ID A0A2A5RJH8_9LACT Unreviewed; 835 AA.
AC A0A2A5RJH8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=RT41_GL001965 {ECO:0000313|EMBL:PCR99324.1};
OS Lactococcus fujiensis JCM 16395.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=1291764 {ECO:0000313|EMBL:PCR99324.1, ECO:0000313|Proteomes:UP000218181};
RN [1] {ECO:0000313|EMBL:PCR99324.1, ECO:0000313|Proteomes:UP000218181}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 16395 {ECO:0000313|EMBL:PCR99324.1,
RC ECO:0000313|Proteomes:UP000218181};
RA Sun Z., Zhong Z., Liu W., Zhang W., Zhang H.;
RT "Draft genome sequences of 10 type strains of Lactococcus.";
RL Submitted (DEC-2014) 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:PCR99324.1}.
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DR EMBL; JXJU01000009; PCR99324.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A5RJH8; -.
DR STRING; 1291764.GCA_001311235_01406; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000218181; 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 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:UP000218181}.
FT DOMAIN 39..161
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 220..407
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 414..577
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 615..643
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 690..799
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 616..620
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 619
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 835 AA; 94384 MW; 44272A2BDE7F71D8 CRC64;
MEYNHQEIEA KWQKYWADNE TFRTKTDKNS PKFYALDMFP YPSGAGLHVG HPEGYTATDI
LSRYKRAQGF NVLHPMGWDA FGLPAENYAM STGHDPAGFT AENIANFKRQ INSLGFSYDW
DREVNTTDPN FYKWTQWIFT KMYEKGLAYE AQVPVNWVEE LGTAIANEEV LPDGTSERGG
YPVVRKPMRQ WILKITAYAD RLLDDLDELD WPESIKEMQR NWIGKSTGAD VTFKVAQSDE
EFTVFTTRPD TLFGATYCVL APEHDLVEAV TTAEQANAVA EYKRQASLKS DLARTDLAKE
KTGVWTGSYA INPVNGKEVP IWIADYVLAT YGHGAIMAVP AHDERDWEFA KVYNLNIIPV
LEGEDGQGSA IDVQKEPFTA DGRHINSDFL DGLNKAEAIA KMVDWLEENK VGTKKVTYKL
RDWLFSRQRY WGEPIPIIHW EDGTSTAVPE SDLPLVLPVT SDIKPSGTGE SPLANLTDWL
TVTREDGVKG RRETNTMPQW AGSSWYYLRY IDPHNDKALA DPELLKQWLP VDIYVGGAEH
AVLHLLYARF WHKFLYDLGI VPTKEPFQKL FNQGMILGTS YRDHRGALVA TDKVEKRDGL
FFNIETGEEL EQAPAKMSKS LKNVVNPDDV VERYGADTLR VYEMFMGPLD ASIAWSEEGL
EGARKFLDRV VRLIDSEKVV SENDGKLDKI YHETVKNVTE RLEHMLFNTA ISQLMIFVNA
SNKVDKLPLE YAKGFVQLLA PFAPHIAEEL WVKLGQTAGI SYVTWPTFDA AKLVESEVEI
VVQVNGKLKA KIKIAKDISR DELAKLGQKA VADQIKGDIV KVIAVPNKLV NIVVK
//
