ID   SYL_RHORT               Reviewed;         862 AA.
AC   Q2RN70;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 113.
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=Rru_A3631;
OS   Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS   NCIMB 8255 / S1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=269796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX   PubMed=21886856; DOI=10.4056/sigs.1804360;
RA   Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA   Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA   Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y.,
RA   Roberts G.P., Reslewic S., Schwartz D.C.;
RT   "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL   Stand. Genomic Sci. 4:293-302(2011).
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; CP000230; ABC24425.1; -; Genomic_DNA.
DR   RefSeq; WP_011391378.1; NC_007643.1.
DR   RefSeq; YP_428712.1; NC_007643.1.
DR   AlphaFoldDB; Q2RN70; -.
DR   SMR; Q2RN70; -.
DR   STRING; 269796.Rru_A3631; -.
DR   EnsemblBacteria; ABC24425; ABC24425; Rru_A3631.
DR   KEGG; rru:Rru_A3631; -.
DR   PATRIC; fig|269796.9.peg.3752; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   PhylomeDB; Q2RN70; -.
DR   Proteomes; UP000001929; 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..862
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334805"
FT   MOTIF           44..54
FT                   /note="'HIGH' region"
FT   MOTIF           622..626
FT                   /note="'KMSKS' region"
FT   BINDING         625
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   862 AA;  95530 MW;  9D92FEB9305F579A CRC64;
     MASEDRYNVK ETEAKWQTAW AEGGCFTARE DRTRPKYYVL EMFPYPSGRI HMGHVRNYTL
     GDVVARFKRA QGFNVLHPMG WDAFGLPAEN AAIQRGVHPA TWTRQNIAIM REQFKPMGLS
     IDWSREVSTC EPAYYRHEQK MFLDFLKAGL AYRRESWVNW DPVEHTVLAN EQVIDGKGWR
     SGAPVERRKL SQWFLRITRY AEDLLAAIGD LDRWPDKVRL MQTNWIGRSE GARVRFGLVG
     RDQALEVYTT RPDTLFGASF CAISANHPLA AEIAATNPDL AAFIAECGRM GTSEVEIETA
     EKKGFDTGLK VRHPFDPAWE LPVYVANFVL MEYGTGAIFG CPAHDQRDMD FARKYGLPVR
     AVVAPAGVDA EAFAKDLEAS DTAFSEDGVA IASGFLDGLP VSEAKARAIA HIAELGAGEG
     VVQFRLRDWG VSRQRYWGCP IPIIHCDDCG PVPVPEDQLP VLLPEDVTFD KPGNPLDHHP
     TWKHVACPQC GKPARRETDT FDTFFESSWY FARFCAPHDT DRAFEREAVD YWLPVDQYVG
     GVEHAVLHLL YSRFFTRALR DCGYLGVSEP FTGLFTQGMI CHETYRDTDG AWLSPDQIDK
     AADGTATLLS DGSPVSVGRS EKMSKSKMNT VDPTAILESY GADAARLFML SDSPPDRDMD
     WTDSGIEGAW RYIGRLWRMA LQPQIDPGAV GAPLPADLGP GAAALVRHVH KAVAGVTDDL
     EKFRFNAAVA RLRELTNAIA ALDGKEAGAG AVYRFALETA ARLAAPMIPH IAEEMWSHLG
     RDGLLAETPW PTWDPLMLID DQVTIAVQVN GKMRGTVDLP KDAKREDAEA AALALPTVLA
     QLAGAAPRKV IVVPNRIINV VV