ID   SYL_HELMI               Reviewed;         846 AA.
AC   B0TBJ3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 96.
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=Helmi_25810; ORFNames=HM1_2677;
OS   Heliobacterium modesticaldum (strain ATCC 51547 / Ice1).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Heliobacteriaceae;
OC   Heliomicrobium.
OX   NCBI_TaxID=498761;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51547 / Ice1;
RX   PubMed=18441057; DOI=10.1128/jb.00299-08;
RA   Sattley W.M., Madigan M.T., Swingley W.D., Cheung P.C., Clocksin K.M.,
RA   Conrad A.L., Dejesa L.C., Honchak B.M., Jung D.O., Karbach L.E.,
RA   Kurdoglu A., Lahiri S., Mastrian S.D., Page L.E., Taylor H.L., Wang Z.T.,
RA   Raymond J., Chen M., Blankenship R.E., Touchman J.W.;
RT   "The genome of Heliobacterium modesticaldum, a phototrophic representative
RT   of the Firmicutes containing the simplest photosynthetic apparatus.";
RL   J. Bacteriol. 190:4687-4696(2008).
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; CP000930; ABZ85206.1; -; Genomic_DNA.
DR   RefSeq; WP_012283691.1; NC_010337.2.
DR   AlphaFoldDB; B0TBJ3; -.
DR   SMR; B0TBJ3; -.
DR   STRING; 498761.HM1_2677; -.
DR   KEGG; hmo:HM1_2677; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000008550; 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; 3.10.20.590; -; 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; 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..846
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091322"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           586..590
FT                   /note="'KMSKS' region"
FT   BINDING         589
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   846 AA;  96367 MW;  D4062D5A09098691 CRC64;
     MQERYDYQQI EKKWQKYWAD TGMFRLQQEE GRPKYYCLEM FPYPSGNLHM GHVRVYSIGD
     VVARFKTMQG YNVLHPMGWD AFGLPAENAA IKHKVPPADW TWSNIANMRR QLQSMGISYD
     WEREVATCHP DYYKWTQWLF LQLYKAGLAY KKKANVNWCP DCATVLANEQ VVDGLCERCD
     ATVEKKALEQ WFFRITDYAQ RLLDDLNKLP GWPDKVKTMQ ENWIGRSEGV EADFALENPV
     GGVDKLTVYT TRQDTIFGVT YMVLAPEHPA VEALVSGNPR EAELRAFIKK VLSQSEIDRT
     ANDTEKEGIF TGHYCINPLT GEKVAVYLAN YVLVDYGTGA VMGVPAHDQR DFEFATKYNI
     PMKVVIQPEG LPDLDVEEMD HAYEGEGRLV NSGEFDGLIN TQALDVIADK LEREGKGVRK
     VNYRLRDWLI SRQRYWGAPI PVIYCEKCGE VAVPDEQLPV MLPTDVAFTP SGESPLTSRP
     DFYECTCPRC GGKGRRETDT MDTFVCSSWY FLRYCTPKDK DHAFLQEDVD YWMNVDQYIG
     GVEHAILHLM YARFFTKVLY DLKLVKVEEP FENLLTQGMV LMGGSKMSKS KGNTVSPEEI
     IAKYGADTAR LFILFAAPPE RDLEWSDRGV EGAHRFLHRL WRLVYAYSDQ IASVPGTMVG
     YGKGQPNGSK GDNLFSLNSD DRELVRVAHY TVKKVTEDIG QRFNFNTAVS AIMEMVNYFY
     QYKDKVPAEQ QNIPLVKDAL ARLVLVLAPF APHICEELWQ VIGGGESVYK QPWPTYDEQA
     LVRDEVEVVV QINGKVREKL RVANGLDGEA IKAKVLEMDK VQALIAGKSV VKLITVPNKL
     VNIVVK
//