SYL_BRAHW
ID SYL_BRAHW Reviewed; 853 AA.
AC C0QWR3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=BHWA1_02260;
OS Brachyspira hyodysenteriae (strain ATCC 49526 / WA1).
OC Bacteria; Spirochaetes; Brachyspirales; Brachyspiraceae; Brachyspira.
OX NCBI_TaxID=565034;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49526 / WA1;
RX PubMed=19262690; DOI=10.1371/journal.pone.0004641;
RA Bellgard M.I., Wanchanthuek P., La T., Ryan K., Moolhuijzen P.,
RA Albertyn Z., Shaban B., Motro Y., Dunn D.S., Schibeci D., Hunter A.,
RA Barrero R., Phillips N.D., Hampson D.J.;
RT "Genome sequence of the pathogenic intestinal spirochete Brachyspira
RT hyodysenteriae reveals adaptations to its lifestyle in the porcine large
RT intestine.";
RL PLoS ONE 4:E4641-E4641(2009).
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; CP001357; ACN84716.1; -; Genomic_DNA.
DR RefSeq; WP_012671748.1; NC_012225.1.
DR AlphaFoldDB; C0QWR3; -.
DR SMR; C0QWR3; -.
DR STRING; 565034.BHWA1_02260; -.
DR EnsemblBacteria; ACN84716; ACN84716; BHWA1_02260.
DR KEGG; bhy:BHWA1_02260; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_12; -.
DR OMA; TFMVLAP; -.
DR Proteomes; UP000001803; 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; 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.
FT CHAIN 1..853
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000199183"
FT MOTIF 40..50
FT /note="'HIGH' region"
FT MOTIF 609..613
FT /note="'KMSKS' region"
FT BINDING 612
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 853 AA; 98617 MW; DB3FF4804951FD5C CRC64;
MEYNFTTIEK KWQKFWKDNQ SFKTVSKPTD KKYYVLEMFP YPSGKMHMGH VSNYTIADSI
ARYYKLLGYD ILHPMGWDAF GMPAENAAIE HKTHPAEWTL KNIANMKDQL NLLGYSYDWD
REVTTCLPDY YKWGQWFILK MYEKGLLYRK GGDVNWCDHC NTVLANEQVT PEGTCWRCDG
EVTKKKLEQW YIKVTDYAEQ LDADLKLLEG YWPDNVIAMQ KNWIGRSVGA YINFNLDDGK
AFPIFTTRPD TIYGVTYMAI AWNYDGLLDM CTTEQKSAVE EFIKKSAKID QKTDYEKEGV
FTGRYVVNPF NGEKAPLYAA NFVLAEYGSG AVMAVPAHDQ RDFEFAKKYN IPVKVVIQNA
DNSLKAENMT EAYTEDGTVV NSDILNGLSS RDAIKRAIEY ATEKGFGKEK VQYKLRDWLI
SRQRYWGNPL PFVHCEKCGV VPVPESELPI TLPMDIEFTV GDNPLKKSES FVNTTCPKCG
GKARRETDTM DTFTCSSWYY ARYTDAHNNQ MPFDPSAANA WLGVDQYIGG IEHACMHLLY
SRFWYKFMRD IGLVKGDEPF NRLLTQGMVL ANSYESRELK KFYTQEQMNN KEYEKDGIKK
EDIIVKMEKM SKSKANGIDP AEIIELFGAD AVRIFVMFVA PPEKDKEWSD EGVKGSSRFL
NRIWNLFLKY KDEEAFKNGK SFDYNNLSKE GQKLFRKYNK TIKKVTIDIK DRFHFNTAIA
ALMELLNDMS VIKLANNDDY AMFKEVIRGY LILLNPIAPH MTEELYQILN FGKMILEERW
VEHDEQYCKD DTFELVFQVN GKIRDRVEAD VNISEDDAKA QALASEKVKA FTDGKNIVKV
VYVKGKLVNI VVK
