ID   SYL_PROM5               Reviewed;         864 AA.
AC   A2BWL7;
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=P9515_09711;
OS   Prochlorococcus marinus (strain MIT 9515).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167542;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9515;
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; CP000552; ABM72178.1; -; Genomic_DNA.
DR   RefSeq; WP_011820280.1; NC_008817.1.
DR   AlphaFoldDB; A2BWL7; -.
DR   SMR; A2BWL7; -.
DR   STRING; 167542.P9515_09711; -.
DR   EnsemblBacteria; ABM72178; ABM72178; P9515_09711.
DR   KEGG; pmc:P9515_09711; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_3; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001589; 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; 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; 3.
DR   Pfam; PF13603; tRNA-synt_1_2; 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..864
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334790"
FT   MOTIF           57..67
FT                   /note="'HIGH' region"
FT   MOTIF           628..632
FT                   /note="'KMSKS' region"
FT   BINDING         631
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   864 AA;  100650 MW;  09D84245422D8C19 CRC64;
     MIYSENTDEK SNQHTNNLYK PCEIENKWQE IWDKENLYKT DDKSSKKEKF YALSMFPYPS
     GNLHMGHVRN YVITDLIARF QRFQGKSLLH PMGWDAFGLP AENAAIERGI NPNDWTKKNI
     AHMKSQLKLL GLSVDWDKEF ATCDENYYLW TQFLFLELHK SGLVYQKESE VNWDPIDNTV
     LANEQVDSEG KSWRSGAKVE KKLLTQWFLK ITNYTEELLQ DLEKLSEWPE RVKIMQENWI
     GKSKGANIIF KINEFENEKI KVFTTRPDTL FGVTYIAISI NNPLINKISD NEILSKLENL
     KIYLKKNQDK DQKKIGIPTN LKAINPINSN EIPIWIASYV LDEYGTGAVM GVPAHDQRDF
     EFAKINFIDI KQVIIKDKDN DKSTFKLKNA FTDNGFLINS NNFNGLCNND AKKQILEQGK
     INGWAEEEIH YRLRDWLISR QRYWGCPIPI IKCNNCGSIP VNKKNLPVKL PKEIEISSNK
     INSLGSYKDW VKTTCPKCGN LASRETDTMD TFMCSSWYFL RYPSSKCKTK PFEKDNVNKW
     LPVDQYVGGV EHAILHLLYA RFLTKALRDN NLFDIDEPFK KLLTQGMVQA AAYKNTKTGK
     YISPKDIKDF NNPTDPNDDS KLEVLFEKMS KSKYNGIDPE SVIKKYGADT ARMFILFKAP
     PEKDLEWGDS DVEGQYRFLC RIWKLFLDYR NNESWDNQKN YNREKENSLT KSINIAIKEI
     SNDIKNNQFN TAISELMKFY NSLSSSMIYV NKDLRKDAFK KFCILLAPFA PHIAEEIWNL
     IGYQKSVHLE RWPIFNEDAL KEDCYELVIQ INGKVRDKIN VGIDISEDQI KQKTLTRPNV
     RKWIDQKTIR KIIIVKGKIM NIVV