ID   SYL_PROMA               Reviewed;         870 AA.
AC   Q7VBZ5;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 111.
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=Pro_0947;
OS   Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167539;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARG / CCMP1375 / SS120;
RX   PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA   Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA   Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA   Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA   Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT   "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT   nearly minimal oxyphototrophic genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(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; AE017126; AAP99991.1; -; Genomic_DNA.
DR   RefSeq; NP_875339.1; NC_005042.1.
DR   RefSeq; WP_011125099.1; NC_005042.1.
DR   AlphaFoldDB; Q7VBZ5; -.
DR   SMR; Q7VBZ5; -.
DR   STRING; 167539.Pro_0947; -.
DR   PRIDE; Q7VBZ5; -.
DR   EnsemblBacteria; AAP99991; AAP99991; Pro_0947.
DR   GeneID; 54200290; -.
DR   KEGG; pma:Pro_0947; -.
DR   PATRIC; fig|167539.5.peg.996; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_3; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001420; 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..870
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152063"
FT   MOTIF           55..65
FT                   /note="'HIGH' region"
FT   MOTIF           626..630
FT                   /note="'KMSKS' region"
FT   BINDING         629
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   870 AA;  99805 MW;  673DF65DC039FA7C CRC64;
     MASKISQTPE KQPSTAYDPL SIETRWQQSW KEQGLYKTKE PTKSQKTFYA LSMFPYPSGT
     LHMGHVRNYV ITDVIARLHR MKGDSVLHPM GWDAFGLPAE NAAIERGIPA DIWTYKNIED
     MRNQLNRLGL SIDWDKEVTT CKEEYYKWTQ YIFLELYEAG LAYQKSATVN WDPIDKTVLA
     NEQVDANGRS WRSGALVEKK KLKQWFLKIT DFADELLEDI ELLSGWPQNV KTMQQNWIGR
     SNGTEIDFYI KGKNNIFITV FTTRPDTLHG TEYLVLAPDH ELINSIIDKN KITELEQFRT
     EISILTDQER TSDGNNKRGM FLGCHAINPI NKKIIPIWVG EYVLSSYATG AVMGVPAHDK
     RDYKFAKKYS LPIQYVIKSP SQEASDLEAS SAYVKEGIMI NSGEFNGINS KEAGFMITKL
     GVKQGWAKNK VTYKLRDWLI SRQRMWGCPI PIIYCPDCGS VPVKREELPV KLTNPSVIGK
     SQENKNNIPI MKCSKCNKDS ILETDTMDTF MCSSWYFLRY IDVENNKLPF TKTEVDKWLP
     VDQYVGGIEH AILHLLYSRF LIKALRNRGL LNIKEPFSNL LTQGMVQGVT FKNPKTSKYI
     SPDHINDINT PLDPETGEPL DVLYEKMSKS KYNGVDPASV IDKYGTDTAR MFILFKAPPE
     KDLEWDESDV EGQYRFLNRL WRIVIYSIET KDINISNCTQ EILLNDLSDK ERKLIKVLNN
     TIKEVTNDLV NDFQFNTAIS ELMILCNSIY ENIDDCGDYI VTETFKKLTL LLAPFAPHIA
     EEFWIKLKGK GSVHENSWPT YDPKALLEDS YKLIIQINGK VRGNISVNHE DSELELKNKA
     LACETTQKWL NGIEPKRIII VKGKIINIVF