ID B5Z9H8_HELPG Unreviewed; 806 AA.
AC B5Z9H8;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=Leucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00049};
DE EC=6.1.1.4 {ECO:0000256|HAMAP-Rule:MF_00049};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00049};
DE Short=LeuRS {ECO:0000256|HAMAP-Rule:MF_00049};
GN Name=leuS {ECO:0000256|HAMAP-Rule:MF_00049};
GN OrderedLocusNames=HPG27_1485 {ECO:0000313|EMBL:ACI28227.1};
OS Helicobacter pylori (strain G27).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=563041 {ECO:0000313|EMBL:ACI28227.1, ECO:0000313|Proteomes:UP000001735};
RN [1] {ECO:0000313|EMBL:ACI28227.1, ECO:0000313|Proteomes:UP000001735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G27 {ECO:0000313|EMBL:ACI28227.1,
RC ECO:0000313|Proteomes:UP000001735};
RX PubMed=18952803; DOI=10.1128/JB.01416-08;
RA Baltrus D.A., Amieva M.R., Covacci A., Lowe T.M., Merrell D.S.,
RA Ottemann K.M., Stein M., Salama N.R., Guillemin K.;
RT "The complete genome sequence of Helicobacter pylori strain G27.";
RL J. Bacteriol. 191:447-448(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:0000256|ARBA:ARBA00001372, ECO:0000256|HAMAP-
CC Rule:MF_00049};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00049}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00049,
CC ECO:0000256|RuleBase:RU363035}.
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DR EMBL; CP001173; ACI28227.1; -; Genomic_DNA.
DR RefSeq; WP_000345650.1; NC_011333.1.
DR AlphaFoldDB; B5Z9H8; -.
DR KEGG; hpg:HPG27_1485; -.
DR HOGENOM; CLU_004427_0_0_7; -.
DR Proteomes; UP000001735; 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 CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 3.10.20.590; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 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 NCBIfam; TIGR00396; leuS_bact; 1.
DR PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00049};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00049};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00049};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00049};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00049};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00049}.
FT DOMAIN 32..178
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 218..398
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 412..611
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT MOTIF 38..48
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 572..576
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 575
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 806 AA; 93011 MW; 49C9DAFB604A6CEA CRC64;
MDFINIEKKW QEFWWKNKSF EPKDDFNLPK KYILSMLPYP SGEIHMGHVR NYTIGDALAR
YYRLHHYNVL HPMGFDSFGM PAENAAIKHG IHPKTWTYEN IEAMQKEFEA LGFSFSKNRE
FATSDPDYTK FEQQFFIDLW EKGLIYRKKA MLNWCPNDKT VLANEQVIDG RCWRCDTEVI
QKELYQYYLK ITNYAEELLK DLETLENHWP SQVLIMQKNW IGKSSGLQFG FKIADECLKA
CNGIQEIEVF TTRADTIYGV TYIAIAPEHP LVEHAIKRVS QEDSKIIKAI LNTTQRERAL
EKKGAFLGVY AIHPLTKQKI PVWVANFALA NYGSGALMGV PACDERDFEF ANLYHIPIKV
ITQSPQNLPH TKEEVLKNSG EWSDLSSSVA REKIIAYFEK ENLGKRVINY RLQDWGVSRQ
RYWGAPIPMI HCKHCGIVPE TQLPVTLPED IVIDGEGNPL EKHASWKFAQ CPKCHKDALR
ETDTMDTFIQ SSWYFLRYTT PKNQRENQAF DQNYLKYFMP VDTYIGGIEH AILHLLYARF
FTKALRDLGY IHLDEPFKQL ITQGMVLKNG TKMSKSKGNV VSPKEILKKY GADAARLFIL
FAAPPAKELE WNDSALEGAH RFIKRLYDKA NAITPTTSKP EFKGVSLNEA QKLARKKVYE
ALKKSHEIFN KAESAYAFNT LIASCMEALN ALNAQNNERI LCEGYFVLLQ ILEPIIPHTA
WELSERLFKR ENFKPIAIDE SALIEESMTL GLTINGKRRA ELKVNINASK EEIIVLAKKE
LEKYLEKASV KKEIYVPNKL VNFVIA
//
