ID   SYL_EHRRW               Reviewed;         830 AA.
AC   Q5HBM8; Q5FE96;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 138.
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=Erum3010, ERWE_CDS_03070;
OS   Ehrlichia ruminantium (strain Welgevonden).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=254945;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Welgevonden;
RX   PubMed=15637156; DOI=10.1073/pnas.0406633102;
RA   Collins N.E., Liebenberg J., de Villiers E.P., Brayton K.A., Louw E.,
RA   Pretorius A., Faber F.E., van Heerden H., Josemans A., van Kleef M.,
RA   Steyn H.C., van Strijp M.F., Zweygarth E., Jongejan F., Maillard J.C.,
RA   Berthier D., Botha M., Joubert F., Corton C.H., Thomson N.R., Allsopp M.T.,
RA   Allsopp B.A.;
RT   "The genome of the heartwater agent Ehrlichia ruminantium contains multiple
RT   tandem repeats of actively variable copy number.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:838-843(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Welgevonden;
RX   PubMed=16547041; DOI=10.1128/jb.188.7.2533-2542.2006;
RA   Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y.,
RA   Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.;
RT   "Comparative genomic analysis of three strains of Ehrlichia ruminantium
RT   reveals an active process of genome size plasticity.";
RL   J. Bacteriol. 188:2533-2542(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; CR767821; CAH58018.1; -; Genomic_DNA.
DR   EMBL; CR925678; CAI26801.1; -; Genomic_DNA.
DR   RefSeq; WP_011154983.1; NC_006832.1.
DR   AlphaFoldDB; Q5HBM8; -.
DR   SMR; Q5HBM8; -.
DR   KEGG; eru:Erum3010; -.
DR   KEGG; erw:ERWE_CDS_03070; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   Proteomes; UP000001021; 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; 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.
FT   CHAIN           1..830
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334755"
FT   MOTIF           34..44
FT                   /note="'HIGH' region"
FT   MOTIF           592..596
FT                   /note="'KMSKS' region"
FT   BINDING         595
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   830 AA;  95353 MW;  255DC2566DEC9A19 CRC64;
     MHYNFKEVER DVQEKWDFTV NVKDVQCYVL EMFPYPSGNI HMGHLRNYTI GDVIARYKRA
     CGLHVFHPIG WDAFGLPAEN AALSYNISPQ VWTRKNIDNM RSQLKSIGLS YNWDKEFATC
     DAEYYKYEQE FFLDFLKYGL AYRKESLVNW DPVDQTVLAN EQVIDGRGWR SGAIIEKRKL
     SQWFLKITDF AAELLDDLKS LNQWPEKVKL MQERWIGKSE GVIIDFQIVG INEVLQVFTT
     SPHTLFGASF IAVSFDHPIL KYVNDVQLIQ LIDNFDRKDL IDESSINTVE KFGINSGLVA
     RHPLLDVDLP IYVANFVLMN YGTGAVFCCP AHDQRDFDFA KKYSLPIRQV IFPEQNVDLE
     QEAYVGSGIM GCSGFLDGMT VDDAKKSMIE KLISLGICKK QVYYRLHDWG ISRQRYWGCP
     IPIIYCKKCG IVPVDKKDLP ITLPEDIDFT KSGNPLDNHP TWKYTKCPSC GADAKRETDT
     FDTFFESSWY FAAFCGIGKG IDKDVCNKLL PVDYYIGGIE HAVLHLLYSR FFCRALTRCG
     YFDVKEPFSS LITQGMVCHS TYLDKYGNYL FPEDGKKMIQ EGKYVTVGRA EKMSKSKKNV
     VHLDDIIDKY GADSARLFIL SDTPPERDIE WLDENIEGVS RYLNKLWKMI VDYDQLEQNF
     VCDNISSDTL EYRINVHKIL NDITNDLEFY RFNCAVAKFR ELSNVISEMI RLSINHHVVS
     EAIYILIRVV EPFIPHIAEK LWQIVGGQGM LCNQLWPKVD PQLLIKKNVN IVVQVNGKFI
     KAVSVPNDID DDTLKSIALE VAQRRIGNSS VKNIYIIPGR VINIVITKSS
//