ID   SYL_PROM2               Reviewed;         856 AA.
AC   A8G4T7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=P9215_10031;
OS   Prochlorococcus marinus (strain MIT 9215).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=93060;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9215;
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; CP000825; ABV50618.1; -; Genomic_DNA.
DR   RefSeq; WP_012007705.1; NC_009840.1.
DR   AlphaFoldDB; A8G4T7; -.
DR   SMR; A8G4T7; -.
DR   STRING; 93060.P9215_10031; -.
DR   EnsemblBacteria; ABV50618; ABV50618; P9215_10031.
DR   KEGG; pmh:P9215_10031; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_3; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000002014; 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..856
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000057346"
FT   MOTIF           53..63
FT                   /note="'HIGH' region"
FT   MOTIF           622..626
FT                   /note="'KMSKS' region"
FT   BINDING         625
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   856 AA;  98952 MW;  CB977FD2125F5D68 CRC64;
     MISPDKQYES FTNLYNPSEI EKKWQLIWTE NNLYKTDELT ENSDKFYALS MFPYPSGNLH
     MGHVRNYVIT DLIARFHRFK GKSVLHPMGW DAFGLPAENA AIERGISPSV WTKQNISHMR
     SQLKLLGLSV DWDREFATCD ENYYIWTQYL FLELYKAGLV YQKESEVNWD PVDNTVLANE
     QVDSEGKSWR SGAVVEKKLL KQWFLRITNY ADELLKDLEK LDNWPERVKI MQDNWIGKSI
     GTNINFNLNT NPEEKITVFT TRPDTLFGVT YLAISVNHSL IKYISDQETI QDIENLKQYL
     KNNKNNELEK IGIKTSLIAI NPINSEPIPI WVASYVLDEY GTGAVMGVPA HDQRDFEFAK
     KNNIDIKQVI INDKSEKTNE LDKAYVENGY LMNSDQYNFM ENTIAKLKIS EEGVDNGWAE
     NKIQYRLRDW LISRQRYWGC PIPIVNCKKC GSVPLKQSEL PVALPKDIDI SANKINALGD
     NNHWINTTCP KCGIAAKKET DTMDTFMCSS WYFLRYPSSK CSNKPFEKIE INKWLPVDQY
     VGGVEHAILH LLYARFFTKA LRDNELFEID EPFKKLLTQG MVQAAAYKNN KTGKYVSPSD
     INDLSNPTDP IDNTKLEVLF EKMSKSKYNG IDPESVIKKY GADTARMFIL FKAPPEKDLE
     WGDTDVEGQF RFLNRIWKLY INCAKDINSK SNSYPDREKS LIKSMNIAIK EISNDILNNQ
     FNTAISELMK FYNSLANSIN DVNNTLKIEA LKTFCILLAP FAPHIAEEIW HLIGFKKSVH
     LEYWPSFNAE ALKEDSYELV IQVNGKVRDK VKINNDMSED QIKELTLKRP NILKWTQDKE
     IRKIIIVKGK IINIVV