ID A0A139NHH0_9STRE Unreviewed; 833 AA.
AC A0A139NHH0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Leucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00049};
DE EC=6.1.1.4 {ECO:0000256|HAMAP-Rule:MF_00049};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00049};
DE Short=LeuRS {ECO:0000256|HAMAP-Rule:MF_00049};
GN Name=leuS {ECO:0000256|HAMAP-Rule:MF_00049};
GN ORFNames=STRDD12_01310 {ECO:0000313|EMBL:KXT75499.1};
OS Streptococcus sp. DD12.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1777880 {ECO:0000313|EMBL:KXT75499.1, ECO:0000313|Proteomes:UP000070638};
RN [1] {ECO:0000313|EMBL:KXT75499.1, ECO:0000313|Proteomes:UP000070638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD12 {ECO:0000313|EMBL:KXT75499.1,
RC ECO:0000313|Proteomes:UP000070638};
RA Denapaite D., Rieger M., Koendgen S., Brueckner R., Ochigava I.,
RA Kappeler P., Maetz-Rensing K., Leendertz F., Hakenbeck R.;
RT "Highly variable Streptococcus oralis are common among viridans
RT streptococci isolated from primates.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001372, ECO:0000256|HAMAP-
CC Rule:MF_00049};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00049}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00049,
CC ECO:0000256|RuleBase:RU363035}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00049}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXT75499.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LQRG01000011; KXT75499.1; -; Genomic_DNA.
DR RefSeq; WP_066916397.1; NZ_KQ969496.1.
DR AlphaFoldDB; A0A139NHH0; -.
DR STRING; 1777880.STRDD12_01310; -.
DR PATRIC; fig|1777880.3.peg.1343; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000070638; Unassembled WGS sequence.
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 Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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 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 {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00049};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00049};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00049};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00049};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00049};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00049}; Reference proteome {ECO:0000313|Proteomes:UP000070638}.
FT DOMAIN 40..164
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 221..401
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 414..571
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 609..637
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 684..794
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 610..614
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 613
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 833 AA; 94044 MW; 9E1D82C895DEDD01 CRC64;
MATYNHKEIE PKWQKYWADH HTFKTGTDAQ KPNFYALDMF PYPSGAGLHV GHPEGYTATD
ILSRYKRAQG YNVLHPMGWD AFGLPAEQYA MDTGNDPADF TAENIANFKR QINALGFSYD
WDREVNTTDP NYYKWTQWIF TKLYEKGLAY EAEVPVNWVE ELGTAIANEE VLPDGTSERG
GYPVVRKPMR QWMLKITAYA ERLLNDLDEL DWPESIKDMQ RNWIGKSTGA NVTFKVKGTD
KEFTVFTTRP DTLFGATFTV LAPEHELVDA ITSPEQAEAV ADYKHQASLK SDLARTDLAK
EKTGVWTGAY AVNPVNGKEI PIWIADYVLA SYGTGAVMAV PAHDERDWEF AKQFGLPIIE
VLEGGNVAEA AYTEDGLHVN SGFLDGLNKE EAIAKIVAWL EEKGCGQEKI TYRLRDWLFS
RQRYWGEPIP IIHWEDGTST AVPESELPLV LPVTKDIRPS GTGESPLANL TDWLEVTRED
GVKGRRETNT MPQWAGSSWY YLRYIDPHNT EKLADEDLLK AWLPVDIYVG GAEHAVLHLL
YARFWHKFLY DLGVVPTKEP FQKLFNQGMI LGTSYRDHRG ALVATDKVEK RDGSFFHVET
GEELEQAPAK MSKSLKNVVN PDDVVDQYGA DTLRVYEMFM GPLDASIAWS EEGLEGSRKF
LDRVYRLLTS KEIVAENSGA LDKVYNETVK AVTEQIESMK FNTAIAQLMV FVNAANKEDE
LYVDYAKGFI QLLAPFAPHL AEELWQTVAG TGESISYVAW PRWDESKLVE DEIEIVVQIK
GKVRAKLTVA KDLSREELQE VALADEKVQA EIAGKEIVKV IAVPNKLVNI VVK
//
