ID B1VTB8_STRGG Unreviewed; 590 AA.
AC B1VTB8;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=Lysine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00177};
DE EC=6.1.1.6 {ECO:0000256|HAMAP-Rule:MF_00177};
DE AltName: Full=Lysyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00177};
DE Short=LysRS {ECO:0000256|HAMAP-Rule:MF_00177};
GN Name=lysS {ECO:0000256|HAMAP-Rule:MF_00177,
GN ECO:0000313|EMBL:BAG21008.1};
GN OrderedLocusNames=SGR_4179 {ECO:0000313|EMBL:BAG21008.1};
OS Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG21008.1, ECO:0000313|Proteomes:UP000001685};
RN [1] {ECO:0000313|EMBL:BAG21008.1, ECO:0000313|Proteomes:UP000001685}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 4626 / NBRC 13350 {ECO:0000313|Proteomes:UP000001685};
RX PubMed=18375553; DOI=10.1128/JB.00204-08;
RA Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA Yamashita A., Hattori M., Horinouchi S.;
RT "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT griseus IFO 13350.";
RL J. Bacteriol. 190:4050-4060(2008).
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_00177};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00177}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00177}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00177}.
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DR EMBL; AP009493; BAG21008.1; -; Genomic_DNA.
DR RefSeq; WP_012380410.1; NC_010572.1.
DR AlphaFoldDB; B1VTB8; -.
DR GeneID; 6211456; -.
DR KEGG; sgr:SGR_4179; -.
DR PATRIC; fig|455632.4.peg.4256; -.
DR eggNOG; COG1384; Bacteria.
DR HOGENOM; CLU_025562_0_0_11; -.
DR Proteomes; UP000001685; 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; HUPs; 2.
DR Gene3D; 6.10.20.10; Lysine tRNA ligase, stem contact fold domain; 1.
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; IPR042078; Lys-tRNA-ligase_SC_fold.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR00467; lysS_arch; 1.
DR PANTHER; PTHR37940; LYSINE--TRNA LIGASE; 1.
DR PANTHER; PTHR37940:SF1; LYSINE--TRNA LIGASE; 1.
DR Pfam; PF01921; tRNA-synt_1f; 1.
DR SUPFAM; SSF48163; An anticodon-binding domain of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00177};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00177};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00177};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00177};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00177};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00177}.
FT REGION 178..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 44..52
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT MOTIF 338..342
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
SQ SEQUENCE 590 AA; 64486 MW; 12D99FB5FFF12D26 CRC64;
MPTVAESQTS TETDWVSRFA DDVIAESERR APGKPVVVAS GLSPSGPIHL GNLREVMTPH
LVADEIRRRG HTVRHLISWD DYDRYRKVPE GIPGVDKATW TEHIGKPLTS VPAPAGSPYA
NWAEHFKAAM TAALDELGVE YDGISQTEQY TAGAYREQIL HAMKHRADID AVLDRYRTKK
DPAGGPQGKG GKKPQQQKKV DEAELEAAEG SGAAAEDDGS GNSAGYFPYK PYCGNCEKDL
TVVTSYDDDT TELNYTCSAC GFAETVRLSE FNRGKLVWKV DWPMRWAYEG VIFEPSGVDH
SSPGSSFVVG GQIVREVFDG VQPIGPMYAF VGISGMAKMS SSKGGVPTPA DALEIMEAPL
LRWLYARRKP NQSFKIAFDQ EIQRLYDEWD SLGRKVADGT VLPADAAAYS RAVRTAAGEL
PSTPRPLPYR TLASVADITA GAEDQTLRIL GELDPANPLT SLDEARPRLD RAENWITTQV
PAEARTIVRD EPDKELLGSL DDQGRESLRL LLEGLDTHWS LDGLTTLVYG VPKVLAGLEP
DAKPTPELKA AQRSFFALLY RLLVSRDTGP RLPTLLLAVG ADRVRRLLGA
//
