ID   SYL_GLOC7               Reviewed;         854 AA.
AC   B7KCI7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 88.
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};
GN   OrderedLocusNames=PCC7424_1860;
OS   Gloeothece citriformis (strain PCC 7424) (Cyanothece sp. (strain PCC
OS   7424)).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Aphanothecaceae; Gloeothece; Gloeothece citriformis.
OX   NCBI_TaxID=65393;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7424;
RX   PubMed=21972240; DOI=10.1128/mbio.00214-11;
RA   Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA   Sherman L.A., Pakrasi H.B.;
RT   "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT   unicellular nitrogen-fixing Cyanobacteria.";
RL   MBio 2:E214-E214(2011).
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; CP001291; ACK70292.1; -; Genomic_DNA.
DR   RefSeq; WP_012599235.1; NC_011729.1.
DR   AlphaFoldDB; B7KCI7; -.
DR   SMR; B7KCI7; -.
DR   STRING; 65393.PCC7424_1860; -.
DR   KEGG; cyc:PCC7424_1860; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_3; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000002384; 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   CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   NCBIfam; TIGR00396; leuS_bact; 1.
DR   PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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..854
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000199189"
FT   REGION          586..607
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           615..619
FT                   /note="'KMSKS' region"
FT   BINDING         618
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   854 AA;  96892 MW;  E7E26E0AA0BBCC43 CRC64;
     MESVYNAEAI EKKWQQTWVE MGLDQTPEDN TKPKYYALSM FPYPSGNLHM GHVRNYVITD
     VIARLKRMQG HRVLHPMGWD AFGLPAENAA IERGIHPAKW TYQNIAQMRQ QLQQLGLSID
     WSREVTTCSP DYYQWTQWLF LQFFQAGLAY QKEAAVNWDP VDQTVLANEQ VDSEGKSWRS
     GAKVERKMLR QWFLKITDYA EQLLNDLDKL PGWPEKVKLM QANWIGKSIG AYLEFPIVGM
     DEKIAVFTTR PDTVYGVTYV VLAPEHPLTP KVTTAKNKKA VEKFIKEVTS ESEQERTAED
     KPKKGILTGG KAINPFNGQE VPILIANYVL YEYGTGAVMG VPAHDIRDFK FAQENKLPIR
     VVIVPEDQQD QDVTLTQAYT EPGIMVNSGS FDGMDSITGK TAIIDYAEKQ GFGKARVQYR
     LRDWLISRQR YWGCPIPVIH CPSCGTVPVP DEDLPVKLPE DVEFSGRGAS PLAKLDSWIN
     VPCPSCGEPA KRETDTMDTF IDSSWYFLRY TDANDQQTAF SLDKVNDWMS VDQYVGGVEH
     AILHLLYSRF FTKVVRDRGL VDVDEPFQRL LTQGMVQGMT YKNPKTGKYI PSSQVNPEDP
     KDPETGEPLS VFYEKMSKSK YNGVDPKQVL AKYGADTARM FILFKAPPEK DLEWDDADVE
     GQFRFLNKVW RIVGEYQSNH KSSSKKKGSL TKVEKDLRRA IHIAIKEITE DLDGEYQFNT
     AVSELMKLSN ALVDAKCYES PVYTEGVQTL LILLAPFAPH IAEELWHTLG HSESVHLQGW
     PQLDPSALEV DEITLVIQIM GKTRGTIQVP SSATKEELEK FAFESEVAQR HLKDQEVKKV
     IVVPGKLVNF VVGK
//