ID   SYL_BACSU               Reviewed;         804 AA.
AC   P36430; O34465;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 3.
DT   03-AUG-2022, entry version 157.
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=BSU30320;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1317842; DOI=10.1128/jb.174.12.3928-3935.1992;
RA   Vander Horn P.B., Zahler S.A.;
RT   "Cloning and nucleotide sequence of the leucyl-tRNA synthetase gene of
RT   Bacillus subtilis.";
RL   J. Bacteriol. 174:3928-3935(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA   Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT   "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT   200 kb rrnB-dnaB region.";
RL   Microbiology 143:3431-3441(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(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}.
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DR   EMBL; M88581; AAA22571.1; -; Genomic_DNA.
DR   EMBL; AF008220; AAC00259.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15010.1; -; Genomic_DNA.
DR   PIR; D69650; D69650.
DR   RefSeq; NP_390910.1; NC_000964.3.
DR   RefSeq; WP_003246072.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P36430; -.
DR   SMR; P36430; -.
DR   IntAct; P36430; 1.
DR   MINT; P36430; -.
DR   STRING; 224308.BSU30320; -.
DR   jPOST; P36430; -.
DR   PaxDb; P36430; -.
DR   PRIDE; P36430; -.
DR   EnsemblBacteria; CAB15010; CAB15010; BSU_30320.
DR   GeneID; 938102; -.
DR   KEGG; bsu:BSU30320; -.
DR   PATRIC; fig|224308.179.peg.3288; -.
DR   eggNOG; COG0495; Bacteria.
DR   InParanoid; P36430; -.
DR   OMA; TFMVLAP; -.
DR   PhylomeDB; P36430; -.
DR   BioCyc; BSUB:BSU30320-MON; -.
DR   Proteomes; UP000001570; 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   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; 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_0000151973"
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"
FT   CONFLICT        186
FT                   /note="P -> L (in Ref. 1; AAA22571)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        195
FT                   /note="T -> N (in Ref. 1; AAA22571)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        247..281
FT                   /note="RPDTLFGATYTVLAPEHALVENITTAEQKEAVEAY -> DQIRCLALHTLSL
FT                   PRNTHWWKTSQRQSKKKLLKLI (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   804 AA;  91543 MW;  306FD5A98FE5C47E CRC64;
     MSFQHKEIEK KWQTYWLENK TFATLDNNEK QKFYALDMFP YPSGAGLHVG HPEGYTATDI
     LSRMKRMQGY DVLHPMGWDA FGLPAEQYAL DTGNDPAVFT KQNIDNFRRQ IQALGFSYDW
     DREINTTDPE YYKWTQWIFL KLYEKGLAYV DEVPVNWCPA LGTVLANEEV IDGKSERGGH
     PVERRPMKQW MLKITAYADR LLEDLEELDW PESIKDMQRN WIGRSEGAHV HFAIDGHDDS
     FTVFTTRPDT LFGATYTVLA PEHALVENIT TAEQKEAVEA YIKEIQSKSD LERTDLAKTK
     TGVFTGAYAI NPVNGEKLPI WIADYVLASY GTGAVMAVPG HDERDFEFAK TFGLPVKEVV
     KGGNVEEAAY TGDGEHVNSD FLNGLHKQEA IEKVIAWLEE TKNGEKKVTY RLRDWLFSRQ
     RYWGEPIPVI HWEDGTSTAV PEEELPLILP KTDEIKPSGT GESPLANIKE WVEVTDPETG
     KKGRRETNTM PQWAGSCWYF LRYIDPHNPD QLASPEKLEK WLPVDMYIGG AEHAVLHLLY
     ARFWHKFLYD IGVVPTKEPF QKLYNQGMIL GENNEKMSKS KGNVVNPDEI VASHGADTLR
     LYEMFMGPLD ASIAWSESGL DGARRFLDRV WRLFIEDSGE LNGKIVEGAG ETLERVYHET
     VMKVTDHYEG LRFNTGISQL MVFINEAYKA TELPKEYMEG FVKLLSPVAP HLAEELWEKL
     GHSGTIAYEA WPVYDETKLV DDEVEIVVQL NGKVKAKLQV PADATKEQLE QLAQADEKVK
     EQLEGKTIRK IIAVPGKLVN IVAN