ID K0KBZ7_SACES Unreviewed; 923 AA.
AC K0KBZ7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 67.
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 ECO:0000313|EMBL:CCH35726.1};
GN OrderedLocusNames=BN6_85120 {ECO:0000313|EMBL:CCH35726.1};
OS Saccharothrix espanaensis (strain ATCC 51144 / DSM 44229 / JCM 9112 / NBRC
OS 15066 / NRRL 15764).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1179773 {ECO:0000313|EMBL:CCH35726.1, ECO:0000313|Proteomes:UP000006281};
RN [1] {ECO:0000313|EMBL:CCH35726.1, ECO:0000313|Proteomes:UP000006281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51144 / DSM 44229 / JCM 9112 / NBRC 15066 / NRRL 15764
RC {ECO:0000313|Proteomes:UP000006281};
RX PubMed=22958348; DOI=10.1186/1471-2164-13-465;
RA Strobel T., Al-Dilaimi A., Blom J., Gessner A., Kalinowski J.,
RA Luzhetska M., Puhler A., Szczepanowski R., Bechthold A., Ruckert C.;
RT "Complete genome sequence of Saccharothrix espanaensis DSM 44229T and
RT comparison to the other completely sequenced Pseudonocardiaceae.";
RL BMC Genomics 13:465-465(2012).
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:RU363039}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00049}.
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DR EMBL; HE804045; CCH35726.1; -; Genomic_DNA.
DR RefSeq; WP_015105833.1; NC_019673.1.
DR AlphaFoldDB; K0KBZ7; -.
DR STRING; 1179773.BN6_85120; -.
DR KEGG; sesp:BN6_85120; -.
DR PATRIC; fig|1179773.3.peg.8597; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_11; -.
DR OrthoDB; 9810365at2; -.
DR BioCyc; SESP1179773:BN6_RS41250-MONOMER; -.
DR Proteomes; UP000006281; 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 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; 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; 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:UP000006281}.
FT DOMAIN 57..160
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 287..465
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 772..886
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 517..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 695..699
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 698
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 923 AA; 103766 MW; D035EA2516F31655 CRC64;
MSTDASETPA FRYTAELAGG IERRWQREWE ERGTFHAPNP VGPLRGEVPA DKLFVQDMFP
YPSGAGLHVG HPLGFIGTDV FARYHRMTGR NVLHTMGFDA FGLPAEQYAV QTGQHPRATT
EANIQTYLRQ IRRVGLGHDE RRRISTIDPG YYKWTQWIFL QIFNSWFDDE AKKARPIAEL
EARFADGTRP TPDGRPWAEL TGAQREQVLG GYRLAYLSEA PVNWCPGLGT VLANEEVTAD
GRSERGNFPV FRRSLRQWMM RITAYSDRLI DDLDRLDWPE KVKSMQRNWI GRSHGARVRF
AVGGHDIEVF TTRPDTLFGA TYVVLAPEHP LVDEIAAADR VGAIAEYRRA VARKSDLDRQ
ENKEKTGVFT GAHAVNPVTG AEIPVYVADY VLMGYGTGAI MAVPGQDQRD WDFATAFDLP
IIRTVRPPDG FEGEAYTGTG PAVNSGFLDG LDVAEAKKTI IAWLEEHDRG EGTVQFKLRD
WLFSRQRYWG EPFPIVYDEA GTPIAVPESM LPIELPDVDD YSPRTFEPDD ANSEPSPPLS
RAGEWVEVEL DLGDGPKKYR RETNTMPNWA GSCWYQLRYV DPTETERFVN AENERYWLGP
RAEHGANDPG GVDLYIGGVE HAVLHLLYSR FWQKVLFDLG HVSGDEPYRR LFNQGYIEAY
AYRDERGTPV PAEQVEERDG KYFFEGAEVK REYGKMGKSL KNVVTPDDMC DRYGVDTFRL
YEMSMGPMDV SRPWATKDVV GAQRFLQRLW RNLVDEETGA LRVTDEEPAE DALRLLHKTI
AGVHDDYANL RYNTAGAKLI ELNNFVTKHF PGGAPRALAE PMVLLLAPLC PHVAEELWAK
LGHAESLAHG PFPRAEEKFL VEDTVEYPIQ VNGKVKARVV VAASASPDEV KAAALGDPKV
AELLTGEPRK VIVVPGRLVN VVL
//
