SYL_BARHE
ID SYL_BARHE Reviewed; 880 AA.
AC Q6G1W2;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=BH15390;
OS Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
OS (Rochalimaea henselae).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=283166;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA La Scola B., Holmberg M., Andersson S.G.E.;
RT "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT of the zoonotic agent Bartonella henselae.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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; BX897699; CAF28302.1; -; Genomic_DNA.
DR RefSeq; WP_011181305.1; NZ_LRIJ02000001.1.
DR AlphaFoldDB; Q6G1W2; -.
DR SMR; Q6G1W2; -.
DR STRING; 283166.BH15390; -.
DR PaxDb; Q6G1W2; -.
DR PRIDE; Q6G1W2; -.
DR EnsemblBacteria; CAF28302; CAF28302; BH15390.
DR KEGG; bhe:BH15390; -.
DR eggNOG; COG0495; Bacteria.
DR OMA; TFMVLAP; -.
DR Proteomes; UP000000421; 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; 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; 3.
DR Pfam; PF13603; tRNA-synt_1_2; 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..880
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000151975"
FT MOTIF 49..59
FT /note="'HIGH' region"
FT MOTIF 638..642
FT /note="'KMSKS' region"
FT BINDING 641
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 880 AA; 100077 MW; 5589AC710AB5F1B8 CRC64;
MTIEHYNLGE RYNPRACERK WQAIWDEKKT FQTVQEDRRE KYYVLEMFPY PSGRIHMGHV
RNYAMGDVVA RYKRAKGFNV LHPMGWDAFG MPAENAAMQN KVHPKTWTYQ NIAVMRGQLK
QLGLSVDWSR EFATCDVDYY HRQQMLFLDF YQKGLVARKV AKVNWDPVDQ TVLANEQVVD
GRGWRSGALV EQRELTQWFF KISDFSEDLL AGLEELEQWP EKVRIMQKNW IGKSQGLLIR
WALKSTEEAD EVCKSFDEVV CYSTRPDTLF GASFLALSVD HPLAQALAQK DKALEFFIEN
CRSGGTTTAE LETAEKQGFR TSLVAVHPFD VAVHIPVYIA NFVLMDYGTG AVFGCPAHDQ
RDFDFARKYD LPVQPVVLPS GVEREDFAIT ETPYLGDGVM INSSFLDGLT PQQAFEEAAK
RLEGQMLNGK PQAEKTVQFR LRDWGISRQR YWGCPIPMIH CTSCGVVPVP RADLPVVLPD
DVTFEQPGNP LVCHETWKSV ACPVCGQFAK RETDTMDTFV DSSWYYARFT APFAQEPVDK
KATTEWLPVQ QYIGGIEHAI LHLLYARFFT RAMKSMGYVT VDEPFKGLFT QGMVVHETYR
DEKDWVSPEE ISIVEKDGKR QAYKLTDQSE VTIGSIEKMS KSKKNVVDPD DIIASYGADT
VRWFILSDSP PERDVIWTES GVEGAHRFVQ RVWRCVALSA PVLRDVVPCV GKQGAALQLS
KVAHRTLYAV EDDLEKFAFN RAIARLYEFL NIMAPLLNRI ENVEDEMKAA LRQAMDFFLA
MIAPIMPHLA EECHAALGEK TLISELAWPV CDRALTVEEC YTLPVQINGK KRGEVTVAAT
ASEAMIEEAV LALDFVKVHL VKKPVKKMII VPKRIVNVVL