ID   SYL_PROM4               Reviewed;         872 AA.
AC   A9BAE4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=P9211_08751;
OS   Prochlorococcus marinus (strain MIT 9211).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=93059;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9211;
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; CP000878; ABX08806.1; -; Genomic_DNA.
DR   RefSeq; WP_012195428.1; NC_009976.1.
DR   AlphaFoldDB; A9BAE4; -.
DR   SMR; A9BAE4; -.
DR   STRING; 93059.P9211_08751; -.
DR   PRIDE; A9BAE4; -.
DR   EnsemblBacteria; ABX08806; ABX08806; P9211_08751.
DR   KEGG; pmj:P9211_08751; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_3; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000000788; 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; Reference proteome.
FT   CHAIN           1..872
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091345"
FT   MOTIF           56..66
FT                   /note="'HIGH' region"
FT   MOTIF           629..633
FT                   /note="'KMSKS' region"
FT   BINDING         632
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   872 AA;  99820 MW;  CBE15658902CED49 CRC64;
     MTDTSSSISR KSLRADSYQP QLIEEKWQNE WKISGLYKTR EPKEDQKTFY ALSMFPYPSG
     NLHMGHVRNY VITDVIARVH RMKGFSVLHP MGWDAFGLPA ENAAIERNIQ PDIWTEKNIS
     HMRSQLDRLG LSIDWDREQT TSKSEYYKWT QSIFLKLYEA GLAYQKSATV NWDPVDKTVL
     ANEQVDADGK SWRSGALVEK KQLKQWFLKI TDYAEILLKD IDTLTEWPER VKTMQSNWIG
     KSVGVKINFQ LLTKEKENLS VFTTRPDTLF GSTYLVLSPE DKLVDKLVDP KLINDLSNFR
     DYVSKLSDKE RTAEGKPKNG MAIGAYAINP INQEKLPIWI ADYVLSGYGT GAVMGVPAHD
     QRDLDFAQKY SLPIKYVIKP SGIIEKKKEV KAYSEVGVMI NSGPFNGQKS DEVKSLITEK
     GIKENWAEKK TTYKLRDWLI SRQRYWGCPI PIVHCAKCGI VPIEKENLPV FLPTNIQLSG
     KGNSPLKDNE WTKTQCPICK GIARRESDTM DTFICSSWYY LRFIDPNNKK NIIDKNLADR
     WMPVDQYVGG IEHAILHLLY ARFITKVLRD KDMISIDEPF KKLLTQGMVQ GITFKNPKTG
     KYIPPNKINN IKTPLDPSTG ESLELIYEKM SKSKHNGIDP STVIDKYGAD TARMFILFKA
     PPEKDLEWDD ADVEGQYRFL QRLWRLINES KTYNKLSLDS NENNNLNNLN QDEISLRRSV
     HLAIKEISND LNEGNQFNTA ISELMKLSNN MNELLGKCRI SVVNESLSIL IRILSPFAPH
     LAEEAWSTLK GKGSVHEQKW PEFDPNALKQ DNYQLVIQMN GKVRGSIKIA SETNKQEIEK
     IALNSDIAKK WLIDGSYKKV IVVLGKLVNI VY