SYL_RICPR
ID SYL_RICPR Reviewed; 828 AA.
AC Q9ZDB1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=RP421;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
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; AJ235271; CAA14878.1; -; Genomic_DNA.
DR PIR; D71700; D71700.
DR RefSeq; NP_220802.1; NC_000963.1.
DR RefSeq; WP_004599464.1; NC_000963.1.
DR AlphaFoldDB; Q9ZDB1; -.
DR SMR; Q9ZDB1; -.
DR STRING; 272947.RP421; -.
DR EnsemblBacteria; CAA14878; CAA14878; CAA14878.
DR GeneID; 57569546; -.
DR KEGG; rpr:RP421; -.
DR PATRIC; fig|272947.5.peg.434; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_5; -.
DR OMA; TFMVLAP; -.
DR Proteomes; UP000002480; 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; Reference proteome.
FT CHAIN 1..828
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000152075"
FT MOTIF 36..46
FT /note="'HIGH' region"
FT MOTIF 595..599
FT /note="'KMSKS' region"
FT BINDING 598
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 828 AA; 96472 MW; 43BACB6398191986 CRC64;
MHKIEKKWQK IWQEEKAFQV SNESSKPKYY VLEMLPYPSG KIHIGHVRNY SIGDVIARFM
TMQGFNVLHP MGWDAFGLPA ENAAIKNNSR PQDWTYSNIE YMKKQLQSMG FAYDWTREIN
SCDPEYYKHE QKFFLELYDR NLVYQKESLV NWDPVDNTVL ANEQVVDGRG WRSGAIIEKR
YLKQWFLKIT DYAEELLNEI QNLKDWPAAV RVMQEEWIGK STGVNFHFKV KYHENTTIEV
FSTKPETIFG ASFIGIAFNH PIIEQLICKT PEIVNFITKC SYITRSSEID KAEKEGIFSG
LYVIHPFDAN IFLPVIITNF VLMDYGTGAI FGCPAHDKRD HELAIKMNLP IKQVIETGNI
QEGILINSDW LNGLTSSEAK QKVIEKFEKL GIGKRSVNYR LKDWSISRQR FWGCPIPMIH
CKTCGVVPVP YKDLPVTLPD DVSFDSNYNP LEHHSSWKYV NCPKCDNSAI RETDTFDTFF
ESSWYFTRYC NSNAVEMTDK KACNYWLPVD KYIGGIEHAV MHLLYARFFT KLMNEHNYVS
IREPFKGLFT QGMVLHATYK DENNNWLYPA EVVKKGNEFF HKENNTRVVQ GRIEKMSKSK
KNIIDLETIR EQYSADAIRL FVLSDSPPEK DLEWSASGIE GCSRFINKLE NMFEAIFSLK
DDMKSEINKD LNRLIHLTIK HVADDIKTFS LNRAIARMRT LTNAIYYEIS KDRIDVRTIK
YGFNVLVQLL NPFIPHITEE IWQKLGNKER LYKSVFAEFD ESILELSTYI MAVQVNGKLR
DTYEFDVDIS EDEVKQITVN LPKVQKFLAG KEPRNIILVP RKIVNIIV