SYL_HELPY
ID SYL_HELPY Reviewed; 806 AA.
AC P56457;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
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=HP_1547;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000511; AAD08585.1; -; Genomic_DNA.
DR PIR; C64713; C64713.
DR RefSeq; NP_208338.1; NC_000915.1.
DR RefSeq; WP_000345715.1; NC_018939.1.
DR AlphaFoldDB; P56457; -.
DR SMR; P56457; -.
DR DIP; DIP-3469N; -.
DR IntAct; P56457; 1.
DR MINT; P56457; -.
DR STRING; 85962.C694_08015; -.
DR PaxDb; P56457; -.
DR EnsemblBacteria; AAD08585; AAD08585; HP_1547.
DR KEGG; hpy:HP_1547; -.
DR PATRIC; fig|85962.47.peg.1662; -.
DR eggNOG; COG0495; Bacteria.
DR OMA; TFMVLAP; -.
DR PhylomeDB; P56457; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central.
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; 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; 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..806
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000152026"
FT MOTIF 38..48
FT /note="'HIGH' region"
FT MOTIF 572..576
FT /note="'KMSKS' region"
FT BINDING 575
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 806 AA; 93164 MW; 731807226C288678 CRC64;
MDFINIEKKW QEFWWKNKSF EPKDDFNLPK KYILSMLPYP SGEIHMGHVR NYTIGDALAR
YYRLHHYNVL HPMGFDSFGM PAENAAIKHG IHPKTWTYEN IENMQKEFEA LGFSFSKNRE
FATSDPDYTK FEQRFFIDLW EKGLIYRKKA MLNWCPNDKT VLANEQVIDG RCWRCDTEVI
QKELYQYYLK ITNYAEELLK DLEALEDHWP SQVLIMQKNW IGKSSGLQFG FKIADECLKA
CNGIQEIEVF TTRADTIYGV TYIAIAPEHP LVEHAIKQVS QEVSKMIKAI LNTTQRERAL
EKKGAFLGIY AIHPLTKQKI PVWVANFALA NYGSGALMGV PACDERDFEF ANLYHIPIKV
ITQSPQNLPH TKEEVLKNSG EWSDLSSSVA REQIIAYFEK ENLGKRVINY RLQDWGVSRQ
RYWGAPIPMI HCNHCGIVPE TQLPVTLPED IVIDGEGNPL EKHASWKFTQ CPKCHKNALR
ETDTMDTFIQ SSWYFLRYTT PKNQRENQAF DQNYLKYFMP VDTYIGGIEH AILHLLYARF
FTKALRDLGY LHLDEPFKQL ITQGMVLKNG AKMSKSKGNV VSPKEILKKY GADAARLFIL
FAAPPAKELE WNDSALEGAH RFIKRLYDKA NAINPTTSKP EFKEVSLNEA QKLGRKKVYE
ALKKSHEIFN KAESAYSFNT LIASCMEALN ALSAQNNERI LCEGYFVLLQ ILEPIIPHTA
WELSERLFKR ENFKPIAIDE DALMEDFMTL GLTINGKRRA ELKVNINASK EEIIVLAKKE
LEKYLENASV KKEIYVPNKL VNFVIA