ID   SYL_PROM1               Reviewed;         862 AA.
AC   A2C242;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=NATL1_09941;
OS   Prochlorococcus marinus (strain NATL1A).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NATL1A;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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; CP000553; ABM75552.1; -; Genomic_DNA.
DR   RefSeq; WP_011823678.1; NC_008819.1.
DR   AlphaFoldDB; A2C242; -.
DR   SMR; A2C242; -.
DR   STRING; 167555.NATL1_09941; -.
DR   EnsemblBacteria; ABM75552; ABM75552; NATL1_09941.
DR   KEGG; pme:NATL1_09941; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_3; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000002592; 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   Gene3D; 3.40.50.620; -; 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   PANTHER; PTHR43740; PTHR43740; 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; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00396; leuS_bact; 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..862
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334791"
FT   MOTIF           51..61
FT                   /note="'HIGH' region"
FT   MOTIF           624..628
FT                   /note="'KMSKS' region"
FT   BINDING         627
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   862 AA;  99157 MW;  51BCCCE7FB0922A4 CRC64;
     MNNTTSDIND QRYEPREVEA YWQKEWANDD LYRTNTEVNK ENTFYALSMF PYPSGSLHMG
     HVRNYVITDV LARYKRMKGL NVLHPMGWDS FGLPAENAAI ERETSPSTWT DKNISQMKDQ
     LDRLGLSIDW SKEVTTCKED YYKWTQYIFN QLHKNNLAYQ KKATVNWDPI DQTVLANEQV
     DAEGKSWRSG AKVEKKELNQ WFLRITSFAE DLNKDLVTLN DWPDRVRVMQ KNWIGKSIGA
     EITFDIKNSD QKITAFTTRI DTVYGVSYLV LASNHPLIDQ LISSNDIDKL NDFRQTQEKL
     SDLERNSDTR QKLGMYLGVD AINPANNKEI PIWIGDYVIM EYGTGAVMGV PAHDSRDYQF
     AKSYDLPIQY VIKPNIGEDE SYLNAEFVDK GVMINSDKFN GIESDIAKTK ILEFGSNSNW
     AKPKITYKLR DWLISRQRYW GCPIPIINCK KCGQVRVPDD DLPVVLPIDI KLTGKGKSPL
     TTKTEWINTC CPKCGTDAKR ETDTMDTFMC SSWYFLRYIN PDNCEKPFLK SEIDKWLPVK
     QYVGGIEHAI LHLLYSRFLT KALKRCGLIN IDEPFKKLLT QGMVQAVTFK NPNTNKYFSK
     DQIKDIDNPK DPLTGENIEI IYEKMSKSKY NGVDPSVVID KYGADTARMF ILFKAPPEKD
     LEWDDSDVEG QYRFIQRLWK FVINTFKLTN NNSRSNIEKE KSKDEEALRL INIAIKEITD
     DLDNLQFNTA ISELMKVVNG LSLIVNYCSN ETLNKVISIL VKITSPFSPH IAEELWKTIG
     NTQSIHLQSW PEFDAGAIEQ DTFKLMIQIN GKVRGSINAS KNLSKENLED LAIKTEAAIK
     WMDGKEPKRI IVVPNKLVNI VI