ID   SYL_WOLSU               Reviewed;         819 AA.
AC   Q7M926;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 117.
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=WS1245;
OS   Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 /
OS   NCTC 11488 / FDC 602W) (Vibrio succinogenes).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Wolinella.
OX   NCBI_TaxID=273121;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 /
RC   NCTC 11488 / FDC 602W;
RX   PubMed=14500908; DOI=10.1073/pnas.1932838100;
RA   Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O.,
RA   Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B.,
RA   Meyer F., Lederer H., Schuster S.C.;
RT   "Complete genome sequence and analysis of Wolinella succinogenes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003).
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; BX571660; CAE10325.1; -; Genomic_DNA.
DR   RefSeq; WP_011139112.1; NC_005090.1.
DR   AlphaFoldDB; Q7M926; -.
DR   SMR; Q7M926; -.
DR   STRING; 273121.WS1245; -.
DR   KEGG; wsu:WS1245; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_7; -.
DR   Proteomes; UP000000422; 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; cd00812; LeuRS_core; 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; 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   NCBIfam; TIGR00396; leuS_bact; 1.
DR   PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF13603; tRNA-synt_1_2; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 2.
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..819
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152119"
FT   MOTIF           40..50
FT                   /note="'HIGH' region"
FT   MOTIF           585..589
FT                   /note="'KMSKS' region"
FT   BINDING         588
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   819 AA;  93291 MW;  8B1FF4634CB6F840 CRC64;
     MEYNPKAIEK KWQEHWKNKR THEPLSDTSL PKKYILSMFP YPSGRIHMGH VRNYCIGDAI
     ARHFRKQNFN VLHPIGWDAF GMPAENAAIK HKSHPKKWTY DNISNMREEL DSLGLSFSNE
     REFATCDPIY SKWEQKFFID MWNRGLIYRK KGFLNWCPND QTVLANEQVI EGRCWRCDTE
     VVQKEMFQYY VKITDYAEEL LGSLDTLEGR WPSQVLTMQR NWIGRSEGLS FAFKLTSSSK
     ERIGGSFDSF EVFTTRPDTL YGVTYCALAP EHPLVRELMR QGKLPQESLE ALAKMQNIPA
     KERAMIPKEG VALGLEAIHP LTGEAIPLWA ANFVLTDYGS GAVMAVPAHD ERDFEFAKKY
     QLPQKQVILS GAAPSLDEAA YTESGTLINS GIFDGLESES AKEKIIRYFE EHSLGRGVIN
     YRLRDWGISR QRYWGTPIPL IHCPSCGIVP EDFSNLPITL PEDVIIDGEG NPLEKHPAWK
     ECRCPKCGGK ATRETDTMDT FVESSWYFLR YTTPKEEWET HALNEAMQRY WMGVDEYIGG
     IEHAILHLLY ARFFTKVLRD LGYTETNEPF THLLTQGMVL KDGAKMSKSK GNVVDPDELI
     ERFGADTARL FVLFAAPPTR ELEWNDSAVE GAYRFIKRLC DKTQFVQKVS SLPQIETATL
     SKTEKLARKK VHETLLKAQE VYSRKNAYAF NTLIASCMEA LNALSDQENP AIFTEGYFIL
     LSVLEPIIPH VAWELSQEYF GLANFKPLTP DTQALKSDSL TIAITVNGKK RGEIEMAPGS
     SNEAMLEAAK NEVSKWLEGM SIIKEIVVPD KLVNLVVKP
//