SYL_PROMH
ID SYL_PROMH Reviewed; 860 AA.
AC B4EV14;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=PMI0433;
OS Proteus mirabilis (strain HI4320).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=529507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI4320;
RX PubMed=18375554; DOI=10.1128/jb.01981-07;
RA Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA Parkhill J., Mobley H.L.T.;
RT "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT both adherence and motility.";
RL J. Bacteriol. 190:4027-4037(2008).
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; AM942759; CAR41076.1; -; Genomic_DNA.
DR RefSeq; WP_004247439.1; NC_010554.1.
DR AlphaFoldDB; B4EV14; -.
DR SMR; B4EV14; -.
DR STRING; 529507.PMI0433; -.
DR PRIDE; B4EV14; -.
DR EnsemblBacteria; CAR41076; CAR41076; PMI0433.
DR GeneID; 6802424; -.
DR KEGG; pmr:PMI0433; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_6; -.
DR OMA; TFMVLAP; -.
DR Proteomes; UP000008319; 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 Gene3D; 3.90.740.10; -; 1.
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..860
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000091346"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 619..623
FT /note="'KMSKS' region"
FT BINDING 622
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 860 AA; 97782 MW; 0A1F73948C0830A9 CRC64;
MQEQYRPEDI EQTIQEHWEK NNTFKVTEDN NKEKYYCLSM LPYPSGRLHM GHVRNYTIGD
VISRYQRMLG KNVLQPIGWD AFGLPAEGAA VKNNTAPAPW TYENINYMKG QLKKLGFGYD
WDREVTTCTP EYYRWEQWFF TKLYEKGLVY KKTSAVNWCP HDLTVLANEQ VIDGCCWRCD
TPVERKEIPQ WFIKITDYAE ELLNDLDTLD EWPEQVKTMQ RNWIGRSEGV EITFDVADSD
DTMTVYTTRP DTFMGVTYVA VAAGHPLAQK AAQNNPEIQH FIDECRNMKM AEAEMATMEK
KGIATGLYAI HPLTQEKVAI WVANFVLMEY GTGAVMAVPG HDERDWEFAT KYGLPIKAVI
ADAEGNQPDL STGALTEKNS LINSGEFSGL DNQAGFNAIA DKLTAMGVGE RKVNYRLRDW
GVSRQRYWGA PIPMATLEDG SVVPVPDDQL PVILPEDVKM DGITSPIKAD PEWAKTTING
QPALRETDTF DTFMESSWYY ARYTCPDYDK GMLDPKAANY WLPVDWYIGG IEHAIMHLMY
FRFFHKLMRD AGLVNSDEPA KRLLCQGMVL ADAFYYTGED GARHWVSPAE AIVERDEKNR
IIKATDSAGH ELTYAGMSKM SKSKNNGIDP QTMVERYGAD TVRLFMMFAA PPELTLEWQE
SSVEGANRFL RRLWRLVHEH TEKGTTQSLD LATLTTEQKD LRRDLHKTIA KVSDDVGRRL
AFNTAIAAIM ELMNKLTRAP QETEQDRALM QEALEAVVRM LSPIIPHACF VMWQALGGKE
DIDVAPWPVA DEEAMVDDTK LIIVQVNGKV RGRITVPANS EKDYVQEMAT KEYSVAKYLE
NVTVRKVIYV PGKLLNIVVG