ID   SYL_RHOCS               Reviewed;         865 AA.
AC   B6IU54;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=RC1_2551;
OS   Rhodospirillum centenum (strain ATCC 51521 / SW).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=414684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51521 / SW;
RA   Touchman J.W., Bauer C., Blankenship R.E.;
RT   "Genome sequence of Rhodospirillum centenum.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000613; ACI99931.1; -; Genomic_DNA.
DR   RefSeq; WP_012567713.1; NC_011420.2.
DR   AlphaFoldDB; B6IU54; -.
DR   SMR; B6IU54; -.
DR   STRING; 414684.RC1_2551; -.
DR   EnsemblBacteria; ACI99931; ACI99931; RC1_2551.
DR   KEGG; rce:RC1_2551; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001591; 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; 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; 2.
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..865
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091352"
FT   MOTIF           41..51
FT                   /note="'HIGH' region"
FT   MOTIF           614..618
FT                   /note="'KMSKS' region"
FT   BINDING         617
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   865 AA;  95609 MW;  E06C81181326B1AF CRC64;
     MSRYNVRETE AKWQAAWADA GSFAVTADPA KPKYYVLEMF PYPSGRIHMG HVRNYTMGDV
     VARFKRAKGF NVLHPMGWDA FGLPAENAAL EKGVHPGKWT YENIATMRGQ LQTMGLAIDW
     SREVATCRPE YYRHEQKIFL DFLKAGLAYR KESWVNWDPV DNTVLANEQV VDGRGWRTGA
     LVEKRKLSQW FLKITHFADD LLEALKGLER WPDKVRTMQE NWIGRSTGCR FFFRMSDGHP
     DLEVFTTRPD TLYGASFVAI SPNHPLAATL AAGNPALADF IAECNRTSTS EADIETAEKK
     GFATGVTAEH PFVPGWTLPV YVANFVLMEY GTGAIFGCPA HDQRDLDFAR KYGLPVKPVV
     IPEGQDPAAF AVADEAYTGP GVLRNSDFLD GLGVEEAKAA AIRRIEEAGR GQGTTMYRLR
     DWGVSRQRYW GCPIPVIHCP KCGAVPVPEA QLPVTLPDDV TFDAPGNPLA RHPTWKHVAC
     PCCGGAAERE TDTFDTFIES SWYFLRFADP RNGTLAFDPE LVKYWLPVDQ YIGGVEHAVL
     HLLYARFWTR ALAHCGYLDL AEPFAGLFTQ GMVTHATYQG TDGKWLFPAE VEFREGAMVK
     SDDGTAVTVG PIIKMSKSKK NVVDPQQIIE SYGADAARLF MMSDSPPDRD LEWTTAGIDG
     AWRYINRLWR LVTEPGFDLP APGTPAPASF GEEATAIRRL AHKAAQQIGE DIEGFRFNSS
     VARLRSFSNG VQDAFAKLAA KAAAGTAPAA DEAWAAREAL EMLARMVEPM MPHLAHEMWV
     ELGHAGLLLD RPWPAVDAAL VVEDTVTVAV QVNGKLRATI NLRRDAGNEE AQAAALADPA
     VQKAVEGKPL RKVVVVPNRI VNVVV