ID E1QVI0_OLSUV Unreviewed; 854 AA.
AC E1QVI0;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 90.
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 OrderedLocusNames=Olsu_1022 {ECO:0000313|EMBL:ADK68133.1};
OS Olsenella uli (strain ATCC 49627 / DSM 7084 / CIP 109912 / JCM 12494 /
OS NCIMB 702895 / VPI D76D-27C) (Lactobacillus uli).
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC Olsenella.
OX NCBI_TaxID=633147 {ECO:0000313|EMBL:ADK68133.1, ECO:0000313|Proteomes:UP000000333};
RN [1] {ECO:0000313|EMBL:ADK68133.1, ECO:0000313|Proteomes:UP000000333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49627 / DSM 7084 / CIP 109912 / JCM 12494 / NCIMB 702895 /
RC VPI D76D-27C {ECO:0000313|Proteomes:UP000000333};
RX PubMed=21304694; DOI=10.4056/sigs.1082860;
RA Goker M., Held B., Lucas S., Nolan M., Yasawong M., Glavina Del Rio T.,
RA Tice H., Cheng J.F., Bruce D., Detter J.C., Tapia R., Han C., Goodwin L.,
RA Pitluck S., Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Rohde M., Sikorski J., Pukall R., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of Olsenella uli type strain (VPI D76D-27C).";
RL Stand. Genomic Sci. 3:76-84(2010).
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}.
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DR EMBL; CP002106; ADK68133.1; -; Genomic_DNA.
DR RefSeq; WP_013251885.1; NZ_JQCO01000001.1.
DR AlphaFoldDB; E1QVI0; -.
DR STRING; 633147.Olsu_1022; -.
DR GeneID; 78512443; -.
DR KEGG; ols:Olsu_1022; -.
DR PATRIC; fig|633147.7.peg.523; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_11; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000000333; 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; 3.10.20.590; -; 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; 1.
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:UP000000333}.
FT DOMAIN 49..189
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 230..431
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 451..650
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 692..818
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 51..61
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 611..615
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 614
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 854 AA; 96259 MW; 434EC2C96C252912 CRC64;
MSEGKTDNSS YPAYDAEAIE TKWQRVWEDE GLYKTDEDPA KPKRYVLEMF PYPSGDLHMG
HARNYTIGDA MARQARMRGF DVLHPMGFDA FGLPAENAAI KHHTQASRWT HQNIAQTVKT
MRRMGFSYDY DRMFNTCDPE YYRWGQWMFI KMWERGLAYR ATSPVNWCPT CQTVLANEQV
VDGRCWRCGS VPEKRELSQW YLRITDYAQE LLGDLDRLDG WPENVKAQQR NWIGRSEGAE
IDFALAAEDG VTPTDRKVTV FTTRADTLFG VSFMLLPPES ALAAELVAGT QCEVAFKELR
AATEKVSSVE RQGSEREKHG VPTGRYVINP VNGRPVPIWV ADYVLMDYGT GAVMGVPCGD
QRDFDFAKKY GLEIAPIICE KDDPLYAELG DERELRIRSV DWDRAMVAEG YLVQSGEFTG
LKGGKHSEAV DAVVKWLGEH GCGRETVQFR LRDWLISRQR YWGNPIPMIH CDDCGDVPVP
EEDLPVLLPD DLDLGAGETL AEYAPFYETT CPRCGRPARR VTDTMDTFTC SSWYYLRYAD
PHNDNLPFSR EAARRWMPVD NYIGGIEHAI LHLLYSRFWT KVMRDLGMLD VDEPFTNLLC
QGMVKDEHGD TMSKSKGNVV PPSSVIEPYG ADTMRLAILF IAPPEKDFDW DPEAVAGANR
FIKRAWRVVW TLARSADRGV VLDAAALGPQ ARELNRVLHE MGLRCTSDFD RGQFNTAISA
VMELVNAASK YANEVSAERR DGALCWRVAH DIVAMLAPIC PHWAEELHHE ALGLAGSVYN
EPWPSFDAEQ AKSDTIEIAV QVKGKVRARI QVAADSSKDE LEAAAREAVS SQIEGKDVRK
VIVVPGRLVN IVAV
//
