVKCPSCG MDAERETDTF
     DTFFESSWYF AAFCGTSNGI NKDVCNMLLP VNYYVGGVEH AVLHLLYSRF FCRALTKCGY
     FNIKEPFSNL ITQGMVCHST YSDEQGNYLF PEEAKKMMEN GQHVTVGRAE KMSKSKKNVV
     NLEYIIDKYG ADTARLFILS DTPPERDIEW LDDGIEGASR YLSKLWRVII SYDKFNLNFN
     KENIIGDDVK YRRSVHKILS GITNDLDFCR LNCAVAKFRE LSNIISEMIR TSVNCYVVSE
     AIYILIRVIE PFIPHIAEKL WENIGGKGML WNQVWPKADS ELLVERNVTI VVQVNGKFVK
     ALTVANDIDD DQLKSMALEI AKNRIGGNVV KDIYVIPKRV INIVAVKPS
//