SYL_STRPJ
ID SYL_STRPJ Reviewed; 833 AA.
AC B8ZKS5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=SPN23F02440;
OS Streptococcus pneumoniae (strain ATCC 700669 / Spain 23F-1).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=561276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700669 / Spain 23F-1;
RX PubMed=19114491; DOI=10.1128/jb.01343-08;
RA Croucher N.J., Walker D., Romero P., Lennard N., Paterson G.K., Bason N.C.,
RA Mitchell A.M., Quail M.A., Andrew P.W., Parkhill J., Bentley S.D.,
RA Mitchell T.J.;
RT "Role of conjugative elements in the evolution of the multidrug-resistant
RT pandemic clone Streptococcus pneumoniae Spain23F ST81.";
RL J. Bacteriol. 191:1480-1489(2009).
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; FM211187; CAR68104.1; -; Genomic_DNA.
DR RefSeq; WP_000011766.1; NC_011900.1.
DR PDB; 4K47; X-ray; 2.02 A; A=228-410.
DR PDB; 4K48; X-ray; 2.49 A; A=228-410.
DR PDB; 7BZJ; X-ray; 2.00 A; A=228-410.
DR PDBsum; 4K47; -.
DR PDBsum; 4K48; -.
DR PDBsum; 7BZJ; -.
DR AlphaFoldDB; B8ZKS5; -.
DR SMR; B8ZKS5; -.
DR KEGG; sne:SPN23F02440; -.
DR HOGENOM; CLU_004427_0_0_9; -.
DR OMA; TFMVLAP; -.
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 Gene3D; 3.90.740.10; -; 1.
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; 1.
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 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..833
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000199226"
FT MOTIF 41..52
FT /note="'HIGH' region"
FT MOTIF 610..614
FT /note="'KMSKS' region"
FT BINDING 613
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
FT STRAND 229..236
FT /evidence="ECO:0007829|PDB:7BZJ"
FT STRAND 242..248
FT /evidence="ECO:0007829|PDB:7BZJ"
FT HELIX 250..255
FT /evidence="ECO:0007829|PDB:7BZJ"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:7BZJ"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:7BZJ"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:7BZJ"
FT HELIX 277..288
FT /evidence="ECO:0007829|PDB:7BZJ"
FT HELIX 292..295
FT /evidence="ECO:0007829|PDB:7BZJ"
FT STRAND 305..312
FT /evidence="ECO:0007829|PDB:7BZJ"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:7BZJ"
FT STRAND 319..324
FT /evidence="ECO:0007829|PDB:7BZJ"
FT STRAND 335..339
FT /evidence="ECO:0007829|PDB:7BZJ"
FT TURN 341..343
FT /evidence="ECO:0007829|PDB:7BZJ"
FT HELIX 345..354
FT /evidence="ECO:0007829|PDB:7BZJ"
FT TURN 367..369
FT /evidence="ECO:0007829|PDB:7BZJ"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:7BZJ"
FT HELIX 389..403
FT /evidence="ECO:0007829|PDB:7BZJ"
FT STRAND 405..409
FT /evidence="ECO:0007829|PDB:7BZJ"
SQ SEQUENCE 833 AA; 94339 MW; C9F166C999CFC3F3 CRC64;
MSFYNHKEIE PKWQGYWAEH HTFKTGTDAS KPKFYALDMF PYPSGAGLHV GHPEGYTATD
ILSRYKRAQG YNVLHPMGWD AFGLPAEQYA MDTGNDPAEF TAENIANFKR QINALGFSYD
WDREVNTTDP NYYKWTQWIF TKLYEKGLAY EAEVPVNWVE ELGTAIANEE VLPDGTSERG
GYPVVRKPMR QWMLKITAYA ERLLNDLDEL DWSESIKDMQ RNWIGKSTGA NVTFKVKGTD
KEFTVFTTRP DTLFGATFTV LAPEHELVDA ITSSEQAEAV ADYKHQASLK SDLVRTDLAK
EKTGVWTGAY AINPVNGKEM PIWIADYVLA SYGTGAVMAV PAHDQRDWEF AKQFDLPIVE
VLEGGNVEEA AYTEDGLHVN SDFLDGLNKE DAIAKIVACL EEKGCGQEKV TYRLRDWLFS
RQRYWGEPIP IIHWEDGTST AVPETELPLV LPVTKDIRPS GTGESPLANL TDWLEVTRED
GVKGRRETNT MPQWAGSSWY YLRYIDPHNT EKLADEDLLK QWLPVDIYVG GAEHAVLHLL
YARFWHKFLY DLGVVPTKEP FQKLFNQGMI LGTSYRDHRG ALVATDKVEK RDGSFFHIET
GEELEQAPAK MSKSLKNVVN PDDVVEQYGA DTLRVYEMFM GPLDASIAWS EEGLEGSRKF
LDRVYRLITS KEILAENNGA LDKAYNETVK AVTEQIESLK FNTAIAQLMV FVNAANKEDK
LYVDYAKGFI QLIAPFAPHL AEELWQTVAE TGESISYVAW PTWDESKLVE DEIEIVVQIK
GKVRAKLMVA KDLSREELQE IALADEKVKA EIDGKEIVKV ISVPNKLVNI VVK
