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Database: UniProt
Entry: H6L957_SAPGL
LinkDB: H6L957_SAPGL
Original site: H6L957_SAPGL 
ID   H6L957_SAPGL            Unreviewed;       545 AA.
AC   H6L957;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 69.
DE   RecName: Full=Lysine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00252};
DE            EC=6.1.1.6 {ECO:0000256|HAMAP-Rule:MF_00252};
DE   AltName: Full=Lysyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00252};
DE            Short=LysRS {ECO:0000256|HAMAP-Rule:MF_00252};
GN   Name=lysS {ECO:0000256|HAMAP-Rule:MF_00252,
GN   ECO:0000313|EMBL:AFC24229.1};
GN   OrderedLocusNames=SGRA_1494 {ECO:0000313|EMBL:AFC24229.1};
OS   Saprospira grandis (strain Lewin).
OC   Bacteria; Bacteroidota; Saprospiria; Saprospirales; Saprospiraceae;
OC   Saprospira.
OX   NCBI_TaxID=984262 {ECO:0000313|EMBL:AFC24229.1, ECO:0000313|Proteomes:UP000007519};
RN   [1] {ECO:0000313|EMBL:AFC24229.1, ECO:0000313|Proteomes:UP000007519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lewin {ECO:0000313|EMBL:AFC24229.1,
RC   ECO:0000313|Proteomes:UP000007519};
RX   PubMed=22675601; DOI=10.4056/sigs.2445005;
RA   Saw J.H., Yuryev A., Kanbe M., Hou S., Young A.G., Aizawa S., Alam M.;
RT   "Complete genome sequencing and analysis of Saprospira grandis str. Lewin,
RT   a predatory marine bacterium.";
RL   Stand. Genomic Sci. 6:84-93(2012).
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:0000256|ARBA:ARBA00000204, ECO:0000256|HAMAP-
CC         Rule:MF_00252, ECO:0000256|RuleBase:RU000336};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00252,
CC         ECO:0000256|RuleBase:RU000336};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000256|HAMAP-Rule:MF_00252,
CC       ECO:0000256|RuleBase:RU000336};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00252}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00252}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00252}.
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DR   EMBL; CP002831; AFC24229.1; -; Genomic_DNA.
DR   RefSeq; WP_015691865.1; NC_016940.1.
DR   AlphaFoldDB; H6L957; -.
DR   STRING; 984262.SGRA_1494; -.
DR   KEGG; sgn:SGRA_1494; -.
DR   eggNOG; COG1190; Bacteria.
DR   HOGENOM; CLU_008255_6_0_10; -.
DR   OMA; EIFGEKC; -.
DR   OrthoDB; 9801152at2; -.
DR   Proteomes; UP000007519; 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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00775; LysRS_core; 1.
DR   CDD; cd04322; LysRS_N; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   HAMAP; MF_00252; Lys_tRNA_synth_class2; 1.
DR   InterPro; IPR004364; Aa-tRNA-synt_II.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR002313; Lys-tRNA-ligase_II.
DR   InterPro; IPR044136; Lys-tRNA-ligase_II_N.
DR   InterPro; IPR018149; Lys-tRNA-synth_II_C.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   NCBIfam; TIGR00499; lysS_bact; 1.
DR   PANTHER; PTHR42918:SF15; LYSINE--TRNA LIGASE, CHLOROPLASTIC/MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42918; LYSYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   PRINTS; PR00982; TRNASYNTHLYS.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00252};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00252}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00252};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00252};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00252, ECO:0000256|RuleBase:RU000336};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00252};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00252}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00252};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007519}.
FT   DOMAIN          209..530
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   BINDING         446
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00252"
FT   BINDING         453
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00252"
FT   BINDING         453
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00252"
SQ   SEQUENCE   545 AA;  62995 MW;  C1E5448BC0579256 CRC64;
     MALTEQASQA WLEELDQLLE AGQLGGRKLN EMERQRITNL RKMVELKINP YPAEAFEVSH
     LAKEVSENFS EEKAEDFKKV RLSGRLMSKR VMGKASFAEL QDSSGRIQFY ISRDEVCPED
     NKDLYNKVFK KLLDIGDYVG IEGYAFYTKT GTLSIHVEEF TFLGKAIRNL PIVKTDNEGN
     VHDAFTDAEQ RYRMRYVDLT VNPQYKEIFL TRSKVVREMR HFFDAQGWLE VETPILQAVH
     GGAAARPFET HHNTLDEDLY LRIANELYLK RLIVAGFDGV YEIGKMFRNE GMDRTHNPEF
     TSMEIYVAYK DYIWMMQMVE QLFEKICLAV HGSSSIKIRK QHGKEFTTHE VNFAGPFEKL
     SIYDAIEKHS GHNLRNMSET EIFALCKELH IDVDASMGRA KLIDEVFGET TEPHLIQPTF
     ITDYPIEMTP LAKKHRSEEG LVERFELFVM GKEIANAYTE LNDPIDQRRR FEDQLRLAER
     GDEEAMAMDE DFLRALEYGM PPCSGLGIGI DRLVMLMTDQ TSIQEVLFFP QMRAIKKKTE
     GQEEA
//
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