ID   SYL_RHOBA               Reviewed;         950 AA.
AC   Q7UMC0;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 119.
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=RB8919;
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=243090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX   PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA   Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA   Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA   Reinhardt R.;
RT   "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT   1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(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; BX294148; CAD75997.1; -; Genomic_DNA.
DR   RefSeq; NP_868620.1; NC_005027.1.
DR   RefSeq; WP_011122073.1; NC_005027.1.
DR   AlphaFoldDB; Q7UMC0; -.
DR   SMR; Q7UMC0; -.
DR   STRING; 243090.RB8919; -.
DR   EnsemblBacteria; CAD75997; CAD75997; RB8919.
DR   KEGG; rba:RB8919; -.
DR   PATRIC; fig|243090.15.peg.4279; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_0; -.
DR   InParanoid; Q7UMC0; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000001025; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   Gene3D; 3.40.50.620; HUPs; 3.
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; 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   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..950
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152072"
FT   MOTIF           41..52
FT                   /note="'HIGH' region"
FT   MOTIF           718..722
FT                   /note="'KMSKS' region"
FT   BINDING         721
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   950 AA;  107071 MW;  7CB553E51E6DA6B6 CRC64;
     MVRYNPNEIE PRWQAYWDEH HTFATPEKVG KKKRYVLDMF PYPSGDGLHV GHPEGYTATD
     IVSRFARARG ESVLHPMGFD AFGLPAEEHA IKTGEHPRVQ TQRNIDNFTR QLKMLGFSYD
     WDRVLATTDE EYFRWTQWIF GVLYDTWFDH DQQKGRPISE LPIPAEVTAE GELEIEQYRD
     SKRLAYLDDA LVNWCPKLGT VLANEEVVDG KSEVGGHPVK RIPLRQWMLR ITDYAERLLD
     GLDDLDWPTG IKKLQSDWIG RSTGGEVDFY LQRGAAGDDT GPFVAFKRAR ESEGFPTDPG
     KDCLRVYTTR PDTLFGATYM VVAPEHPLID VLVKPEQKDE VDAYREKASF KSDRERTDGD
     RAKTGVFTGS YAINPADGRS IPIWVADYVL AGYGTGAIMA VPAHDERDFE FAVAFDLPVI
     PVVDPPADHK QREEILAGKA CFAAEGVAIN SGEYDGKTTA EVKAALTAEL AKQGLACEAV
     NYKLRDWLFS RQRFWGEPFP VLHEIDSEGN ATGVRRLVPD DQLPVTLPEL ADFKPHGRPE
     PPLAKADDDW LIVELDGKRY RRETNTMPQW AGSCWYYLRY IDPKNSDALI DPQKEKDWMP
     VDLYVGGAEH AVLHLLYSRF WHKVLFDRGH VTCPEPFGKL VNQGMILGEV EFTSFVDPSG
     KHVSTKDVKK DAEGNRVHKA TGEQVEIVSL TEEQVVKKGE GFVLASDASI KVDSRAFKMS
     KSRGNVVNPD SVVRDYGADS LRLYEMFMGP LEATKPWAMN GVGGVRSFLD RVWRMIIDEP
     EDELKVSDAV VDTACDEEQL RVLHQTIRKV TEDNEAMSFN TAIAKMMEFT NHFTRCETRP
     REAMESFLIL LAPYAPHMCE ELWKHLGHNE SISLQPWPKW DEAALVQSSI EIPVQINGKV
     KAKISLSPDA KPNEMGEAAL ADPAVQNAIG DKKVVKTIAV PGRMVNLVVK
//