SYL_BACP2
ID SYL_BACP2 Reviewed; 804 AA.
AC A8FGG0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 87.
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=BPUM_2669;
OS Bacillus pumilus (strain SAFR-032).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=315750;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAFR-032;
RX PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA Weinstock G.M.;
RT "Paradoxical DNA repair and peroxide resistance gene conservation in
RT Bacillus pumilus SAFR-032.";
RL PLoS ONE 2:E928-E928(2007).
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 -!- SEQUENCE CAUTION:
CC Sequence=ABV63327.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000813; ABV63327.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041815857.1; NZ_VEIS01000006.1.
DR AlphaFoldDB; A8FGG0; -.
DR SMR; A8FGG0; -.
DR STRING; 315750.BPUM_2669; -.
DR EnsemblBacteria; ABV63327; ABV63327; BPUM_2669.
DR KEGG; bpu:BPUM_2669; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_9; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000001355; 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; 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; PF08264; Anticodon_1; 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..804
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000334730"
FT MOTIF 40..51
FT /note="'HIGH' region"
FT MOTIF 576..580
FT /note="'KMSKS' region"
FT BINDING 579
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 804 AA; 91572 MW; 76385A9ECC40E579 CRC64;
MSFQHREIEK KWQDYWLTHK TFATSDSEDK PKFYALDMFP YPSGAGLHVG HPEGYTATDI
LSRMKRMQGY DVLHPMGWDA FGLPAEQYAL DTGNDPAVFT EENINNFRRQ IQSLGFSYDW
DREINTTDPN YYKWTQWIFL KLYEKGLAYI DEVPVNWCPA LGTVLANEEV IDGKSERGGH
PVERRPMKQW MLKITAYADR LLEDLEDIDW PESIKDMQRN WIGRSEGAHV HFEIEGHDEQ
FTVFTTRPDT LFGATYAVLA PEHALVEKIT TATQKEAVEA YIKEIQSKSD LERTDLAKTK
TGIFTGAYAV NPLNGEKMPI WIADYVLATY GTGAIMAVPA HDERDYEFAK TFDLPIKAVV
EGGDIEEEAY TGDGKHINSD FLDGLGKEEA IEKVIAWLEE HQKGEKKVTY RLRDWLFSRQ
RYWGEPIPII HWEDGTSSAV SEEDLPLILP KTTEIKPSGT GESPLANIKD WVEVVDPVTG
KKGRRETNTM PQWAGSCWYF LRYIDPHNSE ELASPEKLKK WLPVDVYIGG AEHAVLHLLY
ARFWHKFLYD IGVVPTKEPF MKLFNQGMIL GENNEKMSKS KGNVVNPDDI VESHGADTLR
LYEMFMGPLD ASIAWSETGL DGARRFLDRV WRLFTNEDGT ISDKVTEQTG GALERSYHET
VMKVTDHYEG LRFNTGISQL MVFINDAYKA DTLPKEYAEG FVKLLSPIAP HLAEELWNKL
GHEGSISYEA WPQYDESKLV DDEVEIVVQL NGKVKAKLTV PADATKEQLE DLAKSDARVK
EQLEGKTIRK VIAVPGKLVN IVAN
