SYL_CAMC5
ID SYL_CAMC5 Reviewed; 821 AA.
AC A7GZ81;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
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};
GN OrderedLocusNames=Ccur92_12190; ORFNames=CCV52592_0710;
OS Campylobacter curvus (strain 525.92).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360105;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=525.92;
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT "Genome sequence of Campylobacter curvus 525.92 isolated from human
RT feces.";
RL Submitted (JUL-2007) 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: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; CP000767; EAU00405.1; -; Genomic_DNA.
DR RefSeq; WP_011992459.1; NC_009715.2.
DR AlphaFoldDB; A7GZ81; -.
DR SMR; A7GZ81; -.
DR STRING; 360105.CCV52592_0710; -.
DR PRIDE; A7GZ81; -.
DR EnsemblBacteria; EAU00405; EAU00405; CCV52592_0710.
DR KEGG; ccv:CCV52592_0710; -.
DR HOGENOM; CLU_004427_0_0_7; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000006380; 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 Gene3D; 3.40.50.620; -; 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 PANTHER; PTHR43740; PTHR43740; 2.
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 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..821
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000334739"
FT MOTIF 44..54
FT /note="'HIGH' region"
FT MOTIF 589..593
FT /note="'KMSKS' region"
FT BINDING 592
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 821 AA; 93990 MW; 66AF609B342A47A3 CRC64;
MAQNSKYEAA KIEKKWQEIW HKNGEFEPKD DYTLPKKYIL SMFPYPSGRI HMGHVRNYSI
GDALARYYRK NCFNVLHPIG FDSFGMPAEN AAIKHKIHPK KWTYENIDYM KKELSSLGFS
FSDRRMLATS DPLYTKWEQS FFIKMFEKGL VYRKSAIVNW CEHDQTVLAN EQVEDGCCWR
CGNEVVQREF PGYYFKITQY AEELLNDLKT LEGKWPNQVI AMQENWIGKS SGLEFKFYLD
DASSRALGGK FDGFEVFTTR PDTIYGVSYV ALAPEHKVVR ALLSSEILDD TKKAKIKSIL
NQSPRERQAS DKDGVFLDIY MLHPLTNEPV PVWVANFILA DYGSGAIMAV PAHDQRDYEF
ASKFGLPIKQ VVMPKEGKFD TSKANAEYGI SINSPLINGL ETKQAKQAII EKFEKDGLGK
RITNYKLRDW GISRQRYWGA PIPIVHCPNC GVVPENEQNL PIALPDDVVI TGEGNPLDKH
PTWKYTKCPK CGHDAVRETD TMDTFVESSW YFARFASDEK TWQQTAFDKK SVDYWMSVDQ
YIGGIEHAIL HLLYARFFQK VLRDLGYLRD DEPFSNLLTQ GMVLKDGKKM SKSKGNVVDP
DDIINRYGAD TARLFILFAA PPQKELEWND SAVEGAYRFL NRLWDKAKTI KKSEILPAIE
HANLNKDEKY ARMKVYEALK KSNEVFNETF AFNTLIAACM EALNALNAQD NDDVNTEGFF
IILNLLEPIV PHIANELSEE LFRRKNFTKL EILEEVFVKD TINLAVTVNG KKRAEFEISA
DASEADVLQT AKASVAKWIE GKEIIKEIYI KGKLVNLVVK G
