ID   SYK_RHILO               Reviewed;         548 AA.
AC   Q98BC8;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Lysine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00177};
DE            EC=6.1.1.6 {ECO:0000255|HAMAP-Rule:MF_00177};
DE   AltName: Full=Lysyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00177};
DE            Short=LysRS {ECO:0000255|HAMAP-Rule:MF_00177};
GN   Name=lysS {ECO:0000255|HAMAP-Rule:MF_00177}; OrderedLocusNames=mll5634;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-
CC         tRNA(Lys); Xref=Rhea:RHEA:20792, Rhea:RHEA-COMP:9696, Rhea:RHEA-
CC         COMP:9697, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78529, ChEBI:CHEBI:456215; EC=6.1.1.6;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00177};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00177}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00177}.
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DR   EMBL; BA000012; BAB52044.1; -; Genomic_DNA.
DR   RefSeq; WP_010913382.1; NC_002678.2.
DR   AlphaFoldDB; Q98BC8; -.
DR   SMR; Q98BC8; -.
DR   STRING; 266835.14025444; -.
DR   EnsemblBacteria; BAB52044; BAB52044; BAB52044.
DR   KEGG; mlo:mll5634; -.
DR   PATRIC; fig|266835.9.peg.4475; -.
DR   eggNOG; COG1384; Bacteria.
DR   HOGENOM; CLU_025562_2_0_5; -.
DR   OMA; DWPMRWA; -.
DR   OrthoDB; 256927at2; -.
DR   Proteomes; UP000000552; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.350; -; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   HAMAP; MF_00177; Lys_tRNA_synth_class1; 1.
DR   InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR008925; aa_tRNA-synth_I_cd-bd_sf.
DR   InterPro; IPR002904; Lys-tRNA-ligase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR37940; PTHR37940; 1.
DR   Pfam; PF01921; tRNA-synt_1f; 1.
DR   SUPFAM; SSF48163; SSF48163; 1.
DR   TIGRFAMs; TIGR00467; lysS_arch; 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.
FT   CHAIN           1..548
FT                   /note="Lysine--tRNA ligase"
FT                   /id="PRO_0000152741"
FT   MOTIF           52..60
FT                   /note="'HIGH' region"
FT   MOTIF           300..304
FT                   /note="'KMSKS' region"
FT   BINDING         303
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00177"
SQ   SEQUENCE   548 AA;  61014 MW;  B5B44B8DF3D89C29 CRC64;
     MAGSNTIDLN PELLAAAAES KAWPFEEAKK IIERYKGGEF PETILFETGY GPSGLPHIGT
     FGEVARTSMV RHAFRVLTQD KVATKLLCFS DDMDGMRKIP DNVPDRAALE PHLHKPLSSV
     PNPFGGDYAS FADHNNAMLC RFLDTFGFDY EFASATQYYK SGRFDAMLLR AAERYDKIMA
     VMLPTLGPER QATYSPFLPI SPKSGRVLYV PMKHVDAKAG TITFDDEGTE TTLSITGGRV
     KLQWKPDFGM RWAALGVDFE MFGKDHQTNA VVYDRICNIL GGRAPEHFVY ELFLDENGQK
     ISKSKGNGLT IDEWLTYAPT ESLGLYMYQR PRQAKKLYFD VIPRAVDEYY TFLGAYPRQD
     WKERLGNPVW HMHDGNPPAI DMPVPFSLLL NLVSASNAQN KDVLWGFISR HTQGVTPKTH
     PELDQLVGHA IRYFDDFVRP TKTFRAADEV EREALEALDA ALGALPADAG GEAIQNASLN
     VARKIERYQD HSKQSPEGGP GVSGAFFQMI YQVLIGQERG PRFGSFAALY GVAETRALIQ
     QALAGQLA