ID   SYL_PROMM               Reviewed;         878 AA.
AC   Q7TV01;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=PMT_0715;
OS   Prochlorococcus marinus (strain MIT 9313).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=74547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9313;
RX   PubMed=12917642; DOI=10.1038/nature01947;
RA   Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA   Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA   Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA   Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA   Chisholm S.W.;
RT   "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT   differentiation.";
RL   Nature 424:1042-1047(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; BX548175; CAE20890.1; -; Genomic_DNA.
DR   RefSeq; WP_011130093.1; NC_005071.1.
DR   AlphaFoldDB; Q7TV01; -.
DR   SMR; Q7TV01; -.
DR   STRING; 74547.PMT_0715; -.
DR   EnsemblBacteria; CAE20890; CAE20890; PMT_0715.
DR   KEGG; pmt:PMT_0715; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_3; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001423; 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; Reference proteome.
FT   CHAIN           1..878
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152064"
FT   MOTIF           56..66
FT                   /note="'HIGH' region"
FT   MOTIF           630..634
FT                   /note="'KMSKS' region"
FT   BINDING         633
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   878 AA;  98558 MW;  344EA20A16DB279D CRC64;
     MTESFPSTSA SSQSSARYDP IELETRWQKE WLRQGLDRTP VAETNQKRFY ALSMFPYPSG
     KLHMGHVRNY VITDVIARVQ RMRGDAVLHP MGWDAFGLPA ENAAIARNVD PGDWTDQNIA
     QMRAQLDRLG LSIDWDRQQA TCHQDYYRWT QWLFLELFAG GLAYQKEATV NWDPVDKTVL
     ANEQVDGEGR SWRSGALVEQ RQLKQWFLRI TDYADALIDD LDELTGWPER VRTMQANWIG
     RSHGAEIKFR VAGVANSIIT VFTTRPDTLH GASYVVLAPE HPLVESLTSP EQRLAVTAFC
     DLISQLSVKD RTAEDQPKRG VPIGAQVINP VNGESLPVWI ADYVLADYGS GAVMGVPAHD
     ERDFIFARSH ELPIRIVVQL PDTDEHHNDG QAWTGAGVLV NSGAFDGLST EEAKVAITTH
     GASEGWAQSK VQYRLRDWLI SRQRYWGCPI PIIHCASCGI VPVPQEDLPV TLPRDIDLSG
     KGGSPIAQEQ AWVEVKCPIC GEKAHRETDT MDTFMCSSWY YLRFADPLNS QRPFDKDIVD
     EWLPVDQYVG GIEHAILHLL YARFFTKALH DRNLIGFKEP FNRLLTQGMV QGLTYRNAKN
     GSYISPELVS DDSDPRDPES GDRLEVLFEK MSKSKYNGVD PAVVIDRYGA DTARMFILFK
     APPEKDLEWD DADVEGQFRF LQRLIRLIDS FAWPKTDGEN ASISSANLII DSADLSEEEI
     NMRRATHKAI EAITEDLSGD IQLNTAISEL MKLSNSLSGK LDKVRNEVAA EALSVLVRLM
     APFAPHLAEE FWLKLHGHGS IHQQSWPVID PSALVLETIE LVIQVKGKVR GKIQVPANAD
     KKTLEELALN SDIAVKWLEG QSPRRIIIVP GKLVNLVP