SYL_CAUVN
ID SYL_CAUVN Reviewed; 861 AA.
AC B8GW27;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 84.
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}; OrderedLocusNames=CCNA_03865;
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N;
RX PubMed=20472802; DOI=10.1128/jb.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(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: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; CP001340; ACL97330.1; -; Genomic_DNA.
DR RefSeq; WP_010921576.1; NC_011916.1.
DR RefSeq; YP_002519238.1; NC_011916.1.
DR AlphaFoldDB; B8GW27; -.
DR SMR; B8GW27; -.
DR PRIDE; B8GW27; -.
DR EnsemblBacteria; ACL97330; ACL97330; CCNA_03865.
DR GeneID; 7332713; -.
DR KEGG; ccs:CCNA_03865; -.
DR PATRIC; fig|565050.3.peg.3770; -.
DR HOGENOM; CLU_004427_0_0_5; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR PhylomeDB; B8GW27; -.
DR Proteomes; UP000001364; 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 Gene3D; 3.90.740.10; -; 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 PANTHER; PTHR43740; PTHR43740; 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; 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..861
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000199187"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 623..627
FT /note="'KMSKS' region"
FT BINDING 626
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 861 AA; 95536 MW; C546C7C0BD7DB374 CRC64;
MARYNPKDTE PKWREAWAKA DVFKTGEIND GRPKYYVLEM FPYPSGRIHM GHVRNYAMGD
VVARYKRAQG FNVLHPMGWD AFGMPAENAA MERGVHPKGW TYDNIAAMRE QLKSLGISVD
WSREFATCDP EYYGKQQAWF LRLLKRGLVY RKEASVNWDP VDMTVLANEQ VIDGKGWRSG
AVVEKRKLTQ WFLRITDYAD ALIDGLKTLD RWPDKVRLMQ ENWIGRSKGL RFKFQFDGEA
PDGMAEGLEV YTTRPDTLFG ASFVGIAPEH PLAEQLAAAN PQIQTFIADC RKGGTSEAEI
ESAEKLGYDT GLRVKHPLDP SITLPVWIAN FILMDYGTGA IFACPAHDQR DLDFARKYDL
PVLPVVLPNG EDPATFTVGK EAYVGPGKIF NSKFLDGLDV EAAKAEAIAR IEAANQGQGA
TVYRLRDWGV SRQRYWGCPI PVIHCEACGV VPVPEDQLPV ALPDDVTFDK PGNPLLRHPT
WRHTTCPSCG GKAERETDTL DTFIDSSWYF ARFADTQAAE PVGKDAADHW LPVDQYIGGV
EHAILHLLYA RFITRALKDE GLLSVEEPFA GLFTQGMVTH EAYKNEAGEW VEPSDVVITT
EGSTRTAKHA KTGAPIIIGD IEKMSKSKKN VVAPEDIFEA YGVDSARLFV MSDSPPERDV
QWTNSGVEGS WRFTHRLWNE FDSQPAGDFA HDDSDEAALA LRKAAHKLIG FVTDSIEGFR
FNSGVARLYE FLNALKAAPA EGASQAVLAA RAEALNILAR LVAPFTPHLA EEAWARMGGE
GMVVDAPWPK ADPALAADDE RVLPIQINGK RRGEIKVKAG APDDEVTKIA LADPNVMAHL
EGLTVRKVIV VKDRIVNIVA N